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The Serpin Database Back |
Below are listed 219 sequences which were gathered
by searching the Entrez
database using 'serpin'as a keyword.
2160141 --------------------------------------------------- Protein Description: Strong similarity to 2160141: 1..559 Triticum aestivum serpin (gb|Z49890).. NCBI Seq ID: 2160141 Updated May 29, 1997 Created Mar 24, 1997 Citation Data Submission: Athanasios Theologis (1997). Citation S. Theologis (1997). The sequence of BAC F19K23 from Arabidopsis thaliana chromosome 1. Unpublished Citation Data Submission: Athanasios Theologis (1997). Citation Data Submission: Athanasios Theologis (1997). Citation Data Submission: Athanasios Theologis (1997). Coding region 2160132: 34178..34282 2160132: 34354..34777 2160132: 35527..35960 2160132: 36247..36963 Sequence 559 aa 1 mtkrkpfylv ngisvsvpfm ssskdqyiea ydgfkvlrlp yrqgrdntnr 51 nfsmyfylpd kkgelddllk rmtstpgfld shtprervev defripkfki 101 efgfeassvf sdfeidvsfy qkalieidee gteaaaataf vdnedgcgfv 151 etldfvadhp flflireeqt gtvlfadlvi aspslsnidv geamkkqndv 201 aifltgivis svaknsnfvf spasinaalt mvaassggeq geelrsfils 251 flkssstdel naifreiasv vlvdgskkgg pkiavvngmw mdqslsvnpl 301 skdlfknffs aafaqvdfrs kaeevrtevn awasshtngl ikdllprgsv 351 tsltdrvygs alyfkgtwee kysksmtkck pfyllngtsv svpfmssfek 401 qyiaaydgfk vlrlpyrqgr dntnrnfamy iylpdkkgel ddllermtst 451 pgfldshnpe rrvkvgkfri pkfkiefgfe assafsdfel dvsfyqktli 501 eidekgteav tftafrsayl gcalvkpidf vadhpflfli reeqtgtvlf 551 agqifdpsa
2104735 --------------------------------------------------- Protein Name: serine proteinase inhibitor 2104735: 1..374 6 Activities: intracellular inhibitor of granzyme B NCBI Seq ID: 2104735 Created Apr 8, 1997 Citation Data Submission: J Sun, L Ooms, C Bird, V Sutton, J Trapani & P Bird (1997). Citation J Sun, L Ooms, C Bird, V Sutton, J Trapani & P Bird (1997). A new family of ten murine ovalbumin serpins includes two homologs of proteinase inhibitor 8 and two homologs of the granzyme B inhibitor (proteinase inhibitor 9). J. Biol. Chem. , . (In Press) Updated May 9, 1997 Coding region Comments: spi6; similar to human 2104734: 45..1169 granzyme B inhibitor, proteinase inhibitor 9; member of ovalbumin group of serpin superfamily. Sequence 374 aa 1 mntlsegngt faihllkmlc qsnpsknvcy spasissala mvllgakgqt 51 avqisqalgl nkeegihqgf qlllrklnkp drkyslrvan rlfadktcev 101 lqtfkesslh fydsemeqls faeeaevsrq hintwvskqt egkipellsg 151 gsvdsetrlv linalyfkgk whqpfnkeyt mdmpfkinkd ekrpvqmmcr 201 edtynlayvk evqaqvlvmp yegmelslvv llpdegvdls kvennltfek 251 ltawmeadfm kstdvevflp kfklqedydm eslfqrlgvv dvfqedkadl 301 sgmspernlc vskfvhqsvv eineegteaa aasaiiefcc assvptfcad 351 hpflffirhn kansilfcgr fssp
2133935 --------------------------------------------------- Definition serine proteinase inhibitor CP9 - common carp Protein Name: serine proteinase inhibitor 2133935: [ Whole ] CP9 PIR Name: I50494 NCBI Seq ID: 2133935 Created Sep 13, 1996 Updated Mar 31, 1997 Citation C.J. Huang, M.S. Lee, F.L. Huang & G.D. Chang (1995). A protease inhibitor of the serpin family is a major protein in carp perimeningeal fluid: II. cDNA cloning, sequence analysis, and Escherichia coli expression. J. Neurochem. 64, 1721-1727. MEDLINE identifier: 95198028 Sequence 410 aa 1 mawaaphegh dhdghpadhy hhlhhgkdea hpshsgedac hllsphnadf 51 afslykklal hpdaqgknif fspvgismal smlavgakgs tlsqiysslg 101 ysglkaqqvn egyehlihml ghsqdtmqle agagvaireg fkvvdqflkd 151 vqhyynseaf svdfskpeia aeeinqfiak ktndkitdmv kdldsdmvmm 201 linymyfrgk wdkpfeaqlt hkaefkvdkd ttvqvdmmkr tgrydiyqdp 251 vnqttvmmvp ykgntsmmiv lpdegkmkdv eesicrhhlk nwhdklfrss 301 vdlfmpkfsi satsklndil temgvtdafs dtadfsgmte elkvkvsqvv 351 hkavlsvdek gteaaaatti eimpmslpgt vmlnrpflvl ivedttksil 401 fmgkitnptv
481621 --------------------------------------------------- Definition serpin - pig Protein Name: serpin 481621: [ Whole ] PIR Name: S38962 NCBI Seq ID: 481621 Created Mar 19, 1997 Updated Mar 19, 1997 Citation W.F. Teschauer, R. Mentele & C.P. Sommerhoff (1993). Primary structure of a porcine leukocyte serpin. Eur. J. Biochem. 217, 519-526. MEDLINE identifier: 94039085 Sequence 378 aa 1 meqlsaantr faldlfraln esnpagnifi spfsissala millgtrgnt 51 eaqmskalhf dtvkdihsrf qslnadinkc gasyilklan rlfgektyhf 101 lpeflastqk tygaelasvd flraseeark ainewvkeqt egkipellas 151 gvvdsatklv lvnaiyfkgs wqekfmteat kdapfrlnkk dsktvkmmyq 201 kkkfpfgyik elkcrvlelp yqgkdlsmvi llpdsiedes tglrkieqhl 251 tleklrewtk pdnlellevn vhlprfrlee sydlnaplar lgvqdlfgsr 301 adltgmsear dlfiskvvhk sfvevneegt eaaaatxgia vfamlmpeed 351 fiadhpfiff irhnpssnil flgrlssp
108207 --------------------------------------------------- Definition serpin - horse Protein Name: serpin 108207: [ Whole ] PIR Name: S25828 NCBI Seq ID: 108207 Created Mar 19, 1997 Updated Mar 19, 1997 Citation J. Potempa, J.K. Wunderlich & J. Travis (1991). Comparative properties of three functionally different but structurally related serpin variants from horse plasma. Biochem. J. 274, 465-471. MEDLINE identifier: 91174757 Sequence 54 aa 1 edlqgdavpe rhatkddneh pqepaehkka pneairtllh tnvefnrpfv 51 liiy
108206 --------------------------------------------------- Definition serpin - horse Protein Name: serpin 108206: [ Whole ] PIR Name: S25829 NCBI Seq ID: 108206 Created Mar 19, 1997 Updated Mar 19, 1997 Citation J. Potempa, J.K. Wunderlich & J. Travis (1991). Comparative properties of three functionally different but structurally related serpin variants from horse plasma. Biochem. J. 274, 465-471. MEDLINE identifier: 91174757 Sequence 49 aa 1 edlqgdavpe rhatkddneh pqepaehkka pnerpatlll dnvefnrpf
108205 --------------------------------------------------- Definition serpin - horse Protein Name: serpin 108205: [ Whole ] PIR Name: S14338 NCBI Seq ID: 108205 Created Mar 19, 1997 Updated Mar 19, 1997 Citation J. Potempa, J.K. Wunderlich & J. Travis (1991). Comparative properties of three functionally different but structurally related serpin variants from horse plasma. Biochem. J. 274, 465-471. MEDLINE identifier: 91174757 Sequence 54 aa 1 edlqgdavpe rhatkddneh pqepaehkka pnemipmslp pelefnrpfi 51 liiy
100612 --------------------------------------------------- Definition protein Z4 - barley Protein Name: protein Z4 100612: [ Whole ] PIR Name: S13822 NCBI Seq ID: 100612 Created Mar 19, 1997 Updated Mar 19, 1997 Citation A. Brandt, I. Svendsen & J. Hejgaard (1990). A plant serpin gene. Structure, organization and expression of the gene encoding barley protein Z4. Eur. J. Biochem. 194, 499-505. MEDLINE identifier: 91099324 Sequence 399 aa 1 mattlatdvr lsiahqtrfa lrlrsaissn peraagnvaf splslhvals 51 litagaaatr dqlvailgdg gagdakelna laeqvvqfvl anesstggpr 101 iafangifvd aslslkpsfe elavcqykak tqsvdfqhkt leavgqvnsw 151 veqvttglik qilppgsvdn ttklilgnal yfkgawdqkf desntkcdsf 201 hlldgssiqt qfmsstkkqy isssdnlkvl klpyakghdk rqfsmyillp 251 gaqdglwsla krlstepefi enhipkqtve vgrfqlpkfk isyqfeassl 301 lralglqlpf seeadlsemv dssqgleish vfhksfvevn eegteagaat 351 vamgvamsmp lkvdlvdfva nhpflflire diagvvvfvg hvtnplisa
2133926 --------------------------------------------------- Definition alpha-1-antitrypsin precursor - common carp Protein Name: alpha-1-antitrypsin 2133926: [ Whole ] precursor PIR Name: I50492 NCBI Seq ID: 2133926 Created Sep 13, 1996 Updated Mar 18, 1997 Citation C.J. Huang, M.S. Lee, F.L. Huang & G.D. Chang (1995). A protease inhibitor of the serpin family is a major protein in carp perimeningeal fluid: II. cDNA cloning, sequence analysis, and Escherichia coli expression. J. Neurochem. 64, 1721-1727. MEDLINE identifier: 95198028 Sequence 372 aa 1 mpatcllhtm ltlpspstrn lrsiqmprar tfsspsryrn gfehagcrcq 51 gstlsqiyss lgysglqasq vnegyehlih mlghsreamq leagagvair 101 egfkvvdqfl kdvqhyynse afsvdfskpe iaaeeinqfi akktndkitn 151 mvkdldsdtv mmlinymyfr gkwdkpfdaq lthkadfkvd edttvqvdmm 201 krtgrydiyq dpvnqttvmm vpykgntsmm iifpddgkmk eleesisrhh 251 lknwhdklfr ssvdlfmpkf sitatsklkg iledmgvtda fgdtadlsgl 301 teevkvkvsq vvhkavlsvd ekgteaaaat tieimpmslp dtvilnrpfl 351 vlivedttks ilfmgkitnp te
1362853 --------------------------------------------------- Definition leupin - human (fragment) Protein Name: leupin 1362853: [ Whole ] PIR Name: S57522 NCBI Seq ID: 1362853 Created Oct 10, 1995 Updated Mar 18, 1997 Citation Data Submission: R.C. Barnes & D.M. Worrall (1995). Citation R.C. Barnes & D.M. Worrall (1995). Identification of a novel human serpin gene; cloning sequencing and expression of leupin. FEBS Lett. 373, 61-65. MEDLINE identifier: 96013887 Sequence 390 aa 1 mnslseantk fmfdlfqqfr kskennifys pisitsalgm vllgakdnta 51 qqiskvlhfd qvtentteka atyhvdrsgn vhhqfqkllt efnkstdaye 101 lkianklfge ktyqflqeyl daikkfyqts vestdfanap eesrkkinsw 151 vesqtnekik nlfpdgtign dttlvlvnai yfkgqwenkf kkentkeekf 201 wpnkntyksv qmmrqynsfn falledvqak vleipykgkd lsmivllpne 251 idglqkleek ltaeklmewt slqnmretcv dlhlprfkme esydlkdtlr 301 tmgmvnifng dadlsgmtws hglsvskvlh kafvevteeg veaaaatavv 351 vvelsspstn eefccnhpfl ffirqnktns ilfygrfssp
68741 --------------------------------------------------- Definition alpha-1-antitrypsin precursor - human Protein Names: alpha-1-antitrypsin 68741: [ Whole ] precursor; alpha-1-AT; alpha-1- proteinase inhibitor PIR Name: ITHU NCBI Seq ID: 68741 Comment The Z variant allele has Lys-366. Deficiency of the normal inhibitor in individuals homozygous for the Z allele can result in the development of chronic emphysema or infantile liver cirrhosis. Created Nov 30, 1980 Updated Mar 18, 1997 Citation G.L. Long, T. Chandra, S.L. Woo, E.W. Davie & K. Kurachi (1984). Complete sequence of the cDNA for human alpha 1- antitrypsin and the gene for the S variant. Biochemistry 23, 4828-4837. MEDLINE identifier: 85047190 Citation S. Rosenberg, P.J. Barr, R.C. Najarian & R.A. Hallewell (1984). Synthesis in yeast of a functional oxidation- resistant mutant of human alpha-antitrypsin. Nature 312, 77- 80. MEDLINE identifier: 85036645 Citation A. Bollen, A. Herzog, A. Cravador, P. Herion, P. Chuchana, A. Vander Straten, R. Loriau, P. Jacobs & A. van Elsen (1983). Cloning and expression in Escherichia coli of full-length complementary DNA coding for human alpha 1-antitrypsin. DNA 2, 255-264. MEDLINE identifier: 84107980 Citation B. Colau, P. Chuchana & A. Bollen (1984). Revised sequence of full-length complementary DNA coding for human alpha 1- antitrypsin. DNA 3, 327-330. MEDLINE identifier: 85026667 Citation G. Ciliberto, L. Dente & R. Cortese (1985). Cell-specific expression of a transfected human alpha 1-antitrypsin gene. Cell 41, 531-540. MEDLINE identifier: 85176977 Citation R.W. Carrell, J.O. Jeppsson, C.B. Laurell, S.O. Brennan, M.C. Owen, L. Vaughan & D.R. Boswell (1982). Structure and variation of human alpha 1-antitrypsin. Nature 298, 329-334. MEDLINE identifier: 82220135 Citation X.J. Zhu, S.S. Kang, K. Hargrove, D. Shochat, M. Jarrells, M. Mojesky & S.K. Chan (1987). The identification of epitopic sites in human alpha 1-proteinase inhibitor. Biochem. J. 246, 25-36. MEDLINE identifier: 88049621 Citation Data Submission: K.L. Weiland, C.N. Falany & T.P. Dooley (1989). Citation J.H. Riley, I.C. Bathurst, M.R. Edbrooke, R.W. Carrell & R.K. Craig (1985). Alpha 1-antitrypsin and serum albumin mRNA accumulation in normal, acute phase and ZZ human liver. FEBS Lett. 189, 361-366. MEDLINE identifier: 86005469 Citation A.J. Schulze, U. Baumann, S. Knof, E. Jaeger, R. Huber & C.B. Laurell (1990). Structural transition of alpha 1-antitrypsin by a peptide sequentially similar to beta-strand s4A. Eur. J. Biochem. 194, 51-56. MEDLINE identifier: 91071209 Citation M.A. Niemann, A.J. Narkates & E.J. Miller (1992). Isolation and serine protease inhibitory activity of the 44-residue, C- terminal fragment of alpha 1-antitrypsin from human placenta. Matrix 12, 233-241. MEDLINE identifier: 93024095 Citation R. Dengler, G. Eger, F. Lottspeich, A. Plewan, A. Ogilvie & B. Emmerich (1992). Proteolytic inactivation of alpha 1- proteinase inhibitor in vivo: detection, characterization and quantitation of the main fragment excreted in the urine of leukemia patients. Biol. Chem. Hoppe-Seyler 373, 581-588. MEDLINE identifier: 92384968 Citation R. Dengler, F. Lottspeich, W. Oberthur, A.E. Mast & B. Emmerich (1995). Limited proteolysis of alpha 1-proteinase inhibitor (alpha 1-PI) in acute leukemia: studies on the resulting fragments and implication for the structure of the inactivated inhibitor. Biol. Chem. Hoppe-Seyler 376, 165-172. MEDLINE identifier: 95336645 Citation M. Leicht, G.L. Long, T. Chandra, K. Kurachi, V.J. Kidd, M. Mace, E.W. Davie & S.L. Woo (1982). Sequence homology and structural comparison between the chromosomal human alpha 1- antitrypsin and chicken ovalbumin genes. Nature 297, 655-659. MEDLINE identifier: 82220035 Citation W.S. Chang, M.R. Wardell, D.A. Lomas & R.W. Carrell (1996). Probing serpin reactive-loop conformations by proteolytic cleavage. Biochem. J. 314, 647-653. MEDLINE identifier: 96239126 Citation C. Coutelle, A. Speer, J. Rogers, N. Kalsheker, S. Humphries & R. Williamson (1985). Construction and partial characterization of a human liver cDNA library. Biomed. Biochim. Acta 44, 421-431. MEDLINE identifier: 85225507 Citation J.P. Faber, S. Weidinger & K. Olek (1990). Sequence data of the rare deficient alpha 1-antitrypsin variant PI Zaugsburg. Am. J. Hum. Genet. 46, 1158-1162. MEDLINE identifier: 90252805 Citation Data Submission: H. Loebermann, R. Tokuoka, J. Deisenhofer & R. Huber (1988). Citation Data Submission: H. Loebermann, R. Tokuoka, J. Deisenhofer & R. Huber (1988). Citation Data Submission: H. Loebermann, R. Tokuoka, J. Deisenhofer & R. Huber (1988). Citation H. Loebermann, R. Tokuoka, J. Deisenhofer & R. Huber (1984). Human alpha 1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function. J. Mol. Biol. 177, 531-557. MEDLINE identifier: 84292309 Citation R.W. Carrell, J.O. Jeppsson, L. Vaughan, S.O. Brennan, M.C. Owen & D.R. Boswell (1981). Human alpha 1-antitrypsin: carbohydrate attachment and sequence homology. FEBS Lett. 135, 301-303. MEDLINE identifier: 82095611 domain signal sequence 68741: 1..24 product alpha-1-antitrypsin 68741: 25..418 (experimentally determined) binding site carbohydrate (Asn) (covalent) 68741: 70 (experimentally determined) binding site carbohydrate (Asn) (covalent) 68741: 107 (experimentally determined) binding site carbohydrate (Asn) (covalent) 68741: 271 (experimentally determined) inhibit site Met (elastase, collagenase) 68741: 382 (experimentally determined) Sequence 418 aa 1 mpssvswgil llaglcclvp vslaedpqgd aaqktdtshh dqdhptfnki 51 tpnlaefafs lyrqlahqsn stniffspvs iatafamlsl gtkadthdei 101 leglnfnlte ipeaqihegf qellrtlnqp dsqlqlttgn glflseglkl 151 vdkfledvkk lyhseaftvn fgdteeakkq indyvekgtq gkivdlvkel 201 drdtvfalvn yiffkgkwer pfevkdteee dfhvdqvttv kvpmmkrlgm 251 fniqhckkls swvllmkylg nataifflpd egklqhlene lthdiitkfl 301 enedrrsasl hlpklsitgt ydlksvlgql gitkvfsnga dlsgvteeap 351 lklskavhka vltidekgte aagamfleai pmsippevkf nkpfvflmie 401 qntksplfmg kvvnptqk
68734 --------------------------------------------------- Definition antithrombin III precursor - human Protein Name: antithrombin III precursor 68734: [ Whole ] PIR Name: XHHU3 NCBI Seq ID: 68734 Created Apr 5, 1983 Updated Mar 18, 1997 Citation R.J. Olds, D.A. Lane, V. Chowdhury, V. De Stefano, G. Leone & S.L. Thein (1993). Complete nucleotide sequence of the antithrombin gene: evidence for homologous recombination causing thrombophilia. Biochemistry 32, 4216-4224. MEDLINE identifier: 93237227 Citation S.C. Bock, K.L. Wion, G.A. Vehar & R.M. Lawn (1982). Cloning and expression of the cDNA for human antithrombin III. Nucleic Acids Res. 10, 8113-8125. MEDLINE identifier: 83143280 Citation T. Chandra, R. Stackhouse, V.J. Kidd & S.L. Woo (1983). Isolation and sequence characterization of a cDNA clone of human antithrombin III. Proc. Natl. Acad. Sci. U.S.A. 80, 1845-1848. MEDLINE identifier: 83169777 Citation E.V. Prochownik, A.F. Markham & S.H. Orkin (1983). Isolation of a cDNA clone for human antithrombin III. J. Biol. Chem. 258, 8389-8394. MEDLINE identifier: 83238456 Citation J.Y. Chang (1989). Binding of heparin to human antithrombin III activates selective chemical modification at lysine 236. Lys-107, Lys-125, and Lys-136 are situated within the heparin- binding site of antithrombin III. J. Biol. Chem. 264, 3111- 3115. MEDLINE identifier: 89123426 Citation T.E. Petersen, G. Dudek-Wojciechowska, L. Sottrup-Jensen & S. Magnusson (1979). Primary structure of antithrombin-III (heparin cofactor). Partial homology between alpha-1- antitrypsin and antithrombin-III. (in) The Physiological Inhibitors of Blood Coagulation and Fibrinolysis; D., Wiman, B., Collen & M. Verstraete; The Physiological Inhibitors of Blood Coagulation and Fibrinolysis; 43-54. Citation I. Bjork, A. Danielsson, J.W. Fenton & Jornvall (1981). The site in human antithrombin for functional proteolytic cleavage by human thrombin. FEBS Lett. 126, 257-260. MEDLINE identifier: 81212814 Citation G. Zettlmeissl, H.S. Conradt, M. Nimtz & H.E. Karges (1989). Characterization of recombinant human antithrombin III synthesized in Chinese hamster ovary cells. J. Biol. Chem. 264, 21153-21159. MEDLINE identifier: 90078215 Citation C.S. Liu & J.Y. Chang (1987). Probing the heparin-binding domain of human antithrombin III with V8 protease. Eur. J. Biochem. 167, 247-252. MEDLINE identifier: 87304255 Citation J.Y. Borg, S.O. Brennan, R.W. Carrell, P. George, D.J. Perry & J. Shaw (1990). Antithrombin Rouen-IV 24 Arg----Cys. The amino-terminal contribution to heparin binding. FEBS Lett. 266, 163-166. MEDLINE identifier: 90306344 Citation T. Koide, S. Odani, K. Takahashi, T. Ono & N. Sakuragawa (1984). Antithrombin III Toyama: replacement of arginine-47 by cysteine in hereditary abnormal antithrombin III that lacks heparin-binding ability. Proc. Natl. Acad. Sci. U.S.A. 81, 289-293. MEDLINE identifier: 84119472 Citation C.B. Grundy, F. Thomas, D.S. Millar, M. Krawczak, E. Melissari, V. Lindo, E. Moffat, V.V. Kakkar & D.N. Cooper (1991). Recurrent deletion in the human antithrombin III gene. Blood 78, 1027-1032. MEDLINE identifier: 91329813 Citation M.N. Blackburn, R.L. Smith, J. Carson & C.C. Sibley (1984). The heparin-binding site of antithrombin III. Identification of a critical tryptophan in the amino acid sequence. J. Biol. Chem. 259, 939-941. MEDLINE identifier: 84111578 Citation S.C. Bock & D.J. Levitan (1983). Characterization of an unusual DNA length polymorphism 5' to the human antithrombin III gene. Nucleic Acids Res. 11, 8569-8582. MEDLINE identifier: 84169500 Citation S.C. Bock, J.A. Marrinan & E. Radziejewska (1988). Antithrombin III Utah: proline-407 to leucine mutation in a highly conserved region near the inhibitor reactive site. Biochemistry 27, 6171-6178. MEDLINE identifier: 89050967 Citation W.S. Chang, M.R. Wardell, D.A. Lomas & R.W. Carrell (1996). Probing serpin reactive-loop conformations by proteolytic cleavage. Biochem. J. 314, 647-653. MEDLINE identifier: 96239126 domain signal sequence 68734: 1..32 product antithrombin III 68734: 33..464 (experimentally determined) disulfide bond (experimentally determined) 68734: 40 bond 160 disulfide bond (experimentally determined) 68734: 53 bond 127 disulfide bond (experimentally determined) 68734: 279 bond 462 binding site heparin (Trp) 68734: 81 (experimentally determined) binding site carbohydrate (Asn) (covalent) 68734: 128 (experimentally determined) binding site carbohydrate (Asn) (covalent) 68734: 167 (experimentally determined) binding site carbohydrate (Asn) (covalent) 68734: 187 (experimentally determined) binding site carbohydrate (Asn) (covalent) 68734: 224 (experimentally determined) cleavage site Arg-Ser (thrombin) 68734: 425..426 (experimentally determined) inhibit site Arg (thrombin, coagulation factor 68734: 425 Xa) (experimentally determined) Sequence 464 aa 1 mysnvigtvt sgkrkvylls llligfwdcv tchgspvdic takprdipmn 51 pmciyrspek katedegseq kipeatnrrv welskansrf attfyqhlad 101 skndndnifl splsistafa mtklgacndt lqqlmevfkf dtisektsdq 151 ihfffaklnc rlyrkankss klvsanrlfg dksltfnety qdiselvyga 201 klqpldfken aeqsraaink wvsnktegri tdvipseain eltvlvlvnt 251 iyfkglwksk fspentrkel fykadgescs asmmyqegkf ryrrvaegtq 301 vlelpfkgdd itmvlilpkp ekslakveke ltpevlqewl deleemmlvv 351 hmprfriedg fslkeqlqdm glvdlfspek sklpgivaeg rddlyvsdaf 401 hkaflevnee gseaaastav viagrslnpn rvtfkanrpf lvfirevpln 451 tiifmgrvan pcvk
1885350 --------------------------------------------------- Protein Name: serpin 1885350: [ Whole ] NCBI Seq ID: 1885350 Updated Mar 14, 1997 Citation REF [1] S.K. Rasmussen. Natural mutant of wheat serpin. Unpublished Citation REF [2] Data Submission: S.K. Rasmussen (1997). Coding region 1885349: 58..1257 Sequence 399 aa 1 mattlatdvr lsiahqtrfa lrlastissn pksaasnaaf spvslhsals 51 llaagagsat rdqlvatlgt gevegghala eqvvqfvlad assaggprva 101 fangvfvdas lllkpsfqel avckykaetq svdfqtkaae vttqvnswve 151 kvtsgrikni lpsgsvdntt klvlanalyf kgawtdqfds ygtkndyfyl 201 ldgssvqtpf mssmdddqyi sssdglkvlk lpykqggdnr qfsmyillpe 251 apgglsslae klsaepdfle rhiprqrvai rqfklpkfki sfgmeasdll 301 kclglqlpfs deadfsemvd spmpqglrvs svfhqafvev neqgteaaas 351 taikmvpqqa rppsvmdfia dhpflfllre disgvvlfmg hvvnpllss
1885346 --------------------------------------------------- Protein Name: serpin 1885346: [ Whole ] NCBI Seq ID: 1885346 Updated Mar 14, 1997 Citation REF [1] S.K. Rasmussen. Wheat serpin with a putative trypsin inhibitory reactive site. Unpublished Citation REF [2] Data Submission: S.K. Rasmussen (1997). Coding region 1885345: 22..1218 Sequence 398 aa 1 mattlatdvr lsiahqtrfa frlasaissn pestvnnaaf spvslhvals 51 litagaggat rnqlaatlge geveglhala eqvvqfvlad asniggprva 101 fangvfvdas lqlkpsfqel avckykaeaq svdfqtkaae vtaqvnswve 151 kvttglikdi lpagsidntt rlvlgnalyf kgawtdqfdp ratqsddfyl 201 ldgssiqtpf mysseeqyis ssdglkvlkl pykqggdkrq fsmyillpea 251 lsglwslaek lsaepefleq hiprqkvalr qfklpkfkis lgieasdllk 301 glglllpfga eadlsemvds pmaqnlyiss ifhkafvevn etgteaaatt 351 iakvvlrqap ppsvldfivd hpflflired tsgvvlfigh vvnpllss
2136150 --------------------------------------------------- Definition serpin - human (fragments) Protein Name: serpin 2136150: [ Whole ] PIR Name: S65750 NCBI Seq ID: 2136150 Created Dec 6, 1996 Updated Mar 13, 1997 Citation B.Z. Packard, S.S. Lee, E. Remold-O'Donnell & A. Komoriya (1995). A serpin from human tumor cells with direct lymphoid immunomodulatory activity: mitogenic stimulation of human tumor-infiltrating lymphocytes. Biochim. Biophys. Acta 1269, 41-50. MEDLINE identifier: 96049524 Sequence 116 aa 1 tfhfntveev hsrtynflpe flvstqktyg adlasvdfqh asedarfayg 51 yiedlkvlel pyqgeelsmv illpddiede stglklhewt kpenldfiev 101 nvxlplgvqd lfnssk
2134403 --------------------------------------------------- Definition serpin precursor - chicken Protein Name: serpin precursor 2134403: [ Whole ] PIR Name: S70647 NCBI Seq ID: 2134403 Created Feb 14, 1997 Updated Mar 13, 1997 Citation T. Osterwalder, J. Contartese, E.T. Stoeckli, T.B. Kuhn & P. Sonderegger (1996). Neuroserpin, an axonally secreted serine protease inhibitor. EMBO J. 15, 2944-2953. MEDLINE identifier: 96272154 domain signal peptide 2134403: 1..16 product serpin 2134403: 17..410 Sequence 410 aa 1 myflgllsll vlpskafktn fpdetiaels vnvynqlraa redenilfcp 51 lsiaiamgmi elgahgttlk eirhslgfds lkngeeftfl kdlsdmatte 101 eshyvlnman slyvqngfhv sekflqlvkk yfkaevenid fsqsaavath 151 inkwvenhtn nmikdfvssr dfsalthlvl inaiyfkgnw ksqfrpentr 201 tfsftkddet evqipmmyqq gefyygefsd gsneaggiyq vleipyegde 251 ismmivlsrq evplvtlepl vkaslinewa nsvkkqkvev ylprftveqe 301 idlkdvlkgl gitevfsrsa dltamsdnke lylakafhka flevneegse 351 aaaasgmiai srmavlypqv ivdhpffflv rnrrtgtvlf mgrvmhpeam 401 ntsghdfeel
2130110 --------------------------------------------------- Definition serpin - wheat Protein Name: serpin 2130110: [ Whole ] PIR Name: S65782 NCBI Seq ID: 2130110 Created Oct 28, 1996 Updated Mar 13, 1997 Citation S.K. Rasmussen, S.W. Dahl, A. Norgard & J. Hejgaard (1996). A recombinant wheat serpin with inhibitory activity. Plant Mol. Biol. 30, 673-677. MEDLINE identifier: 96189280 Sequence 398 aa 1 mattlatdvr lsiahqtrfa lrlastissn pksaasnaaf spvslysals 51 llaagagsat rdqlvatlgt gkveglhala eqvvqfvlad asstggsacr 101 fangvfvdas lllkpsfqei avckykaetq svdfqtkaae vttqvnswve 151 kvtsgrikdi lppgsidntt klvlanalyf kgawteqfds ygtkndyfyl 201 ldgssvqtpf mssmddqyll ssdglkvlkl pykqggdnrq ffmyillpea 251 pgglsslaek lsaepdfler hiprqrvalr qfklpkfkis fgieasdllk 301 clglqlpfgd eadfsemvds lmpqglrvss vfhqafvevn eqgteaaast 351 aikmvlqqar ppsvmdfiad hpflflvred isgvvlfmgh vvnpllss
90328 --------------------------------------------------- Definition beta-glucuronidase (EC 3.2.1.31) precursor - mouse Protein Names: beta-glucuronidase 90328: [ Whole ] precursor; beta-D-glucuronoside glucuronosohydrolase EC number: 3.2.1.31 PIR Name: A29977 NCBI Seq ID: 90328 Created Nov 19, 1988 Updated Mar 13, 1997 Citation M.A. D'Amore, P.M. Gallagher, T.R. Korfhagen & R.E. Ganschow (1988). Complete sequence and organization of the murine beta- glucuronidase gene. Biochemistry 27, 7131-7140. MEDLINE identifier: 89062453 Citation P.M. Gallagher, M.A. D'Amore, S.D. Lund & R.E. Ganschow (1988). The complete nucleotide sequence of murine beta- glucuronidase mRNA and its deduced polypeptide. Genomics 2, 215-219. MEDLINE identifier: 88284700 Citation H. Li, K.H. Takeuchi, K. Manly, V. Chapman & R.T. Swank (1990). The propeptide of beta-glucuronidase. Further evidence of its involvement in compartmentalization of beta- glucuronidase and sequence similarity with portions of the reactive site region of the serpin superfamily. J. Biol. Chem. 265, 14732-14735. MEDLINE identifier: 90368633 domain signal sequence 90328: 1..22 product beta-glucuronidase 90328: 23..648 Sequence 648 aa 1 mslkwsacwv algqllcsca lalkggmlfp kespsrelka ldglwhfrad 51 lsnnrlqgfe qqwyrqplre sgpvldmpvp ssfnditqea alrdfigwvw 101 yereailprr wtqdtdmrvv lrinsahyya vvwvngihvv ehegghlpfe 151 adisklvqsg plttcritia inntltphtl ppgtivyktd tsmypkgyfv 201 qdtsfdffny aglhrsvvly ttpttyiddi tvitnveqdi glvtywisvq 251 gsehfqlevq lldedgkvva hgtgnqgqlq vpsanlwwpy lmhehpaymy 301 slevkvttte svtdyytlpv girtvavtks kflingkpfy fqgvnkheds 351 dirgkgfdwp llvkdfnllr wlgansfrts hypyseevlq lcdrygivvi 401 decpgvgivl pqsfgneslr hhlevmeelv rrdknhpavv mwsvanepss 451 alkpaayyfk tlithtkald ltrpvtfvsn akydadlgap yvdvicvnsy 501 fswyhdyghl eviqpqlnsq fenwykthqk piiqseygad aipgihedpp 551 rmfseeyqka vlenyhsvld qkrkeyvvge liwnfadfmt nqsplrvign 601 kkgiftrqrq pktsafilre rywrianetg ghgsgprtqc fgsrpftf
107324 --------------------------------------------------- Definition plasminogen activator inhibitor 2 precursor - human Protein Names: plasminogen activator 107324: [ Whole ] inhibitor 2 precursor; urokinase inhibitor PIR Name: A32853 NCBI Seq ID: 107324 Created Nov 22, 1989 Updated Feb 28, 1997 Citation R.D. Ye, S.M. Ahern, M.M. Le Beau, R.V. Lebo & J.E. Sadler (1989). Structure of the gene for human plasminogen activator inhibitor-2. The nearest mammalian homologue of chicken ovalbumin. J. Biol. Chem. 264, 5495-5502. MEDLINE identifier: 89174589 Citation J.A. Samia, S.J. Alexander, K.W. Horton, P.E. Auron, M.G. Byers, T.B. Shows & A.C. Webb (1990). Chromosomal organization and localization of the human urokinase inhibitor gene: perfect structural conservation with ovalbumin. Genomics 6, 159-167. MEDLINE identifier: 90152678 Citation T.M. Antalis, M.A. Clark, T. Barnes, P.R. Lehrbach, P.L. Devine, G. Schevzov, N.H. Goss, R.W. Stephens & P. Tolstoshev (1988). Cloning and expression of a cDNA coding for a human monocyte-derived plasminogen activator inhibitor. Proc. Natl. Acad. Sci. U.S.A. 85, 985-989. MEDLINE identifier: 88125032 Citation A.C. Webb, K.L. Collins, S.E. Snyder, S.J. Alexander, L.J. Rosenwasser, R.L. Eddy, T.B. Shows & P.E. Auron (1987). Human monocyte Arg-Serpin cDNA. Sequence, chromosomal assignment, and homology to plasminogen activator-inhibitor. J. Exp. Med. 166, 77-94. MEDLINE identifier: 87252928 Citation W.D. Schleuning, R.L. Medcalf, C. Hession, R. Rothenbuhler, A. Shaw & E.K. Kruithof (1987). Plasminogen activator inhibitor 2: regulation of gene transcription during phorbol ester- mediated differentiation of U-937 human histiocytic lymphoma cells. Mol. Cell. Biol. 7, 4564-4567. MEDLINE identifier: 88142852 Citation R.D. Ye, T.C. Wun & J.E. Sadler (1987). cDNA cloning and expression in Escherichia coli of a plasminogen activator inhibitor from human placenta. J. Biol. Chem. 262, 3718-3725. MEDLINE identifier: 87137674 Citation P.H. Jensen, E. Schuler, G. Woodrow, M. Richardson, N. Goss, P. Hojrup, T.E. Petersen & L.K. Rasmussen (1994). A unique interhelical insertion in plasminogen activator inhibitor-2 contains three glutamines, Gln83, Gln84, Gln86, essential for transglutaminase-mediated cross-linking. J. Biol. Chem. 269, 15394-15398. MEDLINE identifier: 94253109 Citation E.K. Kruithof, J.D. Vassalli, W.D. Schleuning, R.J. Mattaliano & F. Bachmann (1986). Purification and characterization of a plasminogen activator inhibitor from the histiocytic lymphoma cell line U-937. J. Biol. Chem. 261, 11207-11213. MEDLINE identifier: 86278222 Citation U. Kiso, H. Kaudewitz, A. Henschen, B. Astedt, E.K. Kruithof & F. Bachmann (1988). Determination of intermediates, products and cleavage site in the reaction between plasminogen activator inhibitor type-2 and urokinases. FEBS Lett. 230, 51- 56. MEDLINE identifier: 88167197 Citation E.K. Kruithof & E. Cousin (1988). Plasminogen activator inhibitor 2. Isolation and characterization of the promoter region of the gene. Biochem. Biophys. Res. Commun. 156, 383- 388. MEDLINE identifier: 89025873 domain signal sequence 107324: 1..22 product plasminogen activator inhibitor 2 107324: 23..415 modified site acetylated amino end (Ser) (in 107324: 23 mature form) binding site carbohydrate (Asn) (covalent) 107324: 75 binding site carbohydrate (Asn) (covalent) 107324: 115 binding site carbohydrate (Asn) (covalent) 107324: 339 xlink bond isopeptide (Gln) (interchain to 107324: 83 bond unknown proteins) xlink bond isopeptide (Gln) (interchain to 107324: 84 bond unknown proteins) xlink bond isopeptide (Gln) (interchain to 107324: 86 bond unknown proteins) cleavage site Arg-Thr (plasminogen activator) 107324: 380..381 (experimentally determined) inhibit site Arg (plasminogen activator) 107324: 380 (experimentally determined) Sequence 415 aa 1 medlcvantl falnlfkhla kasptqnlfl spwsisstma mvymgsrgst 51 edqmakvlqf nevganavtp mtpenftscg fmqqiqkgsy pdailqaqaa 101 dkihssfrsl ssainastgn yllesvnklf geksasfree yirlcqkyys 151 sepqavdfle caeearkkin swvktqtkgk ipnllpegsv dgdtrmvlvn 201 avyfkgkwkt pfekklngly pfrvnsaqrt pvqmmylrek lnigyiedlk 251 aqilelpyag dvsmflllpd eiadvstgle lleseitydk lnkwtskdkm 301 aedevevyip qfkleehyel rsilrsmgme dafnkgranf sgmserndlf 351 lsevfhqamv dvneegteaa agtggvmtgr tghggpqfva dhpflflimh 401 kitncilffg rfssp
2118394 --------------------------------------------------- Definition serpin WSZCI - wheat (fragment) Protein Names: serpin WSZCI; 2118394: [ Whole ] chymotrypsin inhibitor; protein Z homolog PIR Name: S43652 NCBI Seq ID: 2118394 Created Nov 23, 1994 Updated Feb 16, 1997 Citation I. Rosenkrands, J. Hejgaard, S.K. Rasmussen & S.E. Bjorn (1994). Serpins from wheat grain. FEBS Lett. 343, 75-80. MEDLINE identifier: 94215711 Sequence 19 aa 1 qarppsvmdf iadhpflfl
1083848 --------------------------------------------------- Definition alpha-1-antiproteinase - Mongolian jird Protein Name: alpha-1-antiproteinase 1083848: [ Whole ] PIR Name: JX0346 NCBI Seq ID: 1083848 Created Apr 22, 1995 Updated Feb 16, 1997 Citation K. Goto, Y. Suzuki, K. Yoshida, K. Yamamoto & H. Sinohara (1994). Plasma alpha-1-antiproteinase from the Mongolian gerbil, Meriones unguiculatus: isolation, partial characterization, sequencing of cDNA, and implications for molecular evolution. J. Biochem. 116, 582-588. MEDLINE identifier: 95155268 domain signal sequence 1083848: 1..24 product alpha-1-antiproteinase 1083848: 25..406 region serpin binding 1083848: 383..387 binding site carbohydrate (Asn) (covalent) 1083848: 59 binding site carbohydrate (Asn) (covalent) 1083848: 96 binding site carbohydrate (Asn) (covalent) 1083848: 134 binding site carbohydrate (Asn) (covalent) 1083848: 260 binding site carbohydrate (Asn) (covalent) 1083848: 403 inhibit site Met (trypsin, chymotrypsin, 1083848: 371 elastase) Sequence 406 aa 1 mtssiswgll llaglcclvp sflaedaekt dsshqdhima snladfafgl 51 yrvlshqsnt tniflsplsi atalamlslg skddtkaqll qglhfnltet 101 seadihkgfq hllktlnrpd nelqlttgss lfvnnslnlv ekfleevknh 151 yhseaffvnf adseeakkti nsfvekathg kivdlvkdle idtvlalvny 201 iffrgkwekp fdpelteead fhvdksttvk vpmmnrmgmf dvhycdtlss 251 wvllmdylgn ataifilpde gkmqhleqtl tkehiykflq nrhtrsanvh 301 lpklsisgty nlkkvlsplg itqvfsngad lsgittdvpl klskavhkav 351 ltldergtea agttvleavp msippdvcfk npfvviicdk htqsplfvgk 401 vvnptq
1836049 --------------------------------------------------- Definition B-43=43 kDa serine proteinase inhibitor-like protein|serpin- like protein [cattle, brain, Peptide Partial, 61 aa 3 segments] Segments 1836046 B-43=43 kDa serine proteinase inhibitor-like protein|serpin-like protein [cattle, brain, Peptide Partial, 19 aa, segment 1 of 3] 1836047 B-43=43 kDa serine proteinase inhibitor-like protein|serpin-like protein [cattle, brain, Peptide Partial, 13 aa, segment 2 of 3] 1836048 B-43=43 kDa serine proteinase inhibitor-like protein|serpin-like protein [cattle, brain, Peptide Partial, 29 aa, segment 3 of 3] NCBI Journal Scan Mol ID: 391421 NCBI Seq ID: 1836049 Updated Feb 10, 1997 Citation BackBone id_pub = 195781 Nishibori,M., Chikai,T., Kawabata,M., Ohta,J., Ubuka,T. & Saeki,K. (1995). Purification of a novel serpin-like protein from bovine brain. Neurosci. Res. 24, 47-52. MEDLINE identifier: 96275130 Protein Name: B-43 1836046: 280..298 Description: 43 kDa serine [ Gap ] proteinase inhibitor-like 1836047: 309..321 protein|serpin-like protein. [ Gap ] *: Partial 1836048: 358..386 1836046 --------------------------------------------------- Definition B-43=43 kDa serine proteinase inhibitor-like protein|serpin- like protein [cattle, brain, Peptide Partial, 19 aa, segment 1 of 3] NCBI Journal Scan Seq ID: 179768 NCBI Seq ID: 1836046 Created Feb 10, 1997 Citation MEDLINE identifier: 96275130 Figure Fig. 2, "B-43 peptide 3" Numbered from 280 Sequence 19 aa 280 deeexenflp rftleesyd 1836047 --------------------------------------------------- Definition B-43=43 kDa serine proteinase inhibitor-like protein|serpin- like protein [cattle, brain, Peptide Partial, 13 aa, segment 2 of 3] NCBI Journal Scan Seq ID: 179770 NCBI Seq ID: 1836047 Created Feb 10, 1997 Citation MEDLINE identifier: 96275130 Figure Fig. 2, "B-43 peptide 2" Numbered from 309 Sequence 13 aa 309 tdafeetrad fsg 1836048 --------------------------------------------------- Definition B-43=43 kDa serine proteinase inhibitor-like protein|serpin- like protein [cattle, brain, Peptide Partial, 29 aa, segment 3 of 3] NCBI Journal Scan Seq ID: 179772 NCBI Seq ID: 1836048 Created Feb 10, 1997 Citation MEDLINE identifier: 96275130 Figure Fig. 2, "B-43 peptide 1" Numbered from 358 Sequence 29 aa 358 lmvvprfnan hpflffiqhs ktgailfmg
2118396 --------------------------------------------------- Definition alpha-1-antiproteinase isoform E precursor - rabbit Protein Name: alpha-1-antiproteinase 2118396: [ Whole ] isoform E precursor PIR Name: S54981 NCBI Seq ID: 2118396 Created Oct 28, 1996 Updated Feb 7, 1997 Citation A. Saito & H. Sinohara (1995). Rabbit alpha-1-antiproteinase E: a novel recombinant serpin which does not inhibit proteinases. Biochem. J. 307, 369-375. MEDLINE identifier: 95251597 domain signal sequence 2118396: 1..24 (experimentally determined) product alpha-1-antiproteinase E 2118396: 25..413 (experimentally determined) Sequence 413 aa 1 mppsvsrall llaglgcllp gfladeaqet avssheqdhp achriapsla 51 efalslyrev ahesnttnif fspvsialaf amlslgakgd thtqvleglk 101 fnltetaeaq ihdgfrhllh tvnrpdselq laagnalvvh enlklqhkfl 151 edaknlyqse aflvdfrdpe qaktkinshv ekgtrgkivd lvqeldartl 201 lalvnyvffk gkwekpfepe ntkeedfhvd atttvrvpmm srlgmyvmfh 251 cstlastvlr mdykgnatal fllpdegklq hledtlttel iakflakssl 301 rsvtvrfpkl sisgtydlkp llgklgitqv fsnnadlsgi teqeplkvsq 351 alhkavltid ergteaagas fvelipesvp dsitldrpfl fviysheiks 401 plfvgkvvdp tqh
1732049 --------------------------------------------------- Protein Name: EPC-1 1732049: [ Whole ] *: Partial NCBI Seq ID: 1732049 Updated Dec 9, 1996 Citation REF [1] [11] Citation REF [2] Data Submission: V.J. Cristofalo (1996). Coding region * Partial 1732042: 192..275 Comments: PEDF; serpin. 1732043: 57..255 (experimentally determined) 1732044: 276..431 1732045: 80..283 1732046: 123..265 1732047: 86..296 Sequence 332 aa 1 mqalvlllci gallghsscq npasppeegs pdpdstgalv eeedpffkvp 51 vnklaaavsn fgydlyrvrs smspttnvll splsvatals alslgadert 101 esiihralyy dlisspdihg tykelldtvt apqknlksas rivfekklri 151 kssfvaplek sygtrprvlt gnprldlqei nnwvqaqmkg klarstkeip 201 deisilllgv ahfkgqwvtk fdsrktsled fyldeertvr vpmmsdpkav 251 lrygldsdls ckiaqlpltg smsiifflpl kvtqnltlie esltsefihd 301 idrelktvqa vltvpklkls yegevtkslq em
2149091 --------------------------------------------------- Protein Name: serpin-2 2149091: 1..381 Activities: serine proteinase inhibitor NCBI Seq ID: 2149091 Created Nov 21, 1996 Citation Data Submission: H. Gan, H. Jiang & M.R. Kanost (1996). Citation H. Gan, H. Jiang & M.R. Kanost. Molecular cloning of a cDNA for serpin-2 from Manduca sexta. Unpublished Updated Nov 27, 1996 Coding region 2149090: 16..1161 Sequence 381 aa 1 mdsaafssav aqfstkfcne ldnttnivcs plsaenllal ltlgstdpaq 51 tellkalgfp dnddhksirs tfgaltsklk aikgvtllva nkvyikdggy 101 evelelkkda edifdtefek infknsasaa qlinqwvehk tknqikdlfs 151 sssfsafsll vlvnalyfkg lwknqfnpkd tikqvfhldd kktvkipmmf 201 keqkfnyias pdlqaqllev syageetsmv filpddivgl navmqnladg 251 hdlmseikkm tptkvkatlp kfkveteidl tkllpqlgik aifnkddsgl 301 sellspaqev yvteaiqkvy ievnetggeg gdgsgidirs isfmadaetr 351 esayfradhp flyllmgpdn tilfigayrg n
92273 --------------------------------------------------- Definition glia-derived nexin precursor - rat (fragment) Protein Name: glia-derived nexin precursor92273: [ Whole ] PIR Name: B27496 NCBI Seq ID: 92273 Created Jun 30, 1988 Updated Nov 22, 1996 Citation J. Sommer, S.M. Gloor, G.F. Rovelli, J. Hofsteenge, H. Nick, R. Meier & D. Monard (1987). cDNA sequence coding for a rat glia-derived nexin and its homology to members of the serpin superfamily. Biochemistry 26, 6407-6410. MEDLINE identifier: 88107544 Citation H. Nick, J. Hofsteenge, E. Shaw, G. Rovelli & D. Monard (1990). Functional sites of glia-derived nexin (GDN): importance of the site reacting with the protease. Biochemistry 29, 2417-2421. MEDLINE identifier: 90248459 domain signal sequence 92273: 1..19 product glia-derived nexin 92273: 20..397 Sequence 397 aa 1 mnwhfpffil ttvtlssvys qlnslsleel gsdtgiqvfn qiiksqphen 51 vvisphgias ilgmlqlgad grtkkqlstv mrynvngvgk vlkkinkaiv 101 skknkdivtv anavfvrngf kvevpfaarn kevfqcevqs vnfqdpasac 151 dainfwvkne trgmidnlls pnlidsaltk lvlvnavyfk glwksrfqpe 201 ntkkrtfvag dgksyqvpml aqlsvfrsgs tktpnglwyn fielpyhges 251 ismlialpte sstplsaiip histktinsw mntmvpkrmq lvlpkftala 301 qtdlkeplka lgitemfeps kanfakitrs eslhvshilq kakievsedg 351 tkaavvttai liarssppwf ivdrpflfci rhnptgailf lgqvnkp
89313 --------------------------------------------------- Definition uteroferrin-associated protein precursor - pig Protein Name: uteroferrin-associated 89313: [ Whole ] protein precursor PIR Name: A34722 NCBI Seq ID: 89313 Created Mar 31, 1991 Updated Nov 22, 1996 Citation P.V. Malathy, K. Imakawa, R.C. Simmen & R.M. Roberts (1990). Molecular cloning of the uteroferrin-associated protein, a major progesterone-induced serpin secreted by the porcine uterus, and the expression of its mRNA during pregnancy. Mol. Endocrinol. 4, 428-440. MEDLINE identifier: 90258936 domain signal sequence 89313: 1..25 product uteroferrin-associated protein 89313: 26..417 Sequence 417 aa 1 mshgkmplvl slvlilcglf nsiscekqqt spktitpvsf kriaalsqkm 51 eanykafaqe lfktlliedp rknmifspvs isislatlsl glrsatrtna 101 idvldvalkn lavmlmaqap talleivhel vnrtakhqdi lidrtemnqm 151 flkeidryik mdiqmidfkd kektkkainq fvadkidkka knlithldpq 201 tllclvnyif fkgilerafq tnltkkedff vnektivqvd mmrktermiy 251 srseellatm vkipckenas iilvlpdtgk fnfalkemaa krarlqktnd 301 frlvhlvvpk ikdnlqdrfk hllpkigind ifttkavtwn ttgtstilea 351 vhhavievke dgltknaakd kdfwkvpvdk kevpvvvkfd rpfflfvede 401 itrrdlfvak vfnpkte
68735 --------------------------------------------------- Definition plasminogen activator inhibitor-1 precursor - human Protein Names: plasminogen activator 68735: [ Whole ] inhibitor-1 precursor; PAI-1; plasminogen activator inhibitor, endothelial-cell type PIR Name: ITHUP1 NCBI Seq ID: 68735 Comment Three types of PAI have been identified. PAI-1 is an acid- stable glycoprotein found in plasma and platelets and in endothelial, hepatoma, and fibrosarcoma cells. Vascular endothelial cells may be the primary site of synthesis of plasma PAI. Created Mar 31, 1988 Updated Nov 22, 1996 Citation P.J. Bosma, E.A. van den Berg, T. Kooistra, D.R. Siemieniak & J.L. Slightom (1988). Human plasminogen activator inhibitor-1 gene. Promoter and structural gene nucleotide sequences. J. Biol. Chem. 263, 9129-9141. MEDLINE identifier: 88243790 Citation L. Strandberg, D. Lawrence & T. Ny (1988). The organization of the human-plasminogen-activator-inhibitor-1 gene. Implications on the evolution of the serine-protease inhibitor family. Eur. J. Biochem. 176, 609-616. MEDLINE identifier: 89005111 Citation D.J. Loskutoff, M. Linders, J. Keijer, H. Veerman, H. van Heerikhuizen & H. Pannekoek (1987). Structure of the human plasminogen activator inhibitor 1 gene: nonrandom distribution of introns. Biochemistry 26, 3763-3768. MEDLINE identifier: 88000586 Citation H. Pannekoek, H. Veerman, H. Lambers, P. Diergaarde, C.L. Verweij, A.J. van Zonneveld & J.A. van Mourik (1986). Endothelial plasminogen activator inhibitor (PAI): a new member of the Serpin gene family. EMBO J. 5, 2539-2544. MEDLINE identifier: 87053819 Citation D. Ginsburg, R. Zeheb, A.Y. Yang, U.M. Rafferty, P.A. Andreasen, L. Nielsen, K. Dano, R.V. Lebo & T.D. Gelehrter (1986). cDNA cloning of human plasminogen activator-inhibitor from endothelial cells. J. Clin. Invest. 78, 1673-1680. MEDLINE identifier: 87058123 Citation M. Follo & D. Ginsburg (1989). Structure and expression of the human gene encoding plasminogen activator inhibitor, PAI- 1. Gene 84, 447-453. MEDLINE identifier: 90128289 Citation T.C. Wun & K.K. Kretzmer (1987). cDNA cloning and expression in E. coli of a plasminogen activator inhibitor (PAI) related to a PAI produced by Hep G2 hepatoma cell. FEBS Lett. 210, 11- 16. MEDLINE identifier: 87105925 Citation T. Ny, M. Sawdey, D. Lawrence, J.L. Millan & D.J. Loskutoff (1986). Cloning and sequence of a cDNA coding for the human beta-migrating endothelial-cell-type plasminogen activator inhibitor. Proc. Natl. Acad. Sci. U.S.A. 83, 6776-6780. MEDLINE identifier: 86313660 Citation P.A. Andreasen, A. Riccio, K.G. Welinder, R. Douglas, R. Sartorio, L.S. Nielsen, C. Oppenheimer, F. Blasi & K. Dano (1986). Plasminogen activator inhibitor type-1: reactive center and amino-terminal heterogeneity determined by protein and cDNA sequencing. FEBS Lett. 209, 213-218. MEDLINE identifier: 87080762 Citation W.E. Laug, R. Aebersold, A. Jong, W. Rideout, B.L. Bergman & J. Baker (1989). Isolation of multiple types of plasminogen activator inhibitors from vascular smooth muscle cells. Thromb. Haemost. 61, 517-521. MEDLINE identifier: 90020174 Citation A.J. van Zonneveld, S.A. Curriden & D.J. Loskutoff (1988). Type 1 plasminogen activator inhibitor gene: functional analysis and glucocorticoid regulation of its promoter. Proc. Natl. Acad. Sci. U.S.A. 85, 5525-5529. MEDLINE identifier: 88289754 domain signal sequence 68735: 1..23 product plasminogen activator inhibitor-1 68735: 24..402 (experimentally determined) binding site carbohydrate (Asn) (covalent) 68735: 232 binding site carbohydrate (Asn) (covalent) 68735: 288 binding site carbohydrate (Asn) (covalent) 68735: 352 inhibit site Arg (plasminogen activator) 68735: 369 Sequence 402 aa 1 mqmspaltcl vlglalvfge gsavhhppsy vahlasdfgv rvfqqvaqas 51 kdrnvvfspy gvasvlamlq lttggetqqq iqaamgfkid dkgmapalrh 101 lykelmgpwn kdeisttdai fvqrdlklvq gfmphffrlf rstvkqvdfs 151 everarfiin dwvkthtkgm isnllgkgav dqltrlvlvn alyfngqwkt 201 pfpdssthrr lfhksdgstv svpmmaqtnk fnytefttpd ghyydilelp 251 yhgdtlsmfi aapyekevpl saltnilsaq lishwkgnmt rlprllvlpk 301 fsletevdlr kplenlgmtd mfrqfqadft slsdqeplhv aqalqkvkie 351 vnesgtvass stavivsarm apeeiimdrp flfvvrhnpt gtvlfmgqvm 401 ep
2144575 --------------------------------------------------- Definition heat shock protein Hsp47 precursor - mouse Protein Names: heat shock protein Hsp47 2144575: [ Whole ] precursor; collagen-specific molecular chaperone, 47K; colligin; gp46; serine proteinase inhibitor homolog J6 PIR Name: A42843 NCBI Seq ID: 2144575 Comment This stress-induced glycoprotein of the ER lumen belongs to the serpin (serine protease inhibitor) superfamily but lacks protease inhibitor activity. Created Sep 30, 1993 Updated Nov 15, 1996 Citation H. Takechi, K. Hirayoshi, A. Nakai, H. Kudo, S. Saga & K. Nagata (1992). Molecular cloning of a mouse 47-kDa heat-shock protein (HSP47), a collagen-binding stress protein, and its expression during the differentiation of F9 teratocarcinoma cells. Eur. J. Biochem. 206, 323-329. MEDLINE identifier: 92283255 Citation N. Hosokawa, H. Takechi, S. Yokota, K. Hirayoshi & K. Nagata (1993). Structure of the gene encoding the mouse 47-kDa heat- shock protein (HSP47). Gene 126, 187-193. MEDLINE identifier: 93246243 Citation S.Y. Wang & L.J. Gudas (1991). A retinoic acid-inducible mRNA from F9 teratocarcinoma cells encodes a novel protease inhibitor homolog. J. Biol. Chem. 266, 14135. MEDLINE identifier: 91310706 Citation S.Y. Wang & L.J. Gudas (1990). A retinoic acid-inducible mRNA from F9 teratocarcinoma cells encodes a novel protease inhibitor homologue. J. Biol. Chem. 265, 15818-15822. MEDLINE identifier: 90368798 Citation S.Y. Wang (1992). Structure of the gene and its retinoic acid- regulatory region for murine J6 serpin. An F9 teratocarcinoma cell retinoic acid-inducible protein. J. Biol. Chem. 267, 15362-15366. MEDLINE identifier: 92348381 Citation K. Nagata (1996). Hsp47: a collagen-specific molecular chaperone. Trends Biochem. Sci. 21, 23-26. domain signal sequence 2144575: 1..17 product heat shock protein Hsp47 2144575: 18..417 region endoplasmic reticulum retention 2144575: 414..417 signal binding site carbohydrate (Asn) (covalent) 2144575: 119 binding site carbohydrate (Asn) (covalent) 2144575: 124 binding site carbohydrate (Asn) (covalent) 2144575: 394 Sequence 417 aa 1 mrslllgtlc llavalaaev kkpleaaapg taeklsskat tlaerstgla 51 fslyqamakd qavenillsp lvvasslglv slggkattas qakavlsaek 101 lrdeevhtgl gellrslsns tarnvtwklg srlygpssvs faddfvrssk 151 qhyncehski nfrdkrsalq sinewasqtt dgklpevtkd vertdgallv 201 namffkphwd erfhhrmvdn rgfmvtrsyt vgvtmmhrtg lynyyddeke 251 klqmvempla hklssliilm phhveplerl eklltkeqlk awmgkmqkka 301 vaislpkgvv evthdlqkhl aglglteaid knkadlsrms gkkdlylasv 351 fhatafewdt egnpfdqdiy greelrspkl fyadhpfifl vrdnqsgsll 401 figrlvrpkg dkmrdel
284550 --------------------------------------------------- Definition leukocyte elastase inhibitor - horse Protein Names: leukocyte elastase 284550: [ Whole ] inhibitor; plasminogen activator inhibitor-2 homolog PIR Name: A42421 NCBI Seq ID: 284550 Created Mar 4, 1993 Updated Nov 15, 1996 Citation A. Dubin, J. Travis, J.J. Enghild & J. Potempa (1992). Equine leukocyte elastase inhibitor. Primary structure and identification as a thymosin-binding protein. J. Biol. Chem. 267, 6576-6583. MEDLINE identifier: 92202200 Citation T. Kordula, A. Dubin, H. Schooltink, A. Koj, P.C. Heinrich & S. Rose-John (1993). Molecular cloning and expression of an intracellular serpin: an elastase inhibitor from horse leucocytes. Biochem. J. 293, 187-193. MEDLINE identifier: 93319507 Sequence 379 aa 1 meqlstanth favdlfraln esdptgnifi splsissala miflgtrgnt 51 aaqvskalyf dtvedihsrf qslnadinkp gapyilklan rlygektynf 101 ladflastqk mygaelasvd fqqapedark einewvkgqt egkipellvk 151 gmvdnmtklv lvnaiyfkgn wqekfmkeat rdapfrlnkk dtktvkmmyq 201 kkkfpynyie dlkcrvlelp yqgkelsmii llpddiedes tglekiekql 251 tleklrewtk penlylaevn vhlprfklee sydltshlar lgvqdlfnrg 301 kadlsgmsga rdlfvskiih ksfvdlneeg teaaaatagt imlamlmpee 351 nfnadhpfif firhnpsani lflgrfssp
105724 --------------------------------------------------- Definition heat shock protein Hsp47 precursor - human Protein Names: heat shock protein Hsp47 105724: [ Whole ] precursor; chaperonin; collagen- binding protein; colligin PIR Name: S20608 NCBI Seq ID: 105724 Comment This stress-induced glycoprotein of the ER lumen belongs to the serpin (serine protease inhibitor) superfamily but lacks protease inhibitor activity. Created Nov 22, 1993 Updated Nov 15, 1996 Citation E.P. Clarke & B.D. Sanwal (1992). Cloning of a human collagen- binding protein, and its homology with rat gp46, chick hsp47 and mouse J6 proteins. Biochim. Biophys. Acta 1129, 246-248. MEDLINE identifier: 92110393 Citation K. Nagata (1996). Hsp47: a collagen-specific molecular chaperone. Trends Biochem. Sci. 21, 23-26. domain signal sequence 105724: 1..17 product heat shock protein Hsp47 105724: 18..417 region endoplasmic reticulum retention 105724: 414..417 signal binding site carbohydrate (Asn) (covalent) 105724: 119 binding site carbohydrate (Asn) (covalent) 105724: 124 Sequence 417 aa 1 mrslllgtlc llavalaaev kkpveaaapg taeklsskat tlaepstgla 51 fslyqamakd qavenilvsp vvvasslglv slggkattas qakavlsaeq 101 lrdeevhagl gellrslsns tarnvtwklg srlygpssvs faddfvrssk 151 qhyncehski nfpdkrsalq sinewaaqtt dgklpevtkd vertdgallv 201 namffkphwd ekfhhkmvdn rgfmvtrsyt vgvtmmhrtg lynyyddeke 251 klqlvempla hklssliilm phhveplerl eklltkeqlk iwmgkmqkka 301 vaislpkgvv evthdlqkhl aglglteaid knkadlsrms gkkdlylasv 351 fhatafeldt dgnpfdqdiy greelrspkl fyadhpfifl vrdtqsgsll 401 figrlvrlkg dkmrdel
104687 --------------------------------------------------- Definition heat shock protein 47 precursor - chicken Protein Name: heat shock protein 47 104687: [ Whole ] precursor PIR Name: A41252 NCBI Seq ID: 104687 Comment This stress-induced glycoprotein of the ER lumen belongs to the serpin (serine protease inhibitor) superfamily but lacks protease inhibitor activity. Created Apr 3, 1992 Updated Nov 15, 1996 Citation K. Hirayoshi, H. Kudo, H. Takechi, A. Nakai, A. Iwamatsu, K.M. Yamada & K. Nagata (1991). HSP47: a tissue-specific, transformation-sensitive, collagen-binding heat shock protein of chicken embryo fibroblasts. Mol. Cell. Biol. 11, 4036- 4044. MEDLINE identifier: 91304395 Citation K. Nagata, S. Saga & K.M. Yamada (1988). Characterization of a novel transformation-sensitive heat-shock protein (HSP47) that binds to collagen. Biochem. Biophys. Res. Commun. 153, 428-434. MEDLINE identifier: 88240438 Citation K. Nagata (1996). Hsp47: a collagen-specific molecular chaperone. Trends Biochem. Sci. 21, 23-26. domain signal sequence 104687: 1..15 region endoplasmic reticulum retention 104687: 402..405 signal Sequence 405 aa 1 mqiflvlalc glaaavpsed rklsdkattl adrsttlafn lyhamakdkn 51 menillspvv vasslglvsl ggkattasqa kavlsadkln ddyvhsglse 101 llnevsnsta rnvtwkignr lygpasinfa ddfvknskkh ynyehskinf 151 rdkrsalksi newaaqttdg klpevtkdve ktdgalivna mffkphwdek 201 fhhkmvdnrg fmvtrsytvg vpmmhrtgly nyyddeaekl qvvemplahk 251 lssmifimpn hveplervek llnreqlktw askmkkrsva islpkvvlev 301 shdlqkhlad lglteaidkt kadlskisgk kdlylsnvfh aaalewdtdg 351 npydadiygr eemrnpklfy adhpfifmik dsktnsilfi grlvrpkgdk 401 mrdel
91903 --------------------------------------------------- Definition heat shock protein 47 precursor - rat Protein Names: heat shock protein 47 91903: [ Whole ] precursor; collagen-binding glycoprotein gp46; colligin; serine proteinase inhibitor homolog PIR Name: A40968 NCBI Seq ID: 91903 Comment This stress-induced glycoprotein of the ER lumen belongs to the serpin (serine protease inhibitor) superfamily but lacks protease inhibitor activity. Created Jul 17, 1992 Updated Nov 15, 1996 Citation E.P. Clarke, G.A. Cates, E.H. Ball & B.D. Sanwal (1991). A collagen-binding protein in the endoplasmic reticulum of myoblasts exhibits relationship with serine protease inhibitors. J. Biol. Chem. 266, 17230-17235. MEDLINE identifier: 91373337 Citation D. Nandan, G.A. Cates, E.H. Ball & B.D. Sanwal (1990). Partial characterization of a collagen-binding, differentiation-related glycoprotein from skeletal myoblasts. Arch. Biochem. Biophys. 278, 291-296. MEDLINE identifier: 90225795 Citation K. Nagata (1996). Hsp47: a collagen-specific molecular chaperone. Trends Biochem. Sci. 21, 23-26. domain signal sequence 91903: 1..17 product heat shock protein Hsp47 91903: 18..417 region endoplasmic reticulum retention 91903: 414..417 signal binding site carbohydrate (Asn) (covalent) 91903: 119 binding site carbohydrate (Asn) (covalent) 91903: 124 binding site carbohydrate (Asn) (covalent) 91903: 394 Sequence 417 aa 1 mrslllgtlc llavalaaev kkpveaaapg taeklsskat tlaerstgla 51 fslyqamakd qavenillsp lvvasslglv slggkattas qakavlsaek 101 lrdeevhtgl gelvrslsns tarnvtwklg srlygpssvs faddfvrssk 151 qhyncehski nfrdkrsalq sinewasqtt dgklpevtkd vertdgallv 201 namffkphwd ekfhhkmvdn rgfmvtrsyt vgvtmmhrtg lynyyddeke 251 klqlvempla hklssliilm phhveplerl eklltkeqlk twmgkmqkka 301 vaislpkgvv evthdlqkhl aglglteaid knkadlsrms gkkdlylasv 351 fhatafewdt egnpfdqdiy greelrspkl fyadhpfifl vrdnqsgsll 401 figrlvrpkg dkmrdel
1197577 --------------------------------------------------- Protein 1197577: 2..397 (experimentally determined) Protein Name: serpin 1197577: [ Whole ] NCBI Seq ID: 1197577 Updated Nov 14, 1996 Citation REF [1] S.K. Rasmussen, J. Klausen, J. Hejgaard, B. Svensson & I. Svendsen (1996). Primary structure of the plant serpin BSZ7 having the capacity of chymotrypsin inhibition. Biochim. Biophys. Acta 1297, 127-130. MEDLINE identifier: 97075187 Citation REF [2] Data Submission: S.K. Rasmussen (1996). Coding region 1197576: 30..1223 (experimentally determined) Sequence 397 aa 1 mattlttdlr lsiahqtrfg lrlasaissd pesaatnvaf spvslhvals 51 lvaagargat rdqlvavlgg ggageaealq slaeqvvqfv ladasinsgp 101 riafangvfv daslslkpsf qelavcnyks evqsvdfktk apeaasqvns 151 wvknvtagli eeilpagsid nttrlvlgna lyfkglwtkk fdesktkydd 201 fhllngstvq tpfmsstnkq ylsssdglkv lklpyqhggd nrqfsmyill 251 peahdglsrl aqklstepdf lenripteev evgqfmlpkf kisfgfeank 301 llktlglqlp fsleanlsem vnspmglyis svfhktfvev deegtkagaa 351 tgdvivdrsl pirmdfvanh pflfliredi agvvlfighv anpavss
1378133 --------------------------------------------------- Definition serpin 1 Protein Name: serpin 1 1378133: [ Whole ] NCBI Seq ID: 1378133 Citation H. Jiang, Y. Wang, Y. Huang, A.B. Mulnix, J. Kadel, K. Cole & M.R. Kanost (1996). Organization of serpin gene-1 from Manduca sexta. Evolution of a family of alternate exons encoding the reactive site loop. J. Biol. Chem. 271, 28017- 28023. MEDLINE identifier: 97067009 Citation Data Submission: H. Jiang, Y. Wang, Y. Huang, A.B. Mulnix, J. Kadel, K. Cole & M.R. Kanost (1996). Updated Nov 7, 1996 Coding region Comments: from mRNA with 1378121: 863..881 alternative exon 9B. 1378121: 2896..2990 1378121: 3647..3790 1378121: 4668..4871 1378121: 5163..5261 1378121: 5769..5909 1378121: 5998..6207 1378121: 6553..6697 1378121: 8174..8295 Sequence 392 aa 1 mkiimcifgl aalamagetd lqkilresnd qftaqmfsev vkanpgqnvv 51 lsafsvlppl gqlalasvge shdellrala lpndnvtkdv fadlnrgvra 101 vkgvdlkmas kiyvakglel nddfaavsrd vfgsevqnvd fvksveaaga 151 inkwvedqtn nriknlvdpd aldettrsvl vnaiyfkgsw kdkfvkertm 201 drdfhvskdk tikvptmigk kdvryadvpe ldakmiemsy egdqasmiii 251 lpnqvdgita leqklkdpka lsraeerlyn teveiylpkf kietttdlke 301 vlsnmnikkl ftpgaarlen llktkeslyv daaiqkafie vneegaeaaa 351 anafgivpas lilypevhid rpfyfelkid gipmfngkvi ep
1378132 --------------------------------------------------- Definition serpin 1 Protein Name: serpin 1 1378132: [ Whole ] NCBI Seq ID: 1378132 Citation H. Jiang, Y. Wang, Y. Huang, A.B. Mulnix, J. Kadel, K. Cole & M.R. Kanost (1996). Organization of serpin gene-1 from Manduca sexta. Evolution of a family of alternate exons encoding the reactive site loop. J. Biol. Chem. 271, 28017- 28023. MEDLINE identifier: 97067009 Citation Data Submission: H. Jiang, Y. Wang, Y. Huang, A.B. Mulnix, J. Kadel, K. Cole & M.R. Kanost (1996). Updated Nov 7, 1996 Coding region Comments: from mRNA with 1378121: 863..881 alternative exon 9A. 1378121: 2896..2990 1378121: 3647..3790 1378121: 4668..4871 1378121: 5163..5261 1378121: 5769..5909 1378121: 5998..6207 1378121: 6553..6697 1378121: 7751..7869 Sequence 391 aa 1 mkiimcifgl aalamagetd lqkilresnd qftaqmfsev vkanpgqnvv 51 lsafsvlppl gqlalasvge shdellrala lpndnvtkdv fadlnrgvra 101 vkgvdlkmas kiyvakglel nddfaavsrd vfgsevqnvd fvksveaaga 151 inkwvedqtn nriknlvdpd aldettrsvl vnaiyfkgsw kdkfvkertm 201 drdfhvskdk tikvptmigk kdvryadvpe ldakmiemsy egdqasmiii 251 lpnqvdgita leqklkdpka lsraeerlyn teveiylpkf kietttdlke 301 vlsnmnikkl ftpgaarlen llktkeslyv daaiqkafie vneegaeaaa 351 anaffitrqa rldiryfvan kpfifllrfn glalfngvfk a
1378131 --------------------------------------------------- Definition serpin 1 Protein Name: serpin 1 1378131: [ Whole ] NCBI Seq ID: 1378131 Citation H. Jiang, Y. Wang, Y. Huang, A.B. Mulnix, J. Kadel, K. Cole & M.R. Kanost (1996). Organization of serpin gene-1 from Manduca sexta. Evolution of a family of alternate exons encoding the reactive site loop. J. Biol. Chem. 271, 28017- 28023. MEDLINE identifier: 97067009 Citation Data Submission: H. Jiang, Y. Wang, Y. Huang, A.B. Mulnix, J. Kadel, K. Cole & M.R. Kanost (1996). Updated Nov 7, 1996 Coding region Comments: from mRNA with 1378121: 863..881 alternative exon 9D. 1378121: 2896..2990 1378121: 3647..3790 1378121: 4668..4871 1378121: 5163..5261 1378121: 5769..5909 1378121: 5998..6207 1378121: 6553..6697 1378121: 9756..9886 Sequence 395 aa 1 mkiimcifgl aalamagetd lqkilresnd qftaqmfsev vkanpgqnvv 51 lsafsvlppl gqlalasvge shdellrala lpndnvtkdv fadlnrgvra 101 vkgvdlkmas kiyvakglel nddfaavsrd vfgsevqnvd fvksveaaga 151 inkwvedqtn nriknlvdpd aldettrsvl vnaiyfkgsw kdkfvkertm 201 drdfhvskdk tikvptmigk kdvryadvpe ldakmiemsy egdqasmiii 251 lpnqvdgita leqklkdpka lsraeerlyn teveiylpkf kietttdlke 301 vlsnmnikkl ftpgaarlen llktkeslyv daaiqkafie vneegaeaaa 351 anvvrgirpr psvrpptpkf eadrpflfym ktndqtlfng icmqp
1378130 --------------------------------------------------- Definition serpin 1 Protein Name: serpin 1 1378130: [ Whole ] NCBI Seq ID: 1378130 Citation H. Jiang, Y. Wang, Y. Huang, A.B. Mulnix, J. Kadel, K. Cole & M.R. Kanost (1996). Organization of serpin gene-1 from Manduca sexta. Evolution of a family of alternate exons encoding the reactive site loop. J. Biol. Chem. 271, 28017- 28023. MEDLINE identifier: 97067009 Citation Data Submission: H. Jiang, Y. Wang, Y. Huang, A.B. Mulnix, J. Kadel, K. Cole & M.R. Kanost (1996). Updated Nov 7, 1996 Coding region Comments: from mRNA with 1378121: 863..881 alternative exon 9J. 1378121: 2896..2990 1378121: 3647..3790 1378121: 4668..4871 1378121: 5163..5261 1378121: 5769..5909 1378121: 5998..6207 1378121: 6553..6697 1378121: 16395..16531 Sequence 397 aa 1 mkiimcifgl aalamagetd lqkilresnd qftaqmfsev vkanpgqnvv 51 lsafsvlppl gqlalasvge shdellrala lpndnvtkdv fadlnrgvra 101 vkgvdlkmas kiyvakglel nddfaavsrd vfgsevqnvd fvksveaaga 151 inkwvedqtn nriknlvdpd aldettrsvl vnaiyfkgsw kdkfvkertm 201 drdfhvskdk tikvptmigk kdvryadvpe ldakmiemsy egdqasmiii 251 lpnqvdgita leqklkdpka lsraeerlyn teveiylpkf kietttdlke 301 vlsnmnikkl ftpgaarlen llktkeslyv daaiqkafie vneegaeaaa 351 anafiltdrc csdyddnief dvnrpfylnl rtnehllfsg iciqpei
1378129 --------------------------------------------------- Definition serpin 1 Protein Name: serpin 1 1378129: [ Whole ] NCBI Seq ID: 1378129 Citation H. Jiang, Y. Wang, Y. Huang, A.B. Mulnix, J. Kadel, K. Cole & M.R. Kanost (1996). Organization of serpin gene-1 from Manduca sexta. Evolution of a family of alternate exons encoding the reactive site loop. J. Biol. Chem. 271, 28017- 28023. MEDLINE identifier: 97067009 Citation Data Submission: H. Jiang, Y. Wang, Y. Huang, A.B. Mulnix, J. Kadel, K. Cole & M.R. Kanost (1996). Updated Nov 7, 1996 Coding region Comments: from mRNA with 1378121: 863..881 alternative exon 9C. 1378121: 2896..2990 1378121: 3647..3790 1378121: 4668..4871 1378121: 5163..5261 1378121: 5769..5909 1378121: 5998..6207 1378121: 6553..6697 1378121: 8769..8899 Sequence 395 aa 1 mkiimcifgl aalamagetd lqkilresnd qftaqmfsev vkanpgqnvv 51 lsafsvlppl gqlalasvge shdellrala lpndnvtkdv fadlnrgvra 101 vkgvdlkmas kiyvakglel nddfaavsrd vfgsevqnvd fvksveaaga 151 inkwvedqtn nriknlvdpd aldettrsvl vnaiyfkgsw kdkfvkertm 201 drdfhvskdk tikvptmigk kdvryadvpe ldakmiemsy egdqasmiii 251 lpnqvdgita leqklkdpka lsraeerlyn teveiylpkf kietttdlke 301 vlsnmnikkl ftpgaarlen llktkeslyv daaiqkafie vneegaeaaa 351 anaffiiesy ssyepvvpvf didkpfyfni rangqslfng lcfqp
1378128 --------------------------------------------------- Definition serpin 1 Protein Name: serpin 1 1378128: [ Whole ] NCBI Seq ID: 1378128 Citation H. Jiang, Y. Wang, Y. Huang, A.B. Mulnix, J. Kadel, K. Cole & M.R. Kanost (1996). Organization of serpin gene-1 from Manduca sexta. Evolution of a family of alternate exons encoding the reactive site loop. J. Biol. Chem. 271, 28017- 28023. MEDLINE identifier: 97067009 Citation Data Submission: H. Jiang, Y. Wang, Y. Huang, A.B. Mulnix, J. Kadel, K. Cole & M.R. Kanost (1996). Updated Nov 7, 1996 Coding region Comments: from mRNA with 1378121: 863..881 alternative exon 9Z. 1378121: 2896..2990 1378121: 3647..3790 1378121: 4668..4871 1378121: 5163..5261 1378121: 5769..5909 1378121: 5998..6207 1378121: 6553..6697 1378121: 19262..19383 Sequence 392 aa 1 mkiimcifgl aalamagetd lqkilresnd qftaqmfsev vkanpgqnvv 51 lsafsvlppl gqlalasvge shdellrala lpndnvtkdv fadlnrgvra 101 vkgvdlkmas kiyvakglel nddfaavsrd vfgsevqnvd fvksveaaga 151 inkwvedqtn nriknlvdpd aldettrsvl vnaiyfkgsw kdkfvkertm 201 drdfhvskdk tikvptmigk kdvryadvpe ldakmiemsy egdqasmiii 251 lpnqvdgita leqklkdpka lsraeerlyn teveiylpkf kietttdlke 301 vlsnmnikkl ftpgaarlen llktkeslyv daaiqkafie vneegaeaaa 351 anafgiayls avirspvfna dhpfvfflrq dkttlfsgvf qs
1378127 --------------------------------------------------- Definition serpin 1 Protein Name: serpin 1 1378127: [ Whole ] NCBI Seq ID: 1378127 Citation H. Jiang, Y. Wang, Y. Huang, A.B. Mulnix, J. Kadel, K. Cole & M.R. Kanost (1996). Organization of serpin gene-1 from Manduca sexta. Evolution of a family of alternate exons encoding the reactive site loop. J. Biol. Chem. 271, 28017- 28023. MEDLINE identifier: 97067009 Citation Data Submission: H. Jiang, Y. Wang, Y. Huang, A.B. Mulnix, J. Kadel, K. Cole & M.R. Kanost (1996). Updated Nov 7, 1996 Coding region Comments: from mRNA with 1378121: 863..881 alternative exon 9I. 1378121: 2896..2990 1378121: 3647..3790 1378121: 4668..4871 1378121: 5163..5261 1378121: 5769..5909 1378121: 5998..6207 1378121: 6553..6697 1378121: 15070..15200 Sequence 395 aa 1 mkiimcifgl aalamagetd lqkilresnd qftaqmfsev vkanpgqnvv 51 lsafsvlppl gqlalasvge shdellrala lpndnvtkdv fadlnrgvra 101 vkgvdlkmas kiyvakglel nddfaavsrd vfgsevqnvd fvksveaaga 151 inkwvedqtn nriknlvdpd aldettrsvl vnaiyfkgsw kdkfvkertm 201 drdfhvskdk tikvptmigk kdvryadvpe ldakmiemsy egdqasmiii 251 lpnqvdgita leqklkdpka lsraeerlyn teveiylpkf kietttdlke 301 vlsnmnikkl ftpgaarlen llktkeslyv daaiqkafie vneegaeaaa 351 anefgivals lefslneikf vvnkpfyfni rsngqhlfng icfqp
1378126 --------------------------------------------------- Definition serpin 1 Protein Name: serpin 1 1378126: [ Whole ] NCBI Seq ID: 1378126 Citation H. Jiang, Y. Wang, Y. Huang, A.B. Mulnix, J. Kadel, K. Cole & M.R. Kanost (1996). Organization of serpin gene-1 from Manduca sexta. Evolution of a family of alternate exons encoding the reactive site loop. J. Biol. Chem. 271, 28017- 28023. MEDLINE identifier: 97067009 Citation Data Submission: H. Jiang, Y. Wang, Y. Huang, A.B. Mulnix, J. Kadel, K. Cole & M.R. Kanost (1996). Updated Nov 7, 1996 Coding region Comments: from mRNA with 1378121: 863..881 alternative exon 9G. 1378121: 2896..2990 1378121: 3647..3790 1378121: 4668..4871 1378121: 5163..5261 1378121: 5769..5909 1378121: 5998..6207 1378121: 6553..6697 1378121: 13203..13336 Sequence 396 aa 1 mkiimcifgl aalamagetd lqkilresnd qftaqmfsev vkanpgqnvv 51 lsafsvlppl gqlalasvge shdellrala lpndnvtkdv fadlnrgvra 101 vkgvdlkmas kiyvakglel nddfaavsrd vfgsevqnvd fvksveaaga 151 inkwvedqtn nriknlvdpd aldettrsvl vnaiyfkgsw kdkfvkertm 201 drdfhvskdk tikvptmigk kdvryadvpe ldakmiemsy egdqasmiii 251 lpnqvdgita leqklkdpka lsraeerlyn teveiylpkf kietttdlke 301 vlsnmnikkl ftpgaarlen llktkeslyv daaiqkafie vneegaeaaa 351 anaffivgit siqfeppvie fhvnrpfffn lkasgqslfn gicvqp
1378125 --------------------------------------------------- Definition serpin 1 Protein Name: serpin 1 1378125: [ Whole ] NCBI Seq ID: 1378125 Citation H. Jiang, Y. Wang, Y. Huang, A.B. Mulnix, J. Kadel, K. Cole & M.R. Kanost (1996). Organization of serpin gene-1 from Manduca sexta. Evolution of a family of alternate exons encoding the reactive site loop. J. Biol. Chem. 271, 28017- 28023. MEDLINE identifier: 97067009 Citation Data Submission: H. Jiang, Y. Wang, Y. Huang, A.B. Mulnix, J. Kadel, K. Cole & M.R. Kanost (1996). Updated Nov 7, 1996 Coding region Comments: from mRNA with 1378121: 863..881 alternative exon 9E. 1378121: 2896..2990 1378121: 3647..3790 1378121: 4668..4871 1378121: 5163..5261 1378121: 5769..5909 1378121: 5998..6207 1378121: 6553..6697 1378121: 10908..11038 Sequence 395 aa 1 mkiimcifgl aalamagetd lqkilresnd qftaqmfsev vkanpgqnvv 51 lsafsvlppl gqlalasvge shdellrala lpndnvtkdv fadlnrgvra 101 vkgvdlkmas kiyvakglel nddfaavsrd vfgsevqnvd fvksveaaga 151 inkwvedqtn nriknlvdpd aldettrsvl vnaiyfkgsw kdkfvkertm 201 drdfhvskdk tikvptmigk kdvryadvpe ldakmiemsy egdqasmiii 251 lpnqvdgita leqklkdpka lsraeerlyn teveiylpkf kietttdlke 301 vlsnmnikkl ftpgaarlen llktkeslyv daaiqkafie vneegaeaaa 351 anvirvvkkk frvippvlkf hvdrpfffnl kandqslfng iclqp
1378124 --------------------------------------------------- Definition serpin 1 Protein Name: serpin 1 1378124: [ Whole ] NCBI Seq ID: 1378124 Citation H. Jiang, Y. Wang, Y. Huang, A.B. Mulnix, J. Kadel, K. Cole & M.R. Kanost (1996). Organization of serpin gene-1 from Manduca sexta. Evolution of a family of alternate exons encoding the reactive site loop. J. Biol. Chem. 271, 28017- 28023. MEDLINE identifier: 97067009 Citation Data Submission: H. Jiang, Y. Wang, Y. Huang, A.B. Mulnix, J. Kadel, K. Cole & M.R. Kanost (1996). Updated Nov 7, 1996 Coding region Comments: from mRNA with 1378121: 863..881 alternative exon 9K. 1378121: 2896..2990 1378121: 3647..3790 1378121: 4668..4871 1378121: 5163..5261 1378121: 5769..5909 1378121: 5998..6207 1378121: 6553..6697 1378121: 18218..18339 Sequence 392 aa 1 mkiimcifgl aalamagetd lqkilresnd qftaqmfsev vkanpgqnvv 51 lsafsvlppl gqlalasvge shdellrala lpndnvtkdv fadlnrgvra 101 vkgvdlkmas kiyvakglel nddfaavsrd vfgsevqnvd fvksveaaga 151 inkwvedqtn nriknlvdpd aldettrsvl vnaiyfkgsw kdkfvkertm 201 drdfhvskdk tikvptmigk kdvryadvpe ldakmiemsy egdqasmiii 251 lpnqvdgita leqklkdpka lsraeerlyn teveiylpkf kietttdlke 301 vlsnmnikkl ftpgaarlen llktkeslyv daaiqkafie vneegaeaaa 351 anafkitfys fhfvpkvein kpfffslkyn rnsmfsgvcv qp
1378123 --------------------------------------------------- Definition serpin 1 Protein Name: serpin 1 1378123: [ Whole ] NCBI Seq ID: 1378123 Citation H. Jiang, Y. Wang, Y. Huang, A.B. Mulnix, J. Kadel, K. Cole & M.R. Kanost (1996). Organization of serpin gene-1 from Manduca sexta. Evolution of a family of alternate exons encoding the reactive site loop. J. Biol. Chem. 271, 28017- 28023. MEDLINE identifier: 97067009 Citation Data Submission: H. Jiang, Y. Wang, Y. Huang, A.B. Mulnix, J. Kadel, K. Cole & M.R. Kanost (1996). Updated Nov 7, 1996 Coding region Comments: from mRNA with 1378121: 863..881 alternative exon 9F. 1378121: 2896..2990 1378121: 3647..3790 1378121: 4668..4871 1378121: 5163..5261 1378121: 5769..5909 1378121: 5998..6207 1378121: 6553..6697 1378121: 11768..11904 Sequence 397 aa 1 mkiimcifgl aalamagetd lqkilresnd qftaqmfsev vkanpgqnvv 51 lsafsvlppl gqlalasvge shdellrala lpndnvtkdv fadlnrgvra 101 vkgvdlkmas kiyvakglel nddfaavsrd vfgsevqnvd fvksveaaga 151 inkwvedqtn nriknlvdpd aldettrsvl vnaiyfkgsw kdkfvkertm 201 drdfhvskdk tikvptmigk kdvryadvpe ldakmiemsy egdqasmiii 251 lpnqvdgita leqklkdpka lsraeerlyn teveiylpkf kietttdlke 301 vlsnmnikkl ftpgaarlen llktkeslyv daaiqkafie vneegaeaaa 351 anafiavvds idifertief hadrpfffnl kangqslfng icvmpml
1378122 --------------------------------------------------- Definition serpin 1 Protein Name: serpin 1 1378122: [ Whole ] NCBI Seq ID: 1378122 Citation H. Jiang, Y. Wang, Y. Huang, A.B. Mulnix, J. Kadel, K. Cole & M.R. Kanost (1996). Organization of serpin gene-1 from Manduca sexta. Evolution of a family of alternate exons encoding the reactive site loop. J. Biol. Chem. 271, 28017- 28023. MEDLINE identifier: 97067009 Citation Data Submission: H. Jiang, Y. Wang, Y. Huang, A.B. Mulnix, J. Kadel, K. Cole & M.R. Kanost (1996). Updated Nov 7, 1996 Coding region Comments: from mRNA with 1378121: 863..881 alternative exon 9H. 1378121: 2896..2990 1378121: 3647..3790 1378121: 4668..4871 1378121: 5163..5261 1378121: 5769..5909 1378121: 5998..6207 1378121: 6553..6697 1378121: 13752..13891 Sequence 398 aa 1 mkiimcifgl aalamagetd lqkilresnd qftaqmfsev vkanpgqnvv 51 lsafsvlppl gqlalasvge shdellrala lpndnvtkdv fadlnrgvra 101 vkgvdlkmas kiyvakglel nddfaavsrd vfgsevqnvd fvksveaaga 151 inkwvedqtn nriknlvdpd aldettrsvl vnaiyfkgsw kdkfvkertm 201 drdfhvskdk tikvptmigk kdvryadvpe ldakmiemsy egdqasmiii 251 lpnqvdgita leqklkdpka lsraeerlyn teveiylpkf kietttdlke 301 vlsnmnikkl ftpgaarlen llktkeslyv daaiqkafie vneegaeaaa 351 anafityves idnfvptief dvnrpfyfnl kandlylfng icvqpklq
1613850 --------------------------------------------------- Protein Name: serine proteinase inhibitor 1613850: [ Whole ] Activities: protease inhibitor NCBI Seq ID: 1613850 Citation J. Sun, C.H. Bird, V. Sutton, L. McDonald, P.B. Coughlin, T.A. De Jong, J.A. Trapani & P.I. Bird (1996). A cytosolic granzyme B inhibitor related to the viral apoptotic regulator cytokine response modifier A is present in cytotoxic lymphocytes. J. Biol. Chem. 271, 27802-27809. MEDLINE identifier: 97066975 Citation Data Submission: P.I. Bird (1996). Updated Oct 31, 1996 Coding region Comments: serpin; granzyme B 1613849: 114..1244 inhibitor; cytoplasmic antiproteinase 3. Sequence 376 aa 1 metlsnasgt fairllkilc qdnpshnvfc spvsissala mvllgakgnt 51 atqmaqalsl nteedihraf qslltevnka gtqyllrtan rlfgektcqf 101 lstfkesclq fyhaelkels firaaeesrk hintwvskkt egkieellpg 151 ssidaetrlv lvnaiyfkgk wnepfdetyt rempfkinqe eqrpvqmmyq 201 eatfklahvg evraqllelp yarkelsllv llpddgvels tveksltfek 251 ltawtkpdcm kstevevllp kfklqedydm esvlrhlgiv dafqqgkadl 301 samsaerdlc lskfvhksfv evneegteaa aasscfvvae ccmesgprfc 351 adhpflffir hnransilfc grfssp
2143953 --------------------------------------------------- Definition regeneration associated serpin-1 - rat Protein Name: regeneration associated 2143953: [ Whole ] serpin-1 PIR Name: JC4841 NCBI Seq ID: 2143953 Comment This protein is liver-specific and associates liver regeneration. It belongs to serine protease inhibitor superfamily. Created Aug 15, 1996 Updated Oct 15, 1996 Citation L. New, K. Liu, V. Kamali, G. Plowman, B.A. Naughton & A.F. Purchio (1996). cDNA cloning of rasp-1, a novel gene encoding a plasma protein associated with liver regeneration. Biochem. Biophys. Res. Commun. 223, 404-412. MEDLINE identifier: 96264653 domain signal sequence 2143953: 1..20 Sequence 436 aa 1 mrvvsslflp vllaevwlvs sfnlsshtpe apirlvsqdy enqtweeyew 51 adprddneyw lrasqqlsne tssfgfsllr kismrhdgnv ifspfglsva 101 mvnlmlgakg etkvqvengl nlqalsqagp lilpalfkrv ketfssnkkl 151 gltqgsfafi hkdfeikkty fnlstmyfdt eyvptnfrns sqarglmnhy 201 inketegkip klfdeinpet klilvdyilf kgkwltpfdp ifteadtfhl 251 dkykavkvpm myregnfast fdkkfrchil klpyqgnatm lvvlmeksgd 301 hlaledyltt dlvemwlqdm ktrkmevffp kfklnqryem hellkqvgir 351 rifstsadls elsavarnlq vskvvqqsvl evdergtevv sgtvseitay 401 cmppvikvdr pfhfiiyeem srmllflgrv vnptvl
1729928 --------------------------------------------------- Definition THYROXINE-BINDING GLOBULIN PRECURSOR (T4-BINDING GLOBULIN). Protein Name: THYROXINE-BINDING GLOBULIN 1729928: 1..412 PRECURSOR SWISS-PROT Name: THBG_SHEEP, Accession: P50450 NCBI Seq ID: 1729928 Comment [FUNCTION] MAJOR THYROID HORMONE TRANSPORT PROTEIN IN SERUM. Comment [SUBCELLULAR LOCATION] EXTRACELLULAR. Comment [TISSUE SPECIFICITY] SYNTHESIZED IN THE LIVER; FOUND IN PLASMA. Comment [SIMILARITY] WITH SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 398825 Cross-ref EMBL Accession: X69795 Created Oct 1, 1996 Updated Oct 1, 1996 Citation REF [1] A. Tsykin & G. Schreiber (1993). Sheep thyroxine-binding globulin: cDNA sequence and expression. Mol. Cell. Endocrinol. 98, 91-97. MEDLINE identifier: 94192879 Signal 1729928: 1..16 Mature chain THYROXINE-BINDING GLOBULIN. 1729928: 17..412 (experimentally determined) glycosylation 1729928: 35 site glycosylation 1729928: 98 site glycosylation 1729928: 164 site glycosylation 1729928: 252 site Gene Locus: TBG 1729928: 1..412 Sequence 412 aa 1 mplffslvll ilglhcappn scegkitscl spqqnatlyk mssinadfaf 51 nlyrkvtvet pdqniffspv sisaglamls lgacsstqtq ileslgfnlt 101 dtpmaeiqqg fqhlicslnf pkkelelqmg nalfigkqlk plekflddvk 151 nlyetevfst dfsnvsaaqq einshverqt kgkivgliqd lkpntitvlv 201 nylcfkaqwa npfdpsktee gssflvdktt tvqvpmmhqv dqyyhlvdte 251 lnctvlqmdy sknalalfvl pkegqmegve gamsskilkk wnrllqkgwv 301 nlfvpkfsis atydlggill kmgiqdafad nadfsgltkd nglkvsnvah 351 kamfyigekg teaipevrfl nqpettllhp iiqfdrsfll lilekntrsi 401 lflgkvvdpt ev
1711495 --------------------------------------------------- Definition SERINE PROTEINASE INHIBITOR. Protein Name: SERINE PROTEINASE INHIBITOR 1711495: 1..10 *: Partial SWISS-PROT Name: SPI_HALRO, Accession: Q10997 NCBI Seq ID: 1711495 Comment [FUNCTION] STRONGLY INHIBITS TRYPSIN AND PLASMA ENZYME(S) ACTIVITY. Comment [SUBUNIT] MONOMER. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Created Oct 1, 1996 Updated Oct 1, 1996 Citation REF [1] F. SHISHIKURA, T. ABE, S.-I. OHTAKE & K. TANAKA (1996)COMP. BIOCHEM. PHYSIOL. 114B, 1-9. Sequence 10 aa 1 tkkdgeekva
1710877 --------------------------------------------------- Definition SQUAMOUS CELL CARCINOMA ANTIGEN 2 (SCCA-2) (LEUPIN). Protein Name: SQUAMOUS CELL CARCINOMA 1710877: 1..390 ANTIGEN 2 SWISS-PROT Name: SCC2_HUMAN, Accession: P48594 NCBI Seq ID: 1710877 Comment [FUNCTION] MAY ACT AS A PROTEASE INHIBITOR TO MODULATE THE HOST IMMUNE RESPONSE AGAINST TUMOR CELLS. Comment [SUBCELLULAR LOCATION] CYTOPLASMIC. Comment [TISSUE SPECIFICITY] SQUAMOUS CELLS. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. BELONGS TO THE OV-SERPIN SUBFAMILY. Cross-ref NCBI Seq ID: 1235617 Cross-ref NCBI Seq ID: 1052871 Cross-ref NCBI Seq ID: 887465 Cross-ref GenBank Accession: U19576 Cross-ref GenBank Accession: U19557 Cross-ref EMBL Accession: X89015 Cross-ref MIM 600518 Created Feb 1, 1996 Updated Oct 1, 1996 Citation REF [1] S.S. Schneider, C. Schick, K.E. Fish, E. Miller, J.C. Pena, S.D. Treter, S.M. Hui & G.A. Silverman (1995). A serine proteinase inhibitor locus at 18q21.3 contains a tandem duplication of the human squamous cell carcinoma antigen gene. Proc. Natl. Acad. Sci. U.S.A. 92, 3147-3151. MEDLINE identifier: 95241462 Citation REF [2] R.C. Barnes & D.M. Worrall (1995). Identification of a novel human serpin gene; cloning sequencing and expression of leupin. FEBS Lett. 373, 61-65. MEDLINE identifier: 96013887 active site REACTIVE BOND. 1710877: 354..355 (experimentally determined) Gene Locus: SCCA2 1710877: 1..390 Sequence 390 aa 1 mnslseantk fmfdlfqqfr kskennifys pisitsalgm vllgakdnta 51 qqiskvlhfd qvtentteka atyhvdrsgn vhhqfqkllt efnkstdaye 101 lkianklfge ktyqflqeyl daikkfyqts vestdfanap eesrkkinsw 151 vesqtnekik nlfpdgtign dttlvlvnai yfkgqwenkf kkentkeekf 201 wpnkntyksv qmmrqynsfn falledvqak vleipykgkd lsmivllpne 251 idglqkleek ltaeklmewt slqnmretcv dlhlprfkme esydlkdtlr 301 tmgmvnifng dadlsgmtws hglsvskvlh kafvevteeg veaaaatavv 351 vvelsspstn eefccnhpfl ffirqnktns ilfygrfssp
1709896 --------------------------------------------------- Definition CYTOPLASMIC ANTIPROTEINASE 3 (CAP3) (PROTEASE INHIBITOR 9). Protein Name: CYTOPLASMIC ANTIPROTEINASE 31709896: 1..376 SWISS-PROT Name: PTI9_HUMAN, Accession: P50453 NCBI Seq ID: 1709896 Comment [SUBCELLULAR LOCATION] CYTOPLASMIC. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. BELONGS TO THE OV-SERPIN SUBFAMILY. Cross-ref NCBI Seq ID: 1160929 Cross-ref GenBank Accession: L40378 Created Oct 1, 1996 Updated Oct 1, 1996 Citation REF [1] C.A. Sprecher, K.A. Morgenstern, S. Mathewes, J.R. Dahlen, S.K. Schrader, D.C. Foster & W. Kisiel (1995). Molecular cloning, expression, and partial characterization of two novel members of the ovalbumin family of serine proteinase inhibitors. J. Biol. Chem. 270, 29854-29861. MEDLINE identifier: 96102039 active site REACTIVE BOND. 1709896: 340..341 Gene Locus: PI9 1709896: 1..376 Sequence 376 aa 1 metlsnasgt fairllkilc qdnpshnvfc spvsissala mvllgakgnt 51 atqmaqalsl nteedihraf qslltevnka gtqyllrtan rlfgektcqf 101 lstfkesclq fyhaelkels firaaeesrk hintwvskkt egkieellpg 151 ssidaetrlv lvnaiyfkgk wnepfdetyt rempfkinqe eqrpvqmmyq 201 eatfklahvg evraqllelp yarkelsllv llpddgvels tveksltfek 251 ltawtkpdcm kstevevllp kfklqedydm esvlrhlgiv dafqqgkadl 301 samsaerdlc lskfvhksfv evneegteaa aasscfvvae ccmesgprfc 351 adhpflffir hnransilfc grfssp
1709895 --------------------------------------------------- Definition CYTOPLASMIC ANTIPROTEINASE 2 (CAP2) (PROTEASE INHIBITOR 8). Protein Name: CYTOPLASMIC ANTIPROTEINASE 21709895: 1..374 SWISS-PROT Name: PTI8_HUMAN, Accession: P50452 NCBI Seq ID: 1709895 Comment [SUBCELLULAR LOCATION] CYTOPLASMIC. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. BELONGS TO THE OV-SERPIN SUBFAMILY. Cross-ref NCBI Seq ID: 1160927 Cross-ref GenBank Accession: L40377 Created Oct 1, 1996 Updated Oct 1, 1996 Citation REF [1] C.A. Sprecher, K.A. Morgenstern, S. Mathewes, J.R. Dahlen, S.K. Schrader, D.C. Foster & W. Kisiel (1995). Molecular cloning, expression, and partial characterization of two novel members of the ovalbumin family of serine proteinase inhibitors. J. Biol. Chem. 270, 29854-29861. MEDLINE identifier: 96102039 active site REACTIVE BOND. 1709895: 339..340 Gene Locus: PI8 1709895: 1..374 Sequence 374 aa 1 mddlceangt faislfkilg eednsrnvff spmsissala mvfmgakgst 51 aaqmsqalcl ykdgdihrgf qsllsevnrt gtqyllrtan rlfgektcdf 101 lpdfkeycqk fyqaeleels faedteecrk hindwvaekt egkisevlda 151 gtvdpltklv lvnaiyfkgk wneqfdrkyt rgmlfktnee kktvqmmfke 201 akfkmgyade vhtqvlelpy veeelsmvil lpddntdlav vekaltyekf 251 kawtnseklt kskvqvflpr lkleesydle pflrrlgmid afdeakadfs 301 gmsteknvpl skvahkcfve vneegteaaa atavvrnsrc srmeprfcad 351 hpflffirrh ktncilfcgr fssp
1709561 --------------------------------------------------- Definition PLASMINOGEN ACTIVATOR INHIBITOR-1 PRECURSOR, ENDOTHELIAL (PAI- 1). Protein Name: PLASMINOGEN ACTIVATOR 1709561: 1..400 INHIBITOR-1 PRECURSOR, ENDOTHELIAL SWISS-PROT Name: PAI1_MUSVI, Accession: P50449 NCBI Seq ID: 1709561 Comment [FUNCTION] THIS INHIBITOR ACTS AS "BAIT" FOR TISSUE PLASMINOGEN ACTIVATOR, UROKINASE, AND PROTEIN C. ITS RAPID INTERACTION WITH TPA MAY FUNCTION AS A MAJOR CONTROL POINT IN THE REGULATION OF FIBRINOLYSIS. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 1164924 Cross-ref EMBL Accession: X58541 Created Oct 1, 1996 Updated Oct 1, 1996 Citation REF [1] T.H. Chuang, R.T. Hamilton & M. Nilsen-Hamilton (1995). Cloning of the mink plasminogen activator inhibitor type-1 messenger RNA: an mRNA with a short half life. Gene 162, 303- 308. MEDLINE identifier: 96032362 Signal 1709561: 1..21 Mature chain PLASMINOGEN ACTIVATOR INHIBITOR I. 1709561: 22..400 (experimentally determined) active site REACTIVE BOND. 1709561: 367..368 glycosylation 1709561: 230 site glycosylation 1709561: 286 site glycosylation 1709561: 350 site Gene Locus: PAI1 1709561: 1..400 Sequence 400 aa 1 mqmstvclal glalvfgeas asylhetraa elatdfgvkv fkqvaqaskd 51 rnmvfspygl asvlamlqlt tagetrqqiq eamrfqidek gmapalrqly 101 kelmgpwnkd eistadaifv qrdlklvhgf mpyffrlfqt tvkqvdfsev 151 erarfiindw vkrhtkgmig dllgrgtvdq ltrlmlvnal yfngqwktpf 201 pksgthhrlf hksdgstvsv pmmaqtnkfn ytefstpegr yydilelpyh 251 gdtlsmfiaa pyekdvplsa ltnildaqli sqwkgnmtrr lrllvlpkfs 301 lesevnlrgp lenlgmtdmf rpnqadfssl sdqealyvsq alqkvkievn 351 esgtvassst aiivsarmap eeiimdrpfl fvvrhnptgt vlfmgqvmep
1708609 --------------------------------------------------- Definition KALLISTATIN PRECURSOR (KALLIKREIN INHIBITOR) (PROTEASE INHIBITOR 4). Protein Name: KALLISTATIN PRECURSOR 1708609: 1..427 SWISS-PROT Name: KAIN_HUMAN, Accession: P29622 NCBI Seq ID: 1708609 Comment [FUNCTION] INHIBITS HUMAN AMIDOLYTIC AND KININOGENASE ACTIVITIES OF HUMAN TISSUE KALLIKREIN. INHIBITION IS ACHIEVED BY FORMATION OF AN EQUIMOLAR, HEAT- AND SDS-STABLE COMPLEX BETWEEN THE INHIBITOR AND THE ENZYME, AND GENERATION OF A SMALL C-TERMINAL FRAGMENT OF THE INHIBITOR DUE TO CLEAVAGE AT THE REACTIVE SITE BY TISSUE KALLIKREIN. Comment HEPARIN BLOCKS KALLISTATIN'S COMPLEX FORMATION WITH TISSUE KALLIKREIN AND ABOLISHES ITS INHIBITORY EFFECT ON TISSUE KALLIKREIN'S ACTIVITY. Comment [PTM] THE N-TERMINAL IS BLOCKED. Comment [SUBUNIT] MONOMER AND SOME HOMODIMERS. Comment [TISSUE SPECIFICITY] SECRETED FROM LIVER CELLS LINES. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 425146 Cross-ref NCBI Seq ID: 619783 Cross-ref GenBank Accession: L19684 Cross-ref GenBank Accession: L28101 Cross-ref MIM 147935 Cross-ref PROSITE PS00284 Created Apr 1, 1993 Updated Oct 1, 1996 Citation REF [1] K.X. Chai, L.M. Chen, J. Chao & L. Chao (1993). Kallistatin: a novel human serine proteinase inhibitor. Molecular cloning, tissue distribution, and expression in Escherichia coli. J. Biol. Chem. 268, 24498-24505. MEDLINE identifier: 94043294 Citation REF [2] K.X. Chai, D.C. Ward, J. Chao & L. Chao (1994). Molecular cloning, sequence analysis, and chromosomal localization of the human protease inhibitor 4 (kallistatin) gene (PI4). Genomics 23, 370-378. MEDLINE identifier: 95137583 Citation REF [3] G.X. Zhou, L. Chao & J. Chao (1992). Kallistatin: a novel human tissue kallikrein inhibitor. Purification, characterization, and reactive center sequence. J. Biol. Chem. 267, 25873-25880. MEDLINE identifier: 93100304 Signal 1708609: 1..20 Mature chain KALLISTATIN. 1708609: 21..427 (experimentally determined) active site REACTIVE BOND. 1708609: 388..389 (experimentally determined) glycosylation 1708609: 33 site glycosylation 1708609: 108 site glycosylation 1708609: 157 site glycosylation 1708609: 238 site Gene Locus: PI4 1708609: 1..427 Sequence 427 aa 1 mhlidyllll lvgllalshg qlhvehdges csnsshqqil etgegspslk 51 iapanadfaf rfyyliaset pgkniffspl sisaayamls lgacshsrsq 101 ileglgfnlt elsesdvhrg fqhllhtlnl pghgletrvg salflshnlk 151 flakflndtm avyeaklfht nfydtvgtiq lindhvkket rgkivdlvse 201 lkkdvlmvlv nyiyfkalwe kpfissrttp kdfyvdentt vrvpmmlqdq 251 ehhwylhdry lpcsvlrmdy kgdatvffil pnqgkmreie evltpemlmr 301 wnnllrkrnf ykklelhlpk fsisgsyvld qilprlgftd lfskwadlsg 351 itkqqkleas ksfhkatldv deagteaaaa ttfaikffsa qtnrhilrfn 401 rpflvvifst stqsvlflgk vvdptkp
1706895 --------------------------------------------------- Definition FUNGAL PROTEASE INHIBITOR F (FPI-F). Protein Name: FUNGAL PROTEASE INHIBITOR F 1706895: 1..55 SWISS-PROT Name: FPIF_BOMMO, Accession: Q10731 NCBI Seq ID: 1706895 Created Oct 1, 1996 Updated Oct 1, 1996 Citation REF [1] T.N. Pham, K. Hayashi, R. Takano, M. Itoh, M. Eguchi, H. Shibata, T. Tanaka & S. Hara (1996). A new family of serine protease inhibitors (Bombyx family) as established from the unique topological relation between the positions of disulphide bridges and reactive site. J. Biochem. 119, 428- 434. MEDLINE identifier: 96271002 active site REACTIVE BOND. 1706895: 29..30 (experimentally determined) disulfide bond (experimentally determined) 1706895: 3 bond 35 disulfide bond (experimentally determined) 1706895: 14 bond 27 disulfide bond (experimentally determined) 1706895: 18 bond 55 disulfide bond (experimentally determined) 1706895: 37 bond 49 Sequence 55 aa 1 lqcpknsevr nspcprtcnd pygqnscitv iretchckge lvfdsdsicv 51 pisqc
1706733 --------------------------------------------------- Definition FACTOR XIIA INHIBITOR PRECURSOR (XIIAINH). Protein Name: FACTOR XIIA INHIBITOR 1706733: 1..468 PRECURSOR SWISS-PROT Name: F12I_BOVIN, Accession: P50448 NCBI Seq ID: 1706733 Comment [FUNCTION] MAY PLAY A POTENTIALLY CRUCIAL ROLE IN REGULATING IMPORTANT PHYSIOLOGICAL PATHWAYS INCLUDING COMPLEMENT ACTIVATION, BLOOD COAGULATION, FIBRINOLYSIS AND THE GENERATION OF KININS. Comment [PTM] N- AND O-GLYCOSYLATED. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 927304 Cross-ref GenBank Accession: U30332 Created Oct 1, 1996 Updated Oct 1, 1996 Citation REF [1] Data Submission: J.E. EDMESTON, A. STRUMPFER, M. MULDBJERG, T. HALKIER & R.T.A. MACGILLIVRAY (1995). Citation REF [2] M. Muldbjerg, S. Markussen, S. Magnusson & T. Halkier (1993). Bovine factor XIIa inhibitor. Blood Coagul. Fibrinolysis 4, 47-54. MEDLINE identifier: 93208265 Citation REF [3] W.E. Van Nostrand & D.D. Cunningham (1987). Purification of a proteinase inhibitor from bovine serum with C1-inhibitor activity. Biochim. Biophys. Acta 923, 167-175. MEDLINE identifier: 87128997 Signal (experimentally determined) 1706733: 1..23 Mature chain FACTOR XIIA INHIBITOR. 1706733: 24..468 (experimentally determined) active site REACTIVE BOND. 1706733: 434..435 (experimentally determined) disulfide bond 1706733: 97 bond 396 disulfide bond 1706733: 104 bond 179 glycosylation 1706733: 65 site glycosylation 1706733: 176 site glycosylation 1706733: 227 site glycosylation 1706733: 326 site Conflict S -> R (IN REF. 2). 1706733: 78 (experimentally determined) Conflict PV -> TL (IN REF. 2). 1706733: 84..85 (experimentally determined) Conflict S -> I (IN REF. 2). 1706733: 87 (experimentally determined) Conflict T -> P (IN REF. 2). 1706733: 92 (experimentally determined) Conflict C -> F (IN REF. 2). 1706733: 97 (experimentally determined) Conflict L -> V (IN REF. 2). 1706733: 134 (experimentally determined) Conflict L -> V (IN REF. 2). 1706733: 171 (experimentally determined) Conflict K -> R (IN REF. 2). 1706733: 207 (experimentally determined) Conflict L -> N (IN REF. 2). 1706733: 332 (experimentally determined) Conflict T -> P (IN REF. 2). 1706733: 336 (experimentally determined) Conflict I -> K (IN REF. 2). 1706733: 409 (experimentally determined) Conflict R -> P (IN REF. 2). 1706733: 462 (experimentally determined) Sequence 468 aa 1 masrltpltl llllllagdr vtsdmivgpg nlqegesegd sqkggildge 51 siqgnedspt lpitnltvvp atvtkpfsqp atepvqstiq ptaepfclap 101 vtscsdseir saeavlgeal tdfslrlyqd fsvlkkretn fifspfsias 151 lltqillgag getrvslehl lsypqnfscv hhalrafmse gftsfsqifh 201 ssdltikdtf aeasqrlygs sprplgndst aslelindwv akktnlrirr 251 lldslpedtr lillnavals akwkiafdkg rtstkpfhlk ssaikvpmmn 301 skkypvasft drtlnrpggr lqlshnlsfv ilvpqtvkhh lqdleqalst 351 avfkavikkl emtkfhpthl tmprikvqss qdmldyfdfi ydvnlcglte 401 dpdvqvsgir hqatleltes gvdataasvv svarnlllfe vqqpflfllw 451 dqqhkfpvfm grvydpkg
1705664 --------------------------------------------------- Definition COLLAGEN-BINDING PROTEIN 2 PRECURSOR (COLLIGIN 2). Protein Name: COLLAGEN-BINDING PROTEIN 2 1705664: 1..418 PRECURSOR SWISS-PROT Name: CBP2_HUMAN, Accession: P50454 NCBI Seq ID: 1705664 Comment [FUNCTION] BINDS SPECIFICALLY TO COLLAGEN. COULD BE INVOLVED AS A CHAPERONE IN THE BIOSYNTHETIC PATHWAY OF COLLAGEN. Comment [SUBCELLULAR LOCATION] ENDOPLASMIC RETICULUM LUMEN. Comment [SIMILARITY] WITH SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 1199487 Cross-ref NCBI Seq ID: 1087085 Cross-ref DDBJ Accession: D83174 Cross-ref GenBank Accession: S79209 Cross-ref MIM 600943 Created Oct 1, 1996 Updated Oct 1, 1996 Citation REF [1] S. Ikegawa, K. Sudo, K. Okui & Y. Nakamura (1995). Isolation, characterization and chromosomal assignment of human colligin- 2 gene (CBP2). Cytogenet. Cell Genet. 71, 182-186. MEDLINE identifier: 95385381 Signal 1705664: 1..18 Mature chain COLLAGEN-BINDING PROTEIN 2. 1705664: 19..418 (experimentally determined) active site REACTIVE BOND. 1705664: 377..378 glycosylation 1705664: 120 site glycosylation 1705664: 125 site other site PREVENT SECRETION FROM ER. 1705664: 415..418 Gene Locus: CBP2 1705664: 1..418 Sequence 418 aa 1 mrsllllsaf clleaalaae vkkpaaaaap gtaeklspka atlaersagl 51 afslyqamak dqavenilvs pvvvasslgl vslggkatta sqakavlsae 101 qlrdeevhag lgellrslsn starnvtwkl gsrlygpssv sfaddfvrss 151 kqhyncehsk infrdkrrpl qsinewaaqt tdgklpevtk dvertdgall 201 vnamffkphw dekfhhkmvd nrgfmvtrsy tvgvmmmhrt glynyyddek 251 eklqivempl ahklssliil mphhvepler leklltkeql kiwmgkmqkk 301 avaislpkgv vevthdlqkh laglglteai dknkadlsrm sgkkdlylas 351 vfhatafeld tdgnpfdqdi ygreelrspk lfyadhpfif lvrdtqsgsl 401 lfigrlvrpk gdkmrdel
1705661 --------------------------------------------------- Definition CORTICOSTEROID-BINDING GLOBULIN PRECURSOR (CBG) (TRANSCORTIN). Protein Name: CORTICOSTEROID-BINDING 1705661: 1..430 GLOBULIN PRECURSOR SWISS-PROT Name: CBG_SHEEP, Accession: P49920 NCBI Seq ID: 1705661 Comment [FUNCTION] MAJOR TRANSPORT PROTEIN FOR GLUCOCORTICOIDS AND PROGESTINS IN THE BLOOD OF ALMOST ALL VERTEBRATE SPECIES. Comment [SUBCELLULAR LOCATION] EXTRACELLULAR. Comment [TISSUE SPECIFICITY] PLASMA; SYNTHESIZED IN LIVER. Comment [SIMILARITY] WITH SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 599938 Cross-ref EMBL Accession: X73615 Created Oct 1, 1996 Updated Oct 1, 1996 Citation REF [1] E.T. Berdusco, G.L. Hammond, R.A. Jacobs, A. Grolla, K. Akagi, D. Langlois & J.R. Challis (1993). Glucocorticoid-induced increase in plasma corticosteroid-binding globulin levels in fetal sheep is associated with increased biosynthesis and alterations in glycosylation. Endocrinology 132, 2001-2008. MEDLINE identifier: 93238621 Signal 1705661: 1..22 Mature chain CORTICOSTEROID-BINDING PROTEIN. 1705661: 23..430 (experimentally determined) glycosylation 1705661: 119 site glycosylation 1705661: 175 site glycosylation 1705661: 243 site glycosylation 1705661: 259 site glycosylation 1705661: 326 site other site CONSERVED CYSTEINE WITHIN STEROID 1705661: 249 BINDING DOMAIN. Gene Locus: CBG 1705661: 1..430 Sequence 430 aa 1 mlltlytcll wlstsglwti qakgtdtdvs trnphrdlap nnvdfaftly 51 khlvasapgk nvfispvsis malamlslga rgytreqllq glgfslvems 101 eaeihqafrh lhhllresnt tlemtmgnal fldhslelle sfsadtkhyy 151 elealttdfq dwagasrqin eyiknktqgk ivdlfsesds samfilvnyi 201 ffkgmwvhsf dlestreenf yvneattvwv pmmfqsntik ylndsvlpcq 251 lvqldytgne tvffvlpvkg kmdsvitals rdtiqrwsks ltmsqvdlyi 301 pkisisgayd lggimgdmgi adllsnrthf sgitqealpk vskvvhkaal 351 qvdekgleaa aptrvsvtaa pgpltlrfnr pfiimifddf twsslflgkv 401 vnptegalpg aklrltrapr ahrkgwegsp
1705660 --------------------------------------------------- Definition CORTICOSTEROID-BINDING GLOBULIN PRECURSOR (CBG) (TRANSCORTIN). Protein Name: CORTICOSTEROID-BINDING 1705660: 1..406 GLOBULIN PRECURSOR SWISS-PROT Name: CBG_SAISC, Accession: P50451 NCBI Seq ID: 1705660 Comment [FUNCTION] MAJOR TRANSPORT PROTEIN FOR GLUCOCORTICOIDS AND PROGESTINS IN THE BLOOD OF ALMOST ALL VERTEBRATE SPECIES. Comment [SUBCELLULAR LOCATION] EXTRACELLULAR. Comment [TISSUE SPECIFICITY] PLASMA; SYNTHESIZED IN LIVER. Comment [SIMILARITY] WITH SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 545179 Cross-ref GenBank Accession: S68757 Created Oct 1, 1996 Updated Oct 1, 1996 Citation REF [1] G.L. Hammond, C.L. Smith, P. Lahteenmaki, A. Grolla, S. Warmels-Rodenhiser, H. Hodgert, J.T. Murai & P.K. Siiteri (1994). Squirrel monkey corticosteroid-binding globulin: primary structure and comparison with the human protein. Endocrinology 134, 891-898. MEDLINE identifier: 94130841 Signal 1705660: 1..22 Mature chain CORTICOSTEROID-BINDING GLOBULIN. 1705660: 23..406 (experimentally determined) glycosylation 1705660: 31 site glycosylation 1705660: 96 site glycosylation 1705660: 261 site glycosylation 1705660: 331 site glycosylation 1705660: 360 site other site CONSERVED CYSTEINE WITHIN STEROID 1705660: 251 BINDING DOMAIN. Gene Locus: CBG 1705660: 1..406 Sequence 406 aa 1 mplllytcll wllssglwtv qamdpnaaym ntsrhhrvla svnadfafsl 51 ykhlvalspk knvfispvsi smalamlslg tcghtraqll hglgfnltek 101 seaeihqsfq hlhqllaesd sslemtlgna lfldgslell esfsadikhy 151 yesevltlnf qdwattasrq ingyvksktq gkiddlfsgl nspavlilin 201 yiffkgtwkq pfdlastree nfyvdettvv kvpmmfqsgt irylhdselp 251 cqlvqlnyag ngtvffilpe kgkmnivita lsrntidrws agltrsqvdl 301 yipkvtisga ydfggvledm giadlftnha nfsritqdaq lklskvfhka 351 vlqlseegvn ttgstgvtln pmskpiimrf nqpflimvfd hftwsslflg 401 rvvnpa
1703309 --------------------------------------------------- Definition ANGIOTENSINOGEN PRECURSOR. Protein Name: ANGIOTENSINOGEN PRECURSOR 1703309: 1..476 SWISS-PROT Name: ANGT_SHEEP, Accession: P20757 NCBI Seq ID: 1703309 Comment [FUNCTION] IN RESPONSE TO LOWERED BLOOD PRESSURE, THE ENZYME RENIN CLEAVES ANGIOTENSIN I, FROM ANGIOTENSINOGEN. ACE (ANGIOTENSIN CONVERTING ENZYME) THEN REMOVES A DIPEPTIDE TO YIELD THE PHYSIOLOGICALLY ACTIVE PEPTIDE ANGIOTENSIN II, THE MOST POTENT PRESSOR SUBSTANCE KNOWN, WHICH HELPS REGULATE VOLUME AND MINERAL BALANCE OF BODY FLUIDS. Comment [TISSUE SPECIFICITY] MADE IN THE LIVER & SECRETED IN THE PLASMA. Comment [SIMILARITY] WITH SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 1197183 Cross-ref DDBJ Accession: D17520 Cross-ref PROSITE PS00284 Created Feb 1, 1991 Updated Oct 1, 1996 Citation REF [1] M. Nagase, F. Suzuki, A. Fukamizu, N. Takeda, K. Takeuchi, K. Murakami & Y. Nakamura (1994). Sequencing and expression of sheep angiotensinogen cDNA. Biosci. Biotechnol. Biochem. 58, 1884-1885. MEDLINE identifier: 95072318 Citation REF [2] R.T. Fernley, M. John, H.D. Niall & J.P. Coghlan (1986). Purification and characterization of ovine angiotensinogen. Eur. J. Biochem. 154, 597-601. MEDLINE identifier: 86136099 Signal (experimentally determined) 1703309: 1..24 Mature chain ANGIOTENSINOGEN. 1703309: 25..476 (experimentally determined) Processed ANGIOTENSIN I. 1703309: 25..34 active peptide (experimentally determined) Processed ANGIOTENSIN II. 1703309: 25..32 active peptide (experimentally determined) glycosylation 1703309: 295 site Gene Locus: AGT 1703309: 1..476 Sequence 476 aa 1 mapaglslga tilcllawag laagdrvyih pfhllvhsks ncdqlekpsv 51 etpadptltp vpiqtksspv deealweqlv ratekleaed rlrasevgll 101 lnfmgfhvyk tlsetwsvas glvfspvalf stltsfytga ldptasrlqa 151 flgvpgegqg ctsrldgrkv lsslqtiqgl lvapggassq arlllstvvg 201 lftapglhlk qpfvqglssf apitlprsld lstdpnlaae kinrfmhsat 251 gwnmgrplaa aspdstllfn ayvhfqgkmk gfsllpglte fwvdnttsvp 301 vpmlsgsgtf hywsdnqnhl smtrvplsan gyllliqphh tldlrkveal 351 ifqhnfltrm knlspraihl tvpqltlkas ydlqdllaqa klptllgaea 401 nlgkisdanl rvgkvlnsvl felkadgeqa pesvpqpagp ealevtlnsp 451 fllavlerss galhflgrvs rplsae
1703308 --------------------------------------------------- Definition ANGIOTENSIN-LIKE PEPTIDE II. Protein Name: ANGIOTENSIN-LIKE PEPTIDE II 1703308: 1..8 *: Partial SWISS-PROT Name: ANG2_BOTJA, Accession: Q10582 NCBI Seq ID: 1703308 Comment [SIMILARITY] WITH SERPIN SERINE PROTEASE INHIBITORS. Created Oct 1, 1996 Updated Oct 1, 1996 Citation REF [1] R.A.M.B. BORGHERESI, J.D. LUCCA, E. CARMONA & Z.P. PICARELLI (1996)COMP. BIOCHEM. PHYSIOL. 113B, 467-473. Sequence 8 aa 1 drvyihpf
1703307 --------------------------------------------------- Definition ANGIOTENSIN-LIKE PEPTIDE I. Protein Name: ANGIOTENSIN-LIKE PEPTIDE I 1703307: 1..10 *: Partial SWISS-PROT Name: ANG1_BOTJA, Accession: Q10581 NCBI Seq ID: 1703307 Comment [SIMILARITY] WITH SERPIN SERINE PROTEASE INHIBITORS. Created Oct 1, 1996 Updated Oct 1, 1996 Citation REF [1] R.A.M.B. BORGHERESI, J.D. LUCCA, E. CARMONA & Z.P. PICARELLI (1996)COMP. BIOCHEM. PHYSIOL. 113B, 467-473. Sequence 10 aa 1 drvyvhpfyl
1703026 --------------------------------------------------- Definition ALPHA-1-ANTITRYPSIN PRECURSOR (ALPHA-1 PROTEASE INHIBITOR) (ALPHA-1-ANTIPROTEINASE). Protein Name: ALPHA-1-ANTITRYPSIN 1703026: 1..421 PRECURSOR SWISS-PROT Name: A1AT_PIG, Accession: P50447 NCBI Seq ID: 1703026 Comment [FUNCTION] INHIBITOR OF SERINE PROTEASES. ITS PRIMARY TARGET IS ELASTASE, BUT IT ALSO HAS A MODERATE AFFINITY FOR PLASMIN AND THROMBIN (BY SIMILARITY). Comment [SUBCELLULAR LOCATION] EXTRACELLULAR. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 975230 Cross-ref EMBL Accession: X88780 Created Oct 1, 1996 Updated Oct 1, 1996 Citation REF [1] Data Submission: A.L. ARCHIBALD, S. COUPERWHITE, C.H.M. MELLINK & Y. LAHBIB-MANSAIS (1995). Signal 1703026: 1..24 Mature chain ALPHA-1-ANTITRYPSIN. 1703026: 25..421 (experimentally determined) active site REACTIVE BOND. 1703026: 385..386 (experimentally determined) glycosylation 1703026: 73 site glycosylation 1703026: 110 site Gene Locus: PI 1703026: 1..421 Sequence 421 aa 1 massstwgll llaglcclvp islaeglqgh avqetdvprh dheqhqeaac 51 hriapnladf afslyrqvar qsntsnifls pvtiarafam lslgtkgath 101 aeileglqfn ltekaeaeih egfqhllhtl nqpdnqlqlt tgnglfidek 151 aklvpkfled vknlyhseaf sinfrdteea kkcindyvek gsqgkivdlv 201 deldkdtvfa lvnyiffkgk wekpfeveqt teedfhvdee ttvkvpmmnr 251 lgmfdlhhcd klsswvllmd yvatataffi lpdqgklhql edmltkeira 301 kflekrypss anlhlpklti sgtydlksll gnlgitkvfs deadlsgvte 351 eqplklskal hravltidek gteatgatil eaipmsippn vkfnkpflfl 401 iydtktkavl fmgkvmnptq k
1703025 --------------------------------------------------- Definition ALPHA-1-ANTITRYPSIN PRECURSOR (ALPHA-1 PROTEASE INHIBITOR) (ALPHA-1-ANTIPROTEINASE). Protein Name: ALPHA-1-ANTITRYPSIN 1703025: 1..418 PRECURSOR SWISS-PROT Name: A1AT_HUMAN, Accession: P01009 NCBI Seq ID: 1703025 Comment [FUNCTION] INHIBITOR OF SERINE PROTEASES. ITS PRIMARY TARGET IS ELASTASE, BUT IT ALSO HAS A MODERATE AFFINITY FOR PLASMIN AND THROMBIN. Comment [SUBCELLULAR LOCATION] EXTRACELLULAR. Comment [TISSUE SPECIFICITY] PLASMA. Comment [POLYMORPHISM] THE SEQUENCE SHOWN IS THAT OF THE M1V ALLELE WHICH IS THE MOST COMMON FORM OF PI (44 TO 49%). OTHER FREQUENT ALLELES ARE: M1A 20 TO 23%; M2 10 TO 11%; M3 14 TO 19%. Comment [DISEASE] THE MAJOR PHYSIOLOGICAL FUNCTION OF AAT IS THE PROTECTION OF THE LOWER RESPIRATORY TRACT AGAINST PROTEOLYTIC DESTRUCTION BY HUMAN LEUKOCYTE ELASTASE (HLE). A HEREDITARY DEFICIENCY OF AAT, IS ASSOCIATED WITH A 20-30 FOLD INCREASED RISK OF DEVELOPING CHRONIC OBSTRUCTIVE PULMONARY DISEASE. Comment [DISEASE] DEFICIENCY OF THE NORMAL INHIBITOR IN INDIVIDUALS HOMOZYGOUS FOR ALLELE Z OR M-MALTON CAN RESULT IN THE DEVELOPMENT OF CHRONIC EMPHYSEMA OR INFANTILE LIVER CIRRHOSIS. Comment [DISEASE] VARIANT PITTSBURGH IS THE CAUSE OF BLEEDING DIATHESIS. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 825632 Cross-ref NCBI Seq ID: 177829 Cross-ref NCBI Seq ID: 28966 Cross-ref NCBI Seq ID: 177822 Cross-ref NCBI Seq ID: 177823 Cross-ref NCBI Seq ID: 177824 Cross-ref NCBI Seq ID: 177836 Cross-ref NCBI Seq ID: 24438 Cross-ref NCBI Seq ID: 177831 Cross-ref EMBL Accession: V00496 Cross-ref GenBank Accession: K01396 Cross-ref EMBL Accession: X01683 Cross-ref GenBank Accession: J00064 Cross-ref GenBank Accession: J00066 Cross-ref GenBank Accession: J00067 Cross-ref GenBank Accession: J02619 Cross-ref EMBL Accession: X02920 Cross-ref GenBank Accession: K02212 Cross-ref PDB Molecule: 7API, Chain: (space) Cross-ref PDB Molecule: 8API, Chain: (space) Cross-ref PDB Molecule: 9API, Chain: (space) Cross-ref SWISS-2DPAGE P01009 Cross-ref HSC-2DPAGE P01009 Cross-ref MIM 107400 Cross-ref PROSITE PS00284 Created Jul 21, 1986 Updated Oct 1, 1996 Citation REF [1] A. Bollen, A. Herzog, A. Cravador, P. Herion, P. Chuchana, A. Vander Straten, R. Loriau, P. Jacobs & A. van Elsen (1983). Cloning and expression in Escherichia coli of full-length complementary DNA coding for human alpha 1-antitrypsin. DNA 2, 255-264. MEDLINE identifier: 84107980 Citation REF [2] S. Rosenberg, P.J. Barr, R.C. Najarian & R.A. Hallewell (1984). Synthesis in yeast of a functional oxidation- resistant mutant of human alpha-antitrypsin. Nature 312, 77- 80. MEDLINE identifier: 85036645 Citation REF [3] G.L. Long, T. Chandra, S.L. Woo, E.W. Davie & K. Kurachi (1984). Complete sequence of the cDNA for human alpha 1- antitrypsin and the gene for the S variant. Biochemistry 23, 4828-4837. MEDLINE identifier: 85047190 Citation REF [4] T. Nukiwa, K. Satoh, M.L. Brantly, F. Ogushi, G.A. Fells, M. Courtney & R.G. Crystal (1986). Identification of a second mutation in the protein-coding sequence of the Z type alpha 1- antitrypsin gene. J. Biol. Chem. 261, 15989-15994. MEDLINE identifier: 87057257 Citation REF [5] T. NUKIWA, K. SATOH, M.L. BRANTLY, F. OGUSHI, G.A. FELLS, M. COURTNEY & R.G. CRYSTAL (1987)J. BIOL. CHEM. 262, 10412-10412. Citation REF [6] R.W. Carrell, J.O. Jeppsson, C.B. Laurell, S.O. Brennan, M.C. Owen, L. Vaughan & D.R. Boswell (1982). Structure and variation of human alpha 1-antitrypsin. Nature 298, 329-334. MEDLINE identifier: 82220135 Citation REF [7] S.K. CHAN (1982)FED. PROC. 41, 1016-1016. Citation REF [8] M. Leicht, G.L. Long, T. Chandra, K. Kurachi, V.J. Kidd, M. Mace, E.W. Davie & S.L. Woo (1982). Sequence homology and structural comparison between the chromosomal human alpha 1- antitrypsin and chicken ovalbumin genes. Nature 297, 655-659. MEDLINE identifier: 82220035 Citation REF [9] J.H. Riley, I.C. Bathurst, M.R. Edbrooke, R.W. Carrell & R.K. Craig (1985). Alpha 1-antitrypsin and serum albumin mRNA accumulation in normal, acute phase and ZZ human liver. FEBS Lett. 189, 361-366. MEDLINE identifier: 86005469 Citation REF [10] K. Kurachi, T. Chandra, S.J. Degen, T.T. White, T.L. Marchioro, S.L. Woo & E.W. Davie (1981). Cloning and sequence of cDNA coding for alpha 1-antitrypsin. Proc. Natl. Acad. Sci. U.S.A. 78, 6826-6830. MEDLINE identifier: 82082539 Citation REF [11] H. Loebermann, R. Tokuoka, J. Deisenhofer & R. Huber (1984). Human alpha 1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function. J. Mol. Biol. 177, 531-557. MEDLINE identifier: 84292309 Citation REF [12] R. Engh, H. Lobermann, M. Schneider, G. Wiegand, R. Huber & C.B. Laurell (1989). The S variant of human alpha 1- antitrypsin, structure and implications for function and metabolism. Protein Eng. 2, 407-415. MEDLINE identifier: 89221004 Citation REF [13] U. Baumann, R. Huber, W. Bode, D. Grosse, M. Lesjak & C.B. Laurell (1991). Crystal structure of cleaved human alpha 1- antichymotrypsin at 2.7 A resolution and its comparison with other serpins. J. Mol. Biol. 218, 595-606. MEDLINE identifier: 91202538 Citation REF [14] T. Nukiwa, M.L. Brantly, F. Ogushi, G.A. Fells & R.G. Crystal (1988). Characterization of the gene and protein of the common alpha 1-antitrypsin normal M2 allele. Am. J. Hum. Genet. 43, 322-330. MEDLINE identifier: 88324438 Citation REF [15] A. Graham, K. Hayes, S. Weidinger, C.R. Newton, A.F. Markham & N.A. Kalsheker (1990). Characterisation of the alpha-1- antitrypsin M3 gene, a normal variant. Hum. Genet. 85, 381- 382. MEDLINE identifier: 90368097 Citation REF [16] H. Okayama, M. Brantly, M. Holmes & R.G. Crystal (1991). Characterization of the molecular basis of the alpha 1- antitrypsin F allele. Am. J. Hum. Genet. 48, 1154-1158. MEDLINE identifier: 91241132 Citation REF [17] M.H. Hofker, T. Nukiwa, H.M. van Paassen, M. Nelen, J.A. Kramps, E.C. Klasen, R.R. Frants & R.G. Crystal (1989). A Pro- ---Leu substitution in codon 369 of the alpha-1-antitrypsin deficiency variant PI MHeerlen. Hum. Genet. 81, 264-268. MEDLINE identifier: 89154435 Citation REF [18] G.C. Fraizer, T.R. Harrold, M.H. Hofker & D.W. Cox (1989). In- frame single codon deletion in the Mmalton deficiency allele of alpha 1-antitrypsin. Am. J. Hum. Genet. 44, 894-902. MEDLINE identifier: 89270478 Citation REF [19] D.T. Curiel, C. Vogelmeier, R.C. Hubbard, L.E. Stier & R.G. Crystal (1990). Molecular basis of alpha 1-antitrypsin deficiency and emphysema associated with the alpha 1- antitrypsin Mmineral springs allele. Mol. Cell. Biol. 10, 47- 56. MEDLINE identifier: 90097863 Citation REF [20] E. Matsunaga, S. Shiokawa, H. Nakamura, T. Maruyama, K. Tsuda & Y. Fukumaki (1990). Molecular analysis of the gene of the alpha 1-antitrypsin deficiency variant, Mnichinan. Am. J. Hum. Genet. 46, 602-612. MEDLINE identifier: 90178096 Citation REF [21] H. Takahashi, T. Nukiwa, K. Satoh, F. Ogushi, M. Brantly, G. Fells, L. Stier, M. Courtney & R.G. Crystal (1988). Characterization of the gene and protein of the alpha 1- antitrypsin "deficiency" allele Mprocida. J. Biol. Chem. 263, 15528-15534. MEDLINE identifier: 89008457 Citation REF [22] J. Hildesheim, G. Kinsley, M. Bissell, J. Pierce & M. Brantly (1993). Genetic diversity from a limited repertoire of mutations on different common allelic backgrounds: alpha 1- antitrypsin deficiency variant Pduarte. Hum. Mutat. 2, 221- 228. MEDLINE identifier: 93372875 Citation REF [23] M.C. OWEN, S.O. BRENNAN, J.H. LEWIS & R.W. CARRELL (1983)NEW ENGL. J. MED. 309, 694-698. Citation REF [24] K. Seyama, T. Nukiwa, K. Takabe, H. Takahashi, K. Miyake & S. Kira (1991). Siiyama (serine 53 (TCC) to phenylalanine 53 (TTC)). A new alpha 1-antitrypsin-deficient variant with mutation on a predicted conserved residue of the serpin backbone. J. Biol. Chem. 266, 12627-12632. MEDLINE identifier: 91286296 Citation REF [25] M.D. Holmes, M.L. Brantly, D.T. Curiel, S. Weidinger & R.G. Crystal (1990). Characterization of the normal alpha 1- antitrypsin allele Vmunich: a variant associated with a unique protein isoelectric focusing pattern. Am. J. Hum. Genet. 46, 810-816. MEDLINE identifier: 90196014 Citation REF [26] M.D. Holmes, M.L. Brantly, G.A. Fells & R.G. Crystal (1990). Alpha 1-antitrypsin Wbethesda: molecular basis of an unusual alpha 1-antitrypsin deficiency variant. Biochem. Biophys. Res. Commun. 170, 1013-1020. MEDLINE identifier: 90358792 Citation REF [27] J.P. Faber, S. Weidinger & K. Olek (1990). Sequence data of the rare deficient alpha 1-antitrypsin variant PI Zaugsburg. Am. J. Hum. Genet. 46, 1158-1162. MEDLINE identifier: 90252805 Citation REF [28] A. Graham, N.A. Kalsheker, F.J. Bamforth, C.R. Newton & A.F. Markham (1990). Molecular characterisation of two alpha-1- antitrypsin deficiency variants: proteinase inhibitor (Pi) Null(Newport) (Gly115----Ser) and (Pi) Z Wrexham (Ser-19---- Leu). Hum. Genet. 85, 537-540. MEDLINE identifier: 91033789 Citation REF [29] A. Graham, N.A. Kalsheker, C.R. Newton, F.J. Bamforth, S.J. Powell & A.F. Markham (1989). Molecular characterisation of three alpha-1-antitrypsin deficiency variants: proteinase inhibitor (Pi) nullcardiff (Asp256----Val); PiMmalton (Phe51--- -deletion) and PiI (Arg39----Cys). Hum. Genet. 84, 55-58. MEDLINE identifier: 90109164 Citation REF [30] G.C. Frazier, M.A. Siewertsen, M.H. Hofker, M.G. Brubacher & D.W. Cox (1990). A null deficiency allele of alpha 1- antitrypsin, QOludwigshafen, with altered tertiary structure. J. Clin. Invest. 86, 1878-1884. MEDLINE identifier: 91072661 Citation REF [31] J.P. Faber, W. Poller, S. Weidinger, M. Kirchgesser, R. Schwaab, F. Bidlingmaier & K. Olek (1994). Identification and DNA sequence analysis of 15 new alpha 1-antitrypsin variants, including two PI*Q0 alleles and one deficient PI*M allele. Am. J. Hum. Genet. 55, 1113-1121. MEDLINE identifier: 95067973 Citation REF [32] N. Kalsheker (1989). Alpha 1-antitrypsin: structure, function and molecular biology of the gene. Biosci. Rep. 9, 129-138. MEDLINE identifier: 89352843 Citation REF [33] Y. Wu & R.C. Foreman (1991). The molecular genetics of alpha 1 antitrypsin deficiency. Bioessays 13, 163-169. MEDLINE identifier: 91315455 Signal (experimentally determined) 1703025: 1..24 Mature chain ALPHA-1-ANTITRYPSIN. 1703025: 25..418 (experimentally determined) glycosylation (experimentally determined) 1703025: 70 site glycosylation (experimentally determined) 1703025: 107 site glycosylation (experimentally determined) 1703025: 271 site Variant S -> L (IN Z-WREXHAM). 1703025: 4 (experimentally determined) Variant D -> A (IN V-MUNICH). 1703025: 26 (experimentally determined) Variant A -> T (IN M5-KARLSRUHE). 1703025: 58 (experimentally determined) Variant R -> C (IN I). 1703025: 63 (experimentally determined) Variant L -> P (IN M-PROCIDA). 1703025: 65 (experimentally determined) Variant S -> F (IN M6-BONN). 1703025: 69 (experimentally determined) Variant MISSING (IN M-MALTON, M-NICHINAN 1703025: 75 AND M-PALERMO; ASSOCIATED WITH VERY LOW SERUM LEVELS OF AAT). (experimentally determined) Variant S -> F (IN S-IIYAMA). 1703025: 77 (experimentally determined) Variant A -> T (IN M6-PASSAU). 1703025: 84 (experimentally determined) Variant G -> E (IN M-MINERAL SPRINGS; 1703025: 91 CAUSES REDUCED AAT SECRETION). (experimentally determined) Variant T -> I (IN QO-LISBON; DEFICIENT 1703025: 92 AAT WITH VERY LOW SERUM LEVELS). (experimentally determined) Variant P -> T (IN M5-BERLIN). 1703025: 112 (experimentally determined) Variant I -> N (IN QO-LUDWIGSHAFEN). 1703025: 116 (experimentally determined) Variant R -> H (IN M2). 1703025: 125 (experimentally determined) Variant G -> S (IN QO-NEWPORT). 1703025: 139 (experimentally determined) Variant G -> R (IN V AND M-NICHINAN). 1703025: 172 (experimentally determined) Variant G -> W (IN M2-OBERNBURG). 1703025: 172 (experimentally determined) Variant Q -> E (IN L-FRANKFURT). 1703025: 180 (experimentally determined) Variant E -> K (IN X). 1703025: 228 (experimentally determined) Variant V -> A (IN M1A AND Z). 1703025: 237 (experimentally determined) Variant R -> C (IN F). 1703025: 247 (experimentally determined) Variant D -> V (IN P-DUARTE/P-CARDIFF/P- 1703025: 280 LOWELL). (experimentally determined) Variant E -> V (IN S AND T). 1703025: 288 (experimentally determined) Variant S -> F (IN S-MUNICH). 1703025: 354 (experimentally determined) Variant A -> T (IN W-BETHESDA). 1703025: 360 (experimentally determined) Variant D -> N (IN P-ST.ALBANS/P- 1703025: 365 DONAUWOERTH). (experimentally determined) Variant E -> K (IN Z/Z-AUGSBURG/Z-TUN). 1703025: 366 (experimentally determined) Variant M -> R (IN PITTSBURGH; HAS 1703025: 382 ANTITHROMBIN ACTIVITY). (experimentally determined) Variant P -> T (IN L-OFFENBACH). 1703025: 386 (experimentally determined) Variant E -> K (IN CHRISTCHURCH). 1703025: 387 (experimentally determined) Variant P -> L (IN M-HEERLEN). 1703025: 393 (experimentally determined) Variant E -> D (IN M2 AND M3). 1703025: 400 (experimentally determined) mutagenized M->V: OXIDATION-RESISTANT 1703025: 382 site INHIBITOR OF THERAPEUTIC IMPORTANCE. (experimentally determined) active site REACTIVE BOND. 1703025: 382..383 (experimentally determined) Conflict GN -> DG (IN REF. 1). 1703025: 139..140 (experimentally determined) Conflict T -> N (IN REF. 1). 1703025: 273 (experimentally determined) Conflict V -> I (IN REF. 2). 1703025: 326 (experimentally determined) Helical region (experimentally determined) 1703025: 47..68 Beta-strand (experimentally determined) 1703025: 74..76 region Helical region (experimentally determined) 1703025: 78..87 Hydrogen (experimentally determined) 1703025: 88 bonded turn Helical region (experimentally determined) 1703025: 89..91 Helical region (experimentally determined) 1703025: 94..103 Hydrogen (experimentally determined) 1703025: 104..105 bonded turn Hydrogen (experimentally determined) 1703025: 108..110 bonded turn Helical region (experimentally determined) 1703025: 113..127 Hydrogen (experimentally determined) 1703025: 128 bonded turn Beta-strand (experimentally determined) 1703025: 135..145 region Hydrogen (experimentally determined) 1703025: 146..147 bonded turn Helical region (experimentally determined) 1703025: 152..160 Hydrogen (experimentally determined) 1703025: 161 bonded turn Beta-strand (experimentally determined) 1703025: 165..169 region Hydrogen (experimentally determined) 1703025: 171..172 bonded turn Helical region (experimentally determined) 1703025: 174..188 Hydrogen (experimentally determined) 1703025: 189..191 bonded turn Hydrogen (experimentally determined) 1703025: 202..203 bonded turn Beta-strand (experimentally determined) 1703025: 206..218 region Helical region (experimentally determined) 1703025: 224..226 Beta-strand (experimentally determined) 1703025: 228..232 region Beta-strand (experimentally determined) 1703025: 240..256 region Helical region (experimentally determined) 1703025: 257..259 Hydrogen (experimentally determined) 1703025: 260 bonded turn Beta-strand (experimentally determined) 1703025: 261..268 region Beta-strand (experimentally determined) 1703025: 272..279 region Hydrogen (experimentally determined) 1703025: 281..282 bonded turn Helical region (experimentally determined) 1703025: 284..290 Helical region (experimentally determined) 1703025: 293..301 Beta-strand (experimentally determined) 1703025: 306..313 region Beta-strand (experimentally determined) 1703025: 315..322 region Helical region (experimentally determined) 1703025: 324..329 Hydrogen (experimentally determined) 1703025: 330..331 bonded turn Helical region (experimentally determined) 1703025: 334..336 Hydrogen (experimentally determined) 1703025: 338..339 bonded turn Hydrogen (experimentally determined) 1703025: 343..345 bonded turn Beta-strand (experimentally determined) 1703025: 351..364 region Beta-strand (experimentally determined) 1703025: 368..381 region Beta-strand (experimentally determined) 1703025: 387..389 region Beta-strand (experimentally determined) 1703025: 394..400 region Hydrogen (experimentally determined) 1703025: 401..403 bonded turn Beta-strand (experimentally determined) 1703025: 406..412 region Hydrogen (experimentally determined) 1703025: 415..416 bonded turn Gene Locus: PI 1703025: 1..418 Sequence 418 aa 1 mpssvswgil llaglcclvp vslaedpqgd aaqktdtshh dqdhptfnki 51 tpnlaefafs lyrqlahqsn stniffspvs iatafamlsl gtkadthdei 101 leglnfnlte ipeaqihegf qellrtlnqp dsqlqlttgn glflseglkl 151 vdkfledvkk lyhseaftvn fgdteeakkq indyvekgtq gkivdlvkel 201 drdtvfalvn yiffkgkwer pfevkdteee dfhvdqvttv kvpmmkrlgm 251 fniqhckkls swvllmkylg nataifflpd egklqhlene lthdiitkfl 301 enedrrsasl hlpklsitgt ydlksvlgql gitkvfsnga dlsgvteeap 351 lklskavhka vltidekgte aagamfleai pmsippevkf nkpfvflmie 401 qntksplfmg kvvnptqk
1703024 --------------------------------------------------- Definition ALPHA-1 ANTITRYPSIN 1 PRECURSOR (ALPHA-1 PROTEASE INHIBITOR) (ALPHA-1-ANTIPROTEINASE) (AAT) (SERINE PROTEASE INHIBITOR-1). Protein Name: ALPHA-1 ANTITRYPSIN 1 1703024: 1..413 PRECURSOR SWISS-PROT Name: A1A1_MOUSE, Accession: P07758 NCBI Seq ID: 1703024 Comment [FUNCTION] INHIBITOR OF SERINE PROTEASES. ITS PRIMARY TARGET IS ELASTASE, BUT IT ALSO HAS A MODERATE AFFINITY FOR PLASMIN AND THROMBIN. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 191842 Cross-ref NCBI Seq ID: 49792 Cross-ref NCBI Seq ID: 192094 Cross-ref GenBank Accession: M75721 Cross-ref EMBL Accession: X00945 Cross-ref GenBank Accession: M12586 Cross-ref HSSP P01009 Cross-ref PROSITE PS00284 Created Aug 1, 1988 Updated Oct 1, 1996 Citation REF [1] F. Borriello & K.S. Krauter (1991). Multiple murine alpha 1- protease inhibitor genes show unusual evolutionary divergence. Proc. Natl. Acad. Sci. U.S.A. 88, 9417-9421. MEDLINE identifier: 92052104 Citation REF [2] R.E. Hill, P.H. Shaw, P.A. Boyd, H. Baumann & N.D. Hastie (1984). Plasma protease inhibitors in mouse and man: divergence within the reactive centre regions. Nature 311, 175-177. MEDLINE identifier: 84295637 Citation REF [3] K.S. Krauter, B.A. Citron, M.T. Hsu, D. Powell & J.E. Darnell (1986). Isolation and characterization of the alpha 1- antitrypsin gene of mice. DNA 5, 29-36. MEDLINE identifier: 86163765 Signal 1703024: 1..24 Mature chain ALPHA-1-ANTITRYPSIN 1. 1703024: 25..413 (experimentally determined) active site REACTIVE BOND. 1703024: 377..378 (experimentally determined) glycosylation 1703024: 64 site glycosylation 1703024: 101 site glycosylation 1703024: 265 site Conflict AL -> SP (IN REF. 2). 1703024: 201..202 (experimentally determined) Conflict H -> D (IN REF. 2 AND 3). 1703024: 246 (experimentally determined) Conflict P -> L (IN REF. 3). 1703024: 323 (experimentally determined) Conflict QM -> LA (IN REF. 2). 1703024: 373..374 (experimentally determined) Conflict M -> Y (IN REF. 2). 1703024: 377 (experimentally determined) Conflict I -> L (IN REF. 2). 1703024: 402 (experimentally determined) Conflict L -> V (IN REF. 2 AND 3). 1703024: 404 (experimentally determined) Gene Locus: SPI1 1703024: 1..413 Sequence 413 aa 1 mtpsiswgll llaglcclvp sflaedvqet dtsqkdqspa sheiatnlgd 51 faislyrelv hqsntsniff spvsiatafa mlslgskgdt htqileglqf 101 nltqtseadi hksfqhllqt lnrpdselql stgnglfvnn dlklvekfle 151 eaknhyqaev fsvnfaesee akkvindfve kgtqgkiaea vkkldqdtvf 201 alanyilfkg kwkkpfdpen teeaefhvde sttvkvpmmt lsgmlhvhhc 251 stlsswvllm dyagnatavf llpddgkmqh leqtlskeli skfllnrrrr 301 laqihfprls isgeynlktl msplgitrif nngadlsgit eenaplklsq 351 avhkavltid etgteaaavt vlqmvpmsmp pilrfdhpfl fiifeehtqs 401 piflgkvvdp thk
1351385 --------------------------------------------------- Definition UTERINE MILK PROTEIN PRECURSOR (UTMP). Protein Name: UTERINE MILK PROTEIN 1351385: 1..429 PRECURSOR SWISS-PROT Name: UTMP_SHEEP, Accession: P21814 NCBI Seq ID: 1351385 Comment [TISSUE SPECIFICITY] SECRETED BY OVINE ENDOMETRIUM UNDER THE INFLUENCE OF PROGESTERONE. Comment [PTM] CARRIES THE SO-CALLED MANNOSE 6-PHOSPHATE LYSOSOMAL RECOGNITION MARKER ON ITS CARBOHYDRATE CHAINS. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. BELONGS TO THE UTMP SUBFAMILY. Cross-ref NCBI Seq ID: 166062 Cross-ref NCBI Seq ID: 166059 Cross-ref GenBank Accession: J04484 Cross-ref GenBank Accession: M21027 Cross-ref HSSP P01008 Cross-ref PROSITE PS00284 Created May 1, 1991 Updated Oct 1, 1996 Citation REF [1] N.H. Ing & R.M. Roberts (1989). The major progesterone- modulated proteins secreted into the sheep uterus are members of the serpin superfamily of serine protease inhibitors. J. Biol. Chem. 264, 3372-3379. MEDLINE identifier: 89123464 Signal (experimentally determined) 1351385: 1..25 Mature chain UTERINE MILK PROTEIN. 1351385: 26..429 (experimentally determined) active site REACTIVE BOND. 1351385: 390..391 glycosylation 1351385: 222 site glycosylation 1351385: 268 site Conflict K -> R (IN AA SEQUENCE). 1351385: 49 (experimentally determined) Conflict H -> L (IN AA SEQUENCE). 1351385: 53 (experimentally determined) Sequence 429 aa 1 mshrrmqlal slvfilcglf nsifcekqqh sqqhanlvll kkisafsqkm 51 eahpkafaqe lfkaliaenp kkniifspaa mtitlatlsl gikstmstnh 101 pedlelelkl ldahkclhhl vhlgrelvkq kqlrhqdilf lnskmmanqm 151 llhqirklqk mdiqmidfsd tekakkaish hvaekthtki rdlitdlnpe 201 tilclvnhif fkgilkrafq pnltqkedff lndktkvqvd mmrkteqmly 251 srseelfatm vkmpfkgnvs lilmlpdagh fdnalkklta kraklqkisn 301 frlvhltlpk fkitfdinfk hllpkinlkh llpkidpkht ltttassqhv 351 tlkaplpnle alhqveiels ehalttdtai htdnllkvpa ntkevpvvvk 401 fnrpfllfve deitqtdlfv gqvlnpqve
1346127 --------------------------------------------------- Definition GLIA DERIVED NEXIN PRECURSOR (GDN) (PROTEASE NEXIN I) (PN-1) (SERINE PROTEASE-INHIBITOR-4). Protein Name: GLIA DERIVED NEXIN PRECURSOR1346127: 1..397 SWISS-PROT Name: GDN_MOUSE, Accession: Q07235 NCBI Seq ID: 1346127 Comment [FUNCTION] THIS GLYCOPROTEIN PROMOTES NEURITE EXTENSION AND IS A SERINE PROTEASE INHIBITOR WITH ACTIVITY TOWARD THROMBIN, TRYPSIN, AND UROKINASE. BINDS HEPARIN. Comment [TISSUE SPECIFICITY] MOST ABUNDANT IN SEMINAL VESICLES. Comment [SUBCELLULAR LOCATION] EXTRACELLULAR. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 551065 Cross-ref NCBI Seq ID: 57931 Cross-ref EMBL Accession: X70296 Cross-ref EMBL Accession: X70946 Cross-ref HSSP P01008 Created Oct 1, 1994 Updated Oct 1, 1996 Citation REF [1] Data Submission: D. BELIN (1994). Citation REF [2] J.D. Vassalli, J. Huarte, D. Bosco, A.P. Sappino, N. Sappino, A. Velardi, A. Wohlwend, H. Erno, D. Monard & D. Belin (1993). Protease-nexin I as an androgen-dependent secretory product of the murine seminal vesicle. EMBO J. 12, 1871-1878. MEDLINE identifier: 93259128 Signal 1346127: 1..19 Mature chain GLIA DERIVED NEXIN. 1346127: 20..397 (experimentally determined) glycosylation 1346127: 159 site active site REACTIVE BOND. 1346127: 364..365 Gene Locus: PI7 1346127: 1..397 Sequence 397 aa 1 mnwhfpffil ttvtlysvhs qfnslsleel gsntgiqvfn qiiksrphen 51 vvvsphgias ilgmlqlgad gktkkqlstv mrynvngvgk vlkkinkaiv 101 skknkdivtv anavflrngf kmevpfavrn kdvfqcevqn vnfqdpasas 151 esinfwvkne trgmidnlls pnlidgaltr lvlvnavyfk glwksrfqpe 201 stkkrtfvag dgksyqvpml aqlsvfrsgs trtpnglwyn fielpyhges 251 ismlialpte sstplsaiip hittktidsw mntmvpkrmq lvlpkftava 301 qtdlkeplka lgitemfeps kanftkitrs eslhvshilq kakievsedg 351 tkasaattai liarssppwf ivdrpflfsi rhnptgailf lgqvnkp
1345616 --------------------------------------------------- Definition BOMAPIN (PROTEASE INHIBITOR 10). Protein Name: BOMAPIN 1345616: 1..397 SWISS-PROT Name: BOMA_HUMAN, Accession: P48595 NCBI Seq ID: 1345616 Comment [FUNCTION] MAY PLAY A ROLE IN THE REGULATION OF PROTEASE ACTIVITIES DURING HEMATOPOIESIS. Comment [TISSUE SPECIFICITY] EXPRESSED SPECIFICALLY IN THE BONE MARROW. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. BELONGS TO THE OV-SERPIN SUBFAMILY. Cross-ref NCBI Seq ID: 1065409 Cross-ref GenBank Accession: U35459 Created Feb 1, 1996 Updated Oct 1, 1996 Citation REF [1] M. Riewald & R.R. Schleef (1995). Molecular cloning of bomapin (protease inhibitor 10), a novel human serpin that is expressed specifically in the bone marrow. J. Biol. Chem. 270, 26754-26757. MEDLINE identifier: 96070759 active site REACTIVE BOND. 1345616: 362..363 Gene Locus: PI10 1345616: 1..397 Sequence 397 aa 1 mdslatsinq falelskkla esaqgkniff sswsistslt ivylgakgtt 51 aaqmaqvlqf nrdqgvkcdp esekkrkmef nlsnseeihs dfqtliseil 101 kpnddyllkt anaiygekty afhnkyledm ktyfgaepqp vnfveasdqi 151 rkdinswver qtegkiqnll pddsvdsttr milvnalyfk giwehqflvq 201 nttekpfrin ettskpvqmm fmkkklhifh iekpkavglq lyyksrdlsl 251 lillpeding leqlekaity eklnewtsad mmelyevqlh lpkfkledsy 301 dlkstlssmg msdafsqska dfsgmssarn lflsnvfhka fveineqgte 351 aaagsgseid irirvpsief nanhpflffi rhnktntilf ygrlcsp
464490 --------------------------------------------------- Definition PLACENTAL THROMBIN INHIBITOR (CYTOPLASMIC ANTIPROTEINASE) (CAP) (PROTEASE INHIBITOR 6). Protein Name: PLACENTAL THROMBIN INHIBITOR464490: 1..376 SWISS-PROT Name: PTI6_HUMAN, Accession: P35237 NCBI Seq ID: 464490 Comment [SUBCELLULAR LOCATION] CYTOPLASMIC. Comment [TISSUE SPECIFICITY] HIGHEST LEVELS IN SKELETAL MUSCLE. ALSO FOUND IN PLACENTA, CARDIAC MUSCLE, LUNG, LIVER, KIDNEY AND PANCREAS. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. BELONGS TO THE OV-SERPIN SUBFAMILY. Cross-ref NCBI Seq ID: 297412 Cross-ref NCBI Seq ID: 546088 Cross-ref EMBL Accession: Z22658 Cross-ref GenBank Accession: S69272 Cross-ref HSSP P01008 Cross-ref MIM 173321 Cross-ref PROSITE PS00284 Created Feb 1, 1994 Updated Oct 1, 1996 Citation REF [1] P. Coughlin, J. Sun, L. Cerruti, H.H. Salem & P. Bird (1993). Cloning and molecular characterization of a human intracellular serine proteinase inhibitor. Proc. Natl. Acad. Sci. U.S.A. 90, 9417-9421. MEDLINE identifier: 94022386 Citation REF [2] K.A. Morgenstern, C. Sprecher, L. Holth, D. Foster, F.J. Grant, A. Ching & W. Kisiel (1994). Complementary DNA cloning and kinetic characterization of a novel intracellular serine proteinase inhibitor: mechanism of action with trypsin and factor Xa as model proteinases. Biochemistry 33, 3432-3441. MEDLINE identifier: 94183847 active site REACTIVE BOND. 464490: 341..342 (experimentally determined) Conflict G -> E (IN REF. 2). 464490: 175 (experimentally determined) Conflict R -> S (IN REF. 2). 464490: 362 (experimentally determined) Gene Locus: PI6 464490: 1..376 Sequence 376 aa 1 mdvlaeangt falnllktlg kdnsknvffs pmsmscalam vymgakgnta 51 aqmaqilsfn ksggggdihq gfqslltevn ktgtqyllrv anrlfgeksc 101 dflssfrdsc qkfyqaemee ldfisaveks rkhintwvae ktegkiaell 151 spgsvdpltr lvlvnavyfr gnwdgqfdke nteerlfkvs kneekpvqmm 201 fkqstfkkty igeiftqilv lpyvgkelnm iimlpdettd lrtvekelty 251 ekfvewtrld mmdeeevevs lprfkleesy dmesvlrnlg mtdafelgka 301 dfsgmsqtdl slskvvhksf vevneegtea aaataaimmm rcarfvprfc 351 adhpflffiq hrktngilfc grfssp
416561 --------------------------------------------------- Definition ALPHA-1-ANTITRYPSIN HOMOLOG PRECURSOR. Protein Name: ALPHA-1-ANTITRYPSIN HOMOLOG 416561: 1..372 PRECURSOR SWISS-PROT Name: A1AT_CYPCA, Accession: P32759 NCBI Seq ID: 416561 Comment [SUBCELLULAR LOCATION] EXTRACELLULAR. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 213046 Cross-ref GenBank Accession: L08689 Cross-ref HSSP P01008 Cross-ref PROSITE PS00284 Created Oct 1, 1993 Updated Oct 1, 1996 Citation REF [1] C.J. Huang, M.S. Lee, F.L. Huang & G.D. Chang (1995). A protease inhibitor of the serpin family is a major protein in carp perimeningeal fluid: II. cDNA cloning, sequence analysis, and Escherichia coli expression. J. Neurochem. 64, 1721-1727. MEDLINE identifier: 95198028 Signal * Partial 416561: 1..372 Mature chain ALPHA-1-ANTITRYPSIN HOMOLOG. 416561: 1..372 * Partial (experimentally determined) active site REACTIVE BOND. 416561: 337..338 glycosylation 416561: 214 site glycosylation 416561: 226 site Sequence 372 aa 1 mpatcllhtm ltlpspstrn lrsiqmprar tfsspsryrn gfehagcrcq 51 gstlsqiyss lgysglqasq vnegyehlih mlghsreamq leagagvair 101 egfkvvdqfl kdvqhyynse afsvdfskpe iaaeeinqfi akktndkitn 151 mvkdldsdtv mmlinymyfr gkwdkpfdaq lthkadfkvd edttvqvdmm 201 krtgrydiyq dpvnqttvmm vpykgntsmm iifpddgkmk eleesisrhh 251 lknwhdklfr ssvdlfmpkf sitatsklkg iledmgvtda fgdtadlsgl 301 teevkvkvsq vvhkavlsvd ekgteaaaat tieimpmslp dtvilnrpfl 351 vlivedttks ilfmgkitnp te
400068 --------------------------------------------------- Definition PLASMA SERINE PROTEASE INHIBITOR PRECURSOR (PCI) (PROTEIN C INHIBITOR) (PLASMINOGEN ACTIVATOR INHIBITOR-3) (PAI3). Protein Name: PLASMA SERINE PROTEASE 400068: 1..406 INHIBITOR PRECURSOR SWISS-PROT Name: IPSP_HUMAN, Accession: P05154 NCBI Seq ID: 400068 Comment [FUNCTION] PRODUCED BY THE LIVER, THIS PROTEIN INHIBITS ACTIVATED PROTEIN C. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Comment [DISEASE] A DEFICIENCY OF PROTEIN C INHIBITOR IS THE CAUSE OF A COMBINED FACTOR V/VIII DEFICIENCY DISEASE. Cross-ref NCBI Seq ID: 189678 Cross-ref NCBI Seq ID: 180550 Cross-ref NCBI Seq ID: 546321 Cross-ref NCBI Seq ID: 1144561 Cross-ref GenBank Accession: M68516 Cross-ref GenBank Accession: J02639 Cross-ref GenBank Accession: S69366 Cross-ref GenBank Accession: U35464 Cross-ref PDB Molecule: 1PAI, Chain: (space) Cross-ref PDB Molecule: 2PAI, Chain: (space) Cross-ref MIM 227300 Cross-ref PROSITE PS00284 Created Aug 13, 1987 Updated Oct 1, 1996 Citation REF [1] K. Suzuki, Y. Deyashiki, J. Nishioka, K. Kurachi, M. Akira, S. Yamamoto & S. Hashimoto (1987). Characterization of a cDNA for human protein C inhibitor. A new member of the plasma serine protease inhibitor superfamily. J. Biol. Chem. 262, 611-616. MEDLINE identifier: 87109153 Citation REF [2] J.C. Meijers & D.W. Chung (1990). Evidence for a glycine residue at position 316 in human protein C inhibitor. Thromb. Res. 59, 389-393. MEDLINE identifier: 91048502 Citation REF [3] J.C. Meijers & D.W. Chung (1991). Organization of the gene coding for human protein C inhibitor (plasminogen activator inhibitor-3). Assignment of the gene to chromosome 14. J. Biol. Chem. 266, 15028-15034. MEDLINE identifier: 91332018 Citation REF [4] T. Hayashi & K. Suzuki (1993). Gene organization of human protein C inhibitor, a member of SERPIN family proteins encoded in five exons. Int. J. Hematol. 58, 213-224. MEDLINE identifier: 94198434 Citation REF [5] Data Submission: K.P. RADTKE, J.S. GREENGARD, J.A. FERNANDEZ, B.O. VILLOUTREIX & J.H. GRIFFIN (1996). Citation REF [6] M. Laurell & J. Stenflo (1989). Protein C inhibitor from human plasma: characterization of native and cleaved inhibitor and demonstration of inhibitor complexes with plasma kallikrein. Thromb. Haemost. 62, 885-891. MEDLINE identifier: 90085156 Citation REF [7] L.A. Kuhn, J.H. Griffin, C.L. Fisher, J.S. Greengard, B.N. Bouma, F. Espana & J.A. Tainer (1990). Elucidating the structural chemistry of glycosaminoglycan recognition by protein C inhibitor. Proc. Natl. Acad. Sci. U.S.A. 87, 8506- 8510. MEDLINE identifier: 91046026 Signal (experimentally determined) 400068: 1..19 Mature chain PLASMA SERINE PROTEASE INHIBITOR. 400068: 20..406 (experimentally determined) glycosylation 400068: 249 site glycosylation 400068: 262 site glycosylation 400068: 338 site active site REACTIVE BOND. 400068: 373..374 (experimentally determined) Variant A -> V (IN ALLELE). 400068: 55 (experimentally determined) Variant K -> E (IN ALLELE). 400068: 105 (experimentally determined) Conflict G -> R (IN REF. 1). 400068: 335 (experimentally determined) Gene Locus: PCI 400068: 1..406 Sequence 406 aa 1 mqlflllclv llspqgaslh rhhpremkkr vedlhvgatv apssrrdftf 51 dlyralasaa psqniffspv sismslamls lgagsstkmq ileglglnlq 101 kssekelhrg fqqllqelnq prdgfqlslg nalftdlvvd lqdtfvsamk 151 tlyladtfpt nfrdsagamk qindyvakqt kgkivdllkn ldsnavvimv 201 nyiffkakwe tsfnhkgtqe qdfyvtsetv vrvpmmsred qyhylldrnl 251 scrvvgvpyq gnatalfilp segkmqqven glsektlrkw lkmfkkrqle 301 lylpkfsieg syqlekvlps lgisnvftsh adlsgisnhs niqvsemvhk 351 avvevdesgt raaaatgtif tfrsarlnsq rlvfnrpflm fivdnnilfl 401 gkvnrp
266995 --------------------------------------------------- Definition SQUAMOUS CELL CARCINOMA ANTIGEN 1 (SCCA-1) (PROTEIN T4-A). Protein Name: SQUAMOUS CELL CARCINOMA 266995: 1..390 ANTIGEN 1 SWISS-PROT Name: SCC1_HUMAN, Accession: P29508 NCBI Seq ID: 266995 Comment [FUNCTION] MAY ACT AS A PROTEASE INHIBITOR TO MODULATE THE HOST IMMUNE RESPONSE AGAINST TUMOR CELLS. Comment [SUBCELLULAR LOCATION] CYTOPLASMIC. Comment [TISSUE SPECIFICITY] SQUAMOUS CELLS. Comment [DEVELOPMENTAL STAGE] ITS EXPRESSION IS CLOSELY RELATED TO CELLULAR DIFFERENTIATION IN BOTH NORMAL AND MALIGNANT SQUAMOUS CELLS. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. BELONGS TO THE OV-SERPIN SUBFAMILY. Cross-ref NCBI Seq ID: 239552 Cross-ref NCBI Seq ID: 1276436 Cross-ref NCBI Seq ID: 1172087 Cross-ref GenBank Accession: S66896 Cross-ref GenBank Accession: U19556 Cross-ref GenBank Accession: U19568 Cross-ref HSSP P01008 Cross-ref MIM 600517 Cross-ref PROSITE PS00284 Created Apr 1, 1993 Updated Oct 1, 1996 Citation REF [1] Y. Suminami, F. Kishi, K. Sekiguchi & H. Kato (1991). Squamous cell carcinoma antigen is a new member of the serine protease inhibitors. Biochem. Biophys. Res. Commun. 181, 51- 58. MEDLINE identifier: 92068241 Citation REF [2] S.S. Schneider, C. Schick, K.E. Fish, E. Miller, J.C. Pena, S.D. Treter, S.M. Hui & G.A. Silverman (1995). A serine proteinase inhibitor locus at 18q21.3 contains a tandem duplication of the human squamous cell carcinoma antigen gene. Proc. Natl. Acad. Sci. U.S.A. 92, 3147-3151. MEDLINE identifier: 95241462 active site REACTIVE BOND. 266995: 354..355 (experimentally determined) Conflict A -> T (IN REF. 2). 266995: 357 (experimentally determined) Gene Locus: SCCA1 266995: 1..390 Sequence 390 aa 1 mnslseantk fmfdlfqqfr kskennifys pisitsalgm vllgakdnta 51 qqikkvlhfd qvtenttgka atyhvdrsgn vhhqfqkllt efnkstdaye 101 lkianklfge ktylflqeyl daikkfyqts vesvdfanap eesrkkinsw 151 vesqtnekik nlipegnigs nttlvlvnai yfkgqwekkf nkedtkeekf 201 wpnkntyksi qmmrqytsfh fasledvqak vleipykgkd lsmivllpne 251 idglqkleek ltaeklmewt slqnmretrv dlhlprfkve esydlkdtlr 301 tmgmvdifng dadlsgmtgs rglvlsgvlh kafvevteeg aeaaaatavv 351 gfgsspastn eefhcnhpfl ffirqnktns ilfygrfssp
266730 --------------------------------------------------- Definition PLASMINOGEN ACTIVATOR INHIBITOR-2, TYPE A (PAI2A). Protein Name: PLASMINOGEN ACTIVATOR 266730: 1..416 INHIBITOR-2, TYPE A SWISS-PROT Name: PAI2_RAT, Accession: P29524 NCBI Seq ID: 266730 Comment [FUNCTION] PAI-2 INHIBITS UROKINASE-TYPE PLASMINOGEN ACTIVATOR. Comment [PTM] THE SIGNAL SEQUENCE IS NOT CLEAVED (BY SIMILARITY). Comment [SUBCELLULAR LOCATION] CYTOPLASMIC OR EXTRACELLULAR. (BY SIMILARITY). Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. BELONGS TO THE OV-SERPIN SUBFAMILY. Cross-ref NCBI Seq ID: 56835 Cross-ref EMBL Accession: X64563 Cross-ref HSSP P01008 Cross-ref PROSITE PS00284 Created Apr 1, 1993 Updated Oct 1, 1996 Citation REF [1] Data Submission: U. GRUNDMANN & T. REIN (1992). Signal NOT CLEAVED. 266730: 1..416 * Partial glycosylation 266730: 23 site glycosylation 266730: 228 site glycosylation 266730: 262 site glycosylation 266730: 402 site active site REACTIVE BOND. 266730: 381..382 Gene Locus: PAI2 266730: 1..416 Sequence 416 aa 1 meelsmantm falnllkqie qsnstqnifi spwsisstla ivflgaqant 51 eeqmakvlnf dkigsydltp gnpenfhgcd faqhiqrdny pvailqaqar 101 dkihsafssl sstintprlg dyllesankl fgeksarfke eyiqrckkyy 151 stepeavdfl ecanearkki nswvktqtkg eipnllpegs vdedtkmvlv 201 ntiyfkgrwk tpfqkrlngl ypfrvnlnes kpvqmmylre klnigyikdl 251 ktqilelpyi gnismflllp deiedsstgl emlereinfd nfnkwisket 301 ldeddvlvyi pkfklaqnye lkpilqrmgm edafnkgkad fsgmsesndl 351 flsevfhqat vdvneegtva aggtgavmtg rtghggpqfv adhpflffim 401 nnitrtilfv grfssp
232283 --------------------------------------------------- Definition 47 KD HEAT SHOCK PROTEIN PRECURSOR (COLLAGEN-BINDING PROTEIN 1) (GP46). Protein Name: 47 KD HEAT SHOCK PROTEIN 232283: 1..417 PRECURSOR SWISS-PROT Name: HS47_RAT, Accession: P29457 NCBI Seq ID: 232283 Comment [FUNCTION] BINDS SPECIFICALLY TO COLLAGEN. COULD BE INVOLVED AS A CHAPERONE IN THE BIOSYNTHETIC PATHWAY OF COLLAGEN. Comment [SUBCELLULAR LOCATION] ENDOPLASMIC RETICULUM LUMEN. Comment [INDUCTION] BY HEAT SHOCK AND BY RETINOIC ACID. Comment [SIMILARITY] WITH SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 204458 Cross-ref GenBank Accession: M69246 Cross-ref HSSP P05619 Cross-ref PROSITE PS00014 Cross-ref PROSITE PS00284 Created Apr 1, 1993 Updated Oct 1, 1996 Citation REF [1] E.P. Clarke, G.A. Cates, E.H. Ball & B.D. Sanwal (1991). A collagen-binding protein in the endoplasmic reticulum of myoblasts exhibits relationship with serine protease inhibitors. J. Biol. Chem. 266, 17230-17235. MEDLINE identifier: 91373337 Citation REF [2] D. Nandan, G.A. Cates, E.H. Ball & B.D. Sanwal (1990). Partial characterization of a collagen-binding, differentiation-related glycoprotein from skeletal myoblasts. Arch. Biochem. Biophys. 278, 291-296. MEDLINE identifier: 90225795 Signal (experimentally determined) 232283: 1..17 Mature chain 47 KD HEAT SHOCK PROTEIN. 232283: 18..417 (experimentally determined) glycosylation 232283: 119 site glycosylation 232283: 124 site glycosylation 232283: 394 site active site REACTIVE BOND. 232283: 376..377 other site PREVENT SECRETION FROM ER. 232283: 414..417 Gene Locus: CBP1 232283: 1..417 Sequence 417 aa 1 mrslllgtlc llavalaaev kkpveaaapg taeklsskat tlaerstgla 51 fslyqamakd qavenillsp lvvasslglv slggkattas qakavlsaek 101 lrdeevhtgl gelvrslsns tarnvtwklg srlygpssvs faddfvrssk 151 qhyncehski nfrdkrsalq sinewasqtt dgklpevtkd vertdgallv 201 namffkphwd ekfhhkmvdn rgfmvtrsyt vgvtmmhrtg lynyyddeke 251 klqlvempla hklssliilm phhveplerl eklltkeqlk twmgkmqkka 301 vaislpkgvv evthdlqkhl aglglteaid knkadlsrms gkkdlylasv 351 fhatafewdt egnpfdqdiy greelrspkl fyadhpfifl vrdnqsgsll 401 figrlvrpkg dkmrdel
129581 --------------------------------------------------- Definition PLASMINOGEN ACTIVATOR INHIBITOR-2, MACROPHAGE (PAI-2). Protein Name: PLASMINOGEN ACTIVATOR 129581: 1..415 INHIBITOR-2, MACROPHAGE SWISS-PROT Name: PAI2_MOUSE, Accession: P12388 NCBI Seq ID: 129581 Comment [FUNCTION] PAI-2 INHIBITS UROKINASE-TYPE PLASMINOGEN ACTIVATOR. THE MONOCYTE DERIVED PAI-2 IS DISTINCT FROM THE ENDOTHELIAL CELL-DERIVED PAI-1. Comment [PTM] THE SIGNAL SEQUENCE IS NOT CLEAVED. Comment [SUBCELLULAR LOCATION] CYTOPLASMIC OR EXTRACELLULAR. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. BELONGS TO THE OV-SERPIN SUBFAMILY. Cross-ref NCBI Seq ID: 53590 Cross-ref EMBL Accession: X16490 Cross-ref HSSP P01008 Cross-ref PROSITE PS00284 Created Oct 1, 1989 Updated Oct 1, 1996 Citation REF [1] D. Belin, A. Wohlwend, W.D. Schleuning, E.K. Kruithof & J.D. Vassalli (1989). Facultative polypeptide translocation allows a single mRNA to encode the secreted and cytosolic forms of plasminogen activators inhibitor 2. EMBO J. 8, 3287-3294. MEDLINE identifier: 90059920 Citation REF [2] Data Submission: D. BELIN (1989). Signal NOT CLEAVED. 129581: 1..415 * Partial (experimentally determined) glycosylation 129581: 23 site glycosylation 129581: 75 site glycosylation 129581: 261 site glycosylation 129581: 339 site active site REACTIVE BOND. 129581: 380..381 (experimentally determined) Gene Locus: PAI2 129581: 1..415 Sequence 415 aa 1 meelsmantm falnllkqie ksnstqnifi spwsisstla ivllgaggnt 51 eqqmakvlqf neigsygitt rnpenfsgcd faqqiqkeny psailqaqag 101 dkihsafssl sstintpqgd yllesanklf geksarfkee yiqlskkyys 151 tepeavdfle caeearekin swvktqtkge ipnllpegsv dedtkmvlvn 201 avyfkgkwkt pfekklngly pfrvnshesi pvqmmflhak lnigyikdlk 251 tqilelphtg nismllllpd eiedastgle lleseinfan fnkwiskdtl 301 deddvvvyip kfklaqsyel ksilqsmgme dafnkgkanf sgmserndlf 351 lsevfhqasv dvteegtvaa ggtgavmtgr tghggpqfva dhpflffimd 401 kithtilfvg rfssp
129578 --------------------------------------------------- Definition PLASMINOGEN ACTIVATOR INHIBITOR-1 PRECURSOR (PAI-1). Protein Name: PLASMINOGEN ACTIVATOR 129578: 1..402 INHIBITOR-1 PRECURSOR SWISS-PROT Name: PAI1_RAT, Accession: P20961 NCBI Seq ID: 129578 Comment [FUNCTION] THIS INHIBITOR ACTS AS "BAIT" FOR TISSUE PLASMINOGEN ACTIVATOR, UROKINASE, AND PROTEIN C. ITS RAPID INTERACTION WITH TPA MAY FUNCTION AS A MAJOR CONTROL POINT IN THE REGULATION OF FIBRINOLYSIS. Comment PAI1 IS INACTIVATED BY PROTEOLYTIC ATTACK OF THE UROKINASE- TYPE (U-PA) AND THE TISSUE-TYPE (TPA), CLEAVING THE 369(R)- 370(M) BOND. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 205966 Cross-ref NCBI Seq ID: 577501 Cross-ref GenBank Accession: J05206 Cross-ref GenBank Accession: M24067 Cross-ref HSSP P01008 Cross-ref PROSITE PS00284 Created Feb 1, 1991 Updated Oct 1, 1996 Citation REF [1] C.J. Bruzdzinski, M. Riordan-Johnson, E.C. Nordby, S.M. Suter & T.D. Gelehrter (1990). Isolation and characterization of the rat plasminogen activator inhibitor-1 gene. J. Biol. Chem. 265, 2078-2085. MEDLINE identifier: 90130456 Citation REF [2] R. Zeheb & T.D. Gelehrter (1988). Cloning and sequencing of cDNA for the rat plasminogen activator inhibitor-1. Gene 73, 459-468. MEDLINE identifier: 89211983 Signal 129578: 1..23 Mature chain PLASMINOGEN ACTIVATOR INHIBITOR I. 129578: 24..402 (experimentally determined) active site REACTIVE BOND. 129578: 369..370 (experimentally determined) glycosylation 129578: 88 site glycosylation 129578: 232 site glycosylation 129578: 288 site glycosylation 129578: 352 site Gene Locus: PAI1 129578: 1..402 Sequence 402 aa 1 mqmssaltcl tlglvlvfgk gfasplpesh taqqatnfgv kvfqhvvqas 51 kdrnvvfspy gvssvlamlq lttagktrqq iqdamgfnis ergtapalrk 101 lskelmgswn kneistadai fvqrdlelvq gfmphffklf rttvkqvdfs 151 everarfiin dwverhtkgm isdllakgav neltrlvlvn alyfngqwkt 201 pfleasthqr lfhksdgsti svpmmaqnnk fnytefttpd gheydilelp 251 yhgetlsmfi aapfekdvpl saitnildae lirqwksnmt rlprllilpk 301 fsletevdlr gpleklgmtd ifsstqadft slsdqeqlsv aqalqkvkie 351 vnesgtvass stailvsarm aptemvldrs flfvvrhnpt etilfmgqlm 401 ep
129577 --------------------------------------------------- Definition PLASMINOGEN ACTIVATOR INHIBITOR-1 PRECURSOR (PAI-1). Protein Name: PLASMINOGEN ACTIVATOR 129577: 1..402 INHIBITOR-1 PRECURSOR SWISS-PROT Name: PAI1_MOUSE, Accession: P22777 NCBI Seq ID: 129577 Comment [FUNCTION] THIS INHIBITOR ACTS AS "BAIT" FOR TISSUE PLASMINOGEN ACTIVATOR, UROKINASE, AND PROTEIN C. ITS RAPID INTERACTION WITH TPA MAY FUNCTION AS A MAJOR CONTROL POINT IN THE REGULATION OF FIBRINOLYSIS. Comment PAI1 IS INACTIVATED BY PROTEOLYTIC ATTACK OF THE UROKINASE- TYPE (U-PA) AND THE TISSUE-TYPE (TPA), CLEAVING THE 369(R)- 370(M) BOND. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 200220 Cross-ref GenBank Accession: M33960 Cross-ref HSSP P01008 Cross-ref PROSITE PS00284 Created Aug 1, 1991 Updated Oct 1, 1996 Citation REF [1] G.C. Prendergast, L.E. Diamond, D. Dahl & M.D. Cole (1990). The c-myc-regulated gene mrl encodes plasminogen activator inhibitor 1. Mol. Cell. Biol. 10, 1265-1269. MEDLINE identifier: 90158593 Signal 129577: 1..23 Mature chain PLASMINOGEN ACTIVATOR INHIBITOR I. 129577: 24..402 (experimentally determined) active site REACTIVE BOND. 129577: 369..370 (experimentally determined) glycosylation 129577: 232 site glycosylation 129577: 288 site glycosylation 129577: 352 site Gene Locus: PAI1 129577: 1..402 Sequence 402 aa 1 mqmssalacl ilglvlvsgk gftlplresh tahqatdfgv kvfqqvvqas 51 kdrnvvfspy gvssvlamlq mttagktrrq iqdamgfkvn ekgtahalrq 101 lskelmgpwn kneistadai fvqrdlelvq gfmphffklf qtmvkqvdfs 151 everarfiin dwverhtkgm indllakgav deltrlvlvn alyfsgqwkt 201 pfleasthqr lfhksdgstv svpmmaqsnk fnytefttpd gleydvvelp 251 yqrdtlsmfi aapfekdvhl saltnildae lirqwkgnmt rlprllilpk 301 fsletevdlr gpleklgmpd mfsatladft slsdqeqlsv aqalqkvrie 351 vnesgtvass stafvisarm aptemvidrs flfvvrhnpt etilfmgqvm 401 ep
129576 --------------------------------------------------- Definition PLASMINOGEN ACTIVATOR INHIBITOR-1 PRECURSOR, ENDOTHELIAL (PAI- 1). Protein Name: PLASMINOGEN ACTIVATOR 129576: 1..402 INHIBITOR-1 PRECURSOR, ENDOTHELIAL SWISS-PROT Name: PAI1_HUMAN, Accession: P05121 NCBI Seq ID: 129576 Comment [FUNCTION] THIS INHIBITOR ACTS AS "BAIT" FOR TISSUE PLASMINOGEN ACTIVATOR, UROKINASE, AND PROTEIN C. ITS RAPID INTERACTION WITH TPA MAY FUNCTION AS A MAJOR CONTROL POINT IN THE REGULATION OF FIBRINOLYSIS. Comment PAI1 IS INACTIVATED BY PROTEOLYTIC ATTACK OF THE UROKINASE- TYPE (U-PA) AND THE TISSUE-TYPE (TPA), CLEAVING THE 369(R)- 370(M) BOND. Comment TWO TYPES OF PAI HAVE BEEN IDENTIFIED. PAI-1 IS AN ACID-STABLE GLYCOPROTEIN FOUND IN PLASMA AND PLATELETS AND IN ENDOTHELIAL, HEPATOMA, AND FIBROSARCOMA CELLS. Comment VASCULAR ENDOTHELIAL CELLS MAY BE THE PRIMARY SITE OF SYNTHESIS OF PLASMA PAI. Comment [DISEASE] HIGH CONCENTRATIONS OF THIS PROTEIN HAVE BEEN ASSOCIATED WITH HUMAN THROMBOEMBOLIC DISEASE. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 35272 Cross-ref NCBI Seq ID: 386997 Cross-ref NCBI Seq ID: 35264 Cross-ref NCBI Seq ID: 35261 Cross-ref NCBI Seq ID: 189542 Cross-ref NCBI Seq ID: 189578 Cross-ref NCBI Seq ID: 35245 Cross-ref NCBI Seq ID: 1335247 Cross-ref NCBI Seq ID: 31147 Cross-ref NCBI Seq ID: 386996 Cross-ref NCBI Seq ID: 755747 Cross-ref EMBL Accession: X04429 Cross-ref GenBank Accession: M14083 Cross-ref EMBL Accession: X04729 Cross-ref EMBL Accession: X04731 Cross-ref GenBank Accession: M16006 Cross-ref GenBank Accession: M22321 Cross-ref EMBL Accession: X13323 Cross-ref EMBL Accession: X13338 Cross-ref EMBL Accession: X13339 Cross-ref EMBL Accession: X13340 Cross-ref EMBL Accession: X13341 Cross-ref EMBL Accession: X13342 Cross-ref EMBL Accession: X13343 Cross-ref EMBL Accession: X13344 Cross-ref EMBL Accession: X13345 Cross-ref EMBL Accession: X12701 Cross-ref GenBank Accession: J03764 Cross-ref EMBL Accession: X04744 Cross-ref HSSP P01008 Cross-ref MIM 173360 Cross-ref PROSITE PS00284 Created Aug 13, 1987 Updated Oct 1, 1996 Citation REF [1] H. Pannekoek, H. Veerman, H. Lambers, P. Diergaarde, C.L. Verweij, A.J. van Zonneveld & J.A. van Mourik (1986). Endothelial plasminogen activator inhibitor (PAI): a new member of the Serpin gene family. EMBO J. 5, 2539-2544. MEDLINE identifier: 87053819 Citation REF [2] D.J. Loskutoff, M. Linders, J. Keijer, H. Veerman, H. van Heerikhuizen & H. Pannekoek (1987). Structure of the human plasminogen activator inhibitor 1 gene: nonrandom distribution of introns. Biochemistry 26, 3763-3768. MEDLINE identifier: 88000586 Citation REF [3] D. Ginsburg, R. Zeheb, A.Y. Yang, U.M. Rafferty, P.A. Andreasen, L. Nielsen, K. Dano, R.V. Lebo & T.D. Gelehrter (1986). cDNA cloning of human plasminogen activator-inhibitor from endothelial cells. J. Clin. Invest. 78, 1673-1680. MEDLINE identifier: 87058123 Citation REF [4] M. Follo & D. Ginsburg (1989). Structure and expression of the human gene encoding plasminogen activator inhibitor, PAI- 1. Gene 84, 447-453. MEDLINE identifier: 90128289 Citation REF [5] L. Strandberg, D. Lawrence & T. Ny (1988). The organization of the human-plasminogen-activator-inhibitor-1 gene. Implications on the evolution of the serine-protease inhibitor family. Eur. J. Biochem. 176, 609-616. MEDLINE identifier: 89005111 Citation REF [6] P.J. Bosma, E.A. van den Berg, T. Kooistra, D.R. Siemieniak & J.L. Slightom (1988). Human plasminogen activator inhibitor-1 gene. Promoter and structural gene nucleotide sequences. J. Biol. Chem. 263, 9129-9141. MEDLINE identifier: 88243790 Citation REF [7] Data Submission: H. PANNEKOEK (1992). Citation REF [8] T. Ny, M. Sawdey, D. Lawrence, J.L. Millan & D.J. Loskutoff (1986). Cloning and sequence of a cDNA coding for the human beta-migrating endothelial-cell-type plasminogen activator inhibitor. Proc. Natl. Acad. Sci. U.S.A. 83, 6776-6780. MEDLINE identifier: 86313660 Citation REF [9] P.A. Andreasen, A. Riccio, K.G. Welinder, R. Douglas, R. Sartorio, L.S. Nielsen, C. Oppenheimer, F. Blasi & K. Dano (1986). Plasminogen activator inhibitor type-1: reactive center and amino-terminal heterogeneity determined by protein and cDNA sequencing. FEBS Lett. 209, 213-218. MEDLINE identifier: 87080762 Citation REF [10] T.C. Wun & K.K. Kretzmer (1987). cDNA cloning and expression in E. coli of a plasminogen activator inhibitor (PAI) related to a PAI produced by Hep G2 hepatoma cell. FEBS Lett. 210, 11- 16. MEDLINE identifier: 87105925 Citation REF [11] J. Mottonen, A. Strand, J. Symersky, R.M. Sweet, D.E. Danley, K.F. Geoghegan, R.D. Gerard & E.J. Goldsmith (1992). Structural basis of latency in plasminogen activator inhibitor- 1. Nature 355, 270-273. MEDLINE identifier: 92114970 Signal (experimentally determined) 129576: 1..23 Mature chain PLASMINOGEN ACTIVATOR INHIBITOR I. 129576: 24..402 (experimentally determined) active site REACTIVE BOND. 129576: 369..370 (experimentally determined) glycosylation 129576: 232 site glycosylation 129576: 288 site glycosylation 129576: 352 site Conflict A -> T (IN REF. 5). 129576: 15 (experimentally determined) Conflict R -> A (IN REF. 7). 129576: 53 (experimentally determined) Conflict V -> L (IN REF. 2). 129576: 55 (experimentally determined) Conflict G -> V (IN REF. 7). 129576: 75 (experimentally determined) Conflict R -> K (IN REF. 7). 129576: 138 (experimentally determined) Conflict QLI -> HVM (IN REF. 7). 129576: 280..282 (experimentally determined) Gene Locus: PAI1 129576: 1..402 Sequence 402 aa 1 mqmspaltcl vlglalvfge gsavhhppsy vahlasdfgv rvfqqvaqas 51 kdrnvvfspy gvasvlamlq lttggetqqq iqaamgfkid dkgmapalrh 101 lykelmgpwn kdeisttdai fvqrdlklvq gfmphffrlf rstvkqvdfs 151 everarfiin dwvkthtkgm isnllgkgav dqltrlvlvn alyfngqwkt 201 pfpdssthrr lfhksdgstv svpmmaqtnk fnytefttpd ghyydilelp 251 yhgdtlsmfi aapyekevpl saltnilsaq lishwkgnmt rlprllvlpk 301 fsletevdlr kplenlgmtd mfrqfqadft slsdqeplhv aqalqkvkie 351 vnesgtvass stavivsarm apeeiimdrp flfvvrhnpt gtvlfmgqvm 401 ep
124096 --------------------------------------------------- Definition PLASMA PROTEASE C1 INHIBITOR PRECURSOR (C1 INH). Protein Name: PLASMA PROTEASE C1 124096: 1..500 INHIBITOR PRECURSOR SWISS-PROT Name: IC1_HUMAN, Accession: P05155 NCBI Seq ID: 124096 Comment [FUNCTION] ACTIVATION OF THE C1 COMPLEX IS UNDER CONTROL OF THE C1-INHIBITOR. IT FORM A PROTEOLYTICALLY INACTIVE STOICHIOMETRIC COMPLEX WITH THE C1R OR C1S PROTEASES. MAY PLAY A POTENTIALLY CRUCIAL ROLE IN REGULATING IMPORTANT PHYSIOLOGICAL PATHWAYS INCLUDING COMPLEMENT ACTIVATION, BLOOD COAGULATION, FIBRINOLYSIS AND THE GENERATION OF KININS. Comment [PTM] HIGHLY GLYCOSYLATED (49%). Comment [POLYMORPHISM] THERE ARE TWO ALLELES. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Comment [DISEASE] DEFECTS IN C1NH ARE THE CAUSE OF HEREDITARY ANGIONEUROTIC EDEMA (HAE) ALSO CALLED TYPE II HEREDITARY ANGIOEDEMA (TYPE-II HANE). Cross-ref NCBI Seq ID: 1340170 Cross-ref NCBI Seq ID: 29535 Cross-ref NCBI Seq ID: 1197499 Cross-ref NCBI Seq ID: 179617 Cross-ref NCBI Seq ID: 179621 Cross-ref NCBI Seq ID: 553208 Cross-ref NCBI Seq ID: 179619 Cross-ref NCBI Seq ID: 553230 Cross-ref EMBL Accession: X07577 Cross-ref EMBL Accession: X54486 Cross-ref EMBL Accession: X07427 Cross-ref GenBank Accession: M14036 Cross-ref GenBank Accession: M13656 Cross-ref GenBank Accession: M13203 Cross-ref GenBank Accession: M13690 Cross-ref GenBank Accession: M30688 Cross-ref HSSP P01011 Cross-ref SWISS-2DPAGE P05155 Cross-ref MIM 106100 Cross-ref PROSITE PS00284 Created Aug 13, 1987 Updated Oct 1, 1996 Citation REF [1] P.E. Carter, B. Dunbar & J.E. Fothergill (1988). Genomic and cDNA cloning of the human C1 inhibitor. Intron-exon junctions and comparison with other serpins. Eur. J. Biochem. 173, 163- 169. MEDLINE identifier: 88185313 Citation REF [2] P.E. Carter, C. Duponchel, M. Tosi & J.E. Fothergill (1991). Complete nucleotide sequence of the gene for human C1 inhibitor with an unusually high density of Alu elements. Eur. J. Biochem. 197, 301-308. MEDLINE identifier: 91224119 Citation REF [3] S.C. BOCK, K. SKRIVER, E. NIELSEN, H.-C. THOGERSEN, B. WIMAN, V.H. DONALDSON, R.L. EDDY, J. MARRINAN, E. RADZIEJEWSKA, R. HUBER, T.B. SHOWS & S. MAGNUSSON (1986). Human C1 inhibitor: primary structure, cDNA cloning, and chromosomal localization. Biochemistry 25, 4292-4301. MEDLINE identifier: 87000544 Citation REF [4] B.G. Que & P.H. Petra (1986). Isolation and analysis of a cDNA coding for human C1 inhibitor. Biochem. Biophys. Res. Commun. 137, 620-625. MEDLINE identifier: 86268965 Citation REF [5] G. Rauth, G. Schumacher, P. Buckel & W. Muller-Esterl (1988). Molecular cloning of the cDNA coding for human C1 inhibitor. Protein Seq. Data Anal. 1, 251-257. MEDLINE identifier: 88276848 Citation REF [6] M. Tosi, C. Duponchel, P. Bourgarel, M. Colomb & T. Meo (1986). Molecular cloning of human C1 inhibitor: sequence homologies with alpha 1-antitrypsin and other members of the serpins superfamily. Gene 42, 265-272. MEDLINE identifier: 86276001 Citation REF [7] A.E. Davis, A.S. Whitehead, R.A. Harrison, A. Dauphinais, G.A. Bruns, M. Cicardi & F.S. Rosen (1986). Human inhibitor of the first component of complement, C1: characterization of cDNA clones and localization of the gene to chromosome 11. Proc. Natl. Acad. Sci. U.S.A. 83, 3161-3165. MEDLINE identifier: 86205856 Citation REF [8] D. Stoppa-Lyonnet, P.E. Carter, T. Meo & M. Tosi (1990). Clusters of intragenic Alu repeats predispose the human C1 inhibitor locus to deleterious rearrangements. Proc. Natl. Acad. Sci. U.S.A. 87, 1551-1555. MEDLINE identifier: 90160364 Citation REF [9] R.A. Harrison (1983). Human C1 inhibitor: improved isolation and preliminary structural characterization. Biochemistry 22, 5001-5007. MEDLINE identifier: 84053355 Citation REF [10] P.E. Stein & R.W. Carrell (1995). What do dysfunctional serpins tell us about molecular mobility and disease?. Nat. Struct. Biol. 2, 96-113. MEDLINE identifier: 95269065 Citation REF [11] K.S. Aulak, P.A. Pemberton, F.S. Rosen, R.W. Carrell, P.J. Lachmann & R.A. Harrison (1988). Dysfunctional C1- inhibitor(At), isolated from a type II hereditary-angio-oedema plasma, contains a P1 'reactive centre' (Arg444----His) mutation. Biochem. J. 253, 615-618. MEDLINE identifier: 89025602 Citation REF [12] K.S. Aulak, M. Cicardi & R.A. Harrison (1990). Identification of a new P1 residue mutation (444Arg----Ser) in a dysfunctional C1 inhibitor protein contained in a type II hereditary angioedema plasma. FEBS Lett. 266, 13-16. MEDLINE identifier: 90306337 Citation REF [13] N.J. Levy, N. Ramesh, M. Cicardi, R.A. Harrison & A.E. Davis (1990). Type II hereditary angioneurotic edema that may result from a single nucleotide change in the codon for alanine-436 in the C1 inhibitor gene. Proc. Natl. Acad. Sci. U.S.A. 87, 265-268. MEDLINE identifier: 90115854 Citation REF [14] R.B. Parad, J. Kramer, R.C. Strunk, F.S. Rosen & A.E. Davis (1990). Dysfunctional C1 inhibitor Ta: deletion of Lys-251 results in acquisition of an N-glycosylation site. Proc. Natl. Acad. Sci. U.S.A. 87, 6786-6790. MEDLINE identifier: 90370868 Citation REF [15] Z.M. SIDDIQUE, A.R. MCPHADEN & K. WHALEY (1991)CLIN. EXP. IMMUNOL. 86, 11-11. Citation REF [16] D. Frangi, K.S. Aulak, M. Cicardi, R.A. Harrison & A.E. Davis (1992). A dysfunctional C1 inhibitor protein with a new reactive center mutation (Arg-444-->Leu). FEBS Lett. 301, 34- 36. MEDLINE identifier: 93083618 Citation REF [17] A.E. Davis, K. Aulak, R.B. Parad, H.P. Stecklein, E. Eldering, C.E. Hack, J. Kramer, R.C. Strunk, J. Bissler & F.S. Rosen (1992). C1 inhibitor hinge region mutations produce dysfunction by different mechanisms. Nature Genet. 1, 354- 358. MEDLINE identifier: 93251025 Citation REF [18] A.E. Davis, J.J. Bissler & M. Cicardi (1993). Mutations in the C1 inhibitor gene that result in hereditary angioneurotic edema. Behring Inst. Mitt. 93, 313-320. MEDLINE identifier: 94226584 Signal (experimentally determined) 124096: 1..22 Mature chain PLASMA PROTEASE C1 INHIBITOR. 124096: 23..500 (experimentally determined) Domain 7 X 4 AA TANDEM REPEATS OF [QE]-P- 124096: 85..119 T-[TQ]. (experimentally determined) Repetitive 1. 124096: 85..88 region (experimentally determined) Repetitive 2. 124096: 89..92 region (experimentally determined) Repetitive 3. 124096: 93..96 region (experimentally determined) Repetitive 4. 124096: 97..100 region (experimentally determined) Repetitive 5. 124096: 101..104 region (experimentally determined) Repetitive 6. 124096: 105..108 region (experimentally determined) Repetitive 7. 124096: 116..119 region (experimentally determined) active site REACTIVE BOND. 124096: 466..467 (experimentally determined) disulfide bond (experimentally determined) 124096: 123 bond 428 disulfide bond (experimentally determined) 124096: 130 bond 205 glycosylation (experimentally determined) 124096: 25 site glycosylation (experimentally determined) 124096: 48 site glycosylation (experimentally determined) 124096: 64 site glycosylation (experimentally determined) 124096: 69 site glycosylation (experimentally determined) 124096: 71 site glycosylation (experimentally determined) 124096: 81 site glycosylation (experimentally determined) 124096: 83 site glycosylation (experimentally determined) 124096: 88 site glycosylation (experimentally determined) 124096: 92 site glycosylation (experimentally determined) 124096: 96 site glycosylation (experimentally determined) 124096: 238 site glycosylation (experimentally determined) 124096: 253 site glycosylation IN VARIANT TA. 124096: 272 site (experimentally determined) glycosylation (experimentally determined) 124096: 352 site Variant MISSING (IN TA; TYPE-II HANE; 124096: 273 CREATES A NEW GLYCOSYLATION SITE). (experimentally determined) Variant G -> R (IN TYPE-II HANE). 124096: 429 (experimentally determined) Variant V -> E (IN WE; TYPE-II HANE). 124096: 454 (experimentally determined) Variant A -> E (IN MA; TYPE-II HANE). 124096: 456 (experimentally determined) Variant A -> T (IN MO; TYPE-II HANE). 124096: 458 (experimentally determined) Variant A -> V (IN TYPE-II HANE). 124096: 458 (experimentally determined) Variant R -> C (IN DA; TYPE-II HANE). 124096: 466 (experimentally determined) Variant R -> H (IN AT; TYPE-II HANE). 124096: 466 (experimentally determined) Variant R -> S (IN TYPE-II HANE). 124096: 466 (experimentally determined) Variant R -> L (IN TYPE-II HANE). 124096: 466 (experimentally determined) Variant V -> M (IN TYPE-II HANE). 124096: 473 (experimentally determined) Variant Q -> E. 124096: 474 (experimentally determined) Variant F -> S (IN TYPE-II HANE). 124096: 477 (experimentally determined) Variant V -> M (IN A SECOND ALLELE). 124096: 480 (experimentally determined) Variant L -> P (IN TYPE-II HANE). 124096: 481 (experimentally determined) Variant L -> R (IN TYPE-II HANE). 124096: 481 (experimentally determined) Variant P -> R (IN TYPE-II HANE). 124096: 489 (experimentally determined) Conflict E -> Q (IN REF. 3). 124096: 187 (experimentally determined) Conflict K -> R (IN REF. 4). 124096: 306 (experimentally determined) Conflict HFKNSVI -> QLQKLSY (IN REF. 7). 124096: 314..320 (experimentally determined) Conflict V -> M (IN REF. 7). 124096: 322 (experimentally determined) Conflict V -> L (IN REF. 7). 124096: 332 (experimentally determined) Conflict MEQALS -> TGTGSQ (IN REF. 7). 124096: 370..375 (experimentally determined) Conflict E -> V (IN REF. 7). 124096: 417 (experimentally determined) Conflict S -> F (IN REF. 7). 124096: 439 (experimentally determined) Gene Locus: C1NH 124096: 1..500 Sequence 500 aa 1 masrltlltl lllllagdra ssnpnatsss sqdpeslqdr gegkvattvi 51 skmlfvepil evsslpttns ttnsatkita nttdepttqp ttepttqpti 101 qptqpttqlp tdsptqpttg sfcpgpvtlc sdleshstea vlgdalvdfs 151 lklyhafsam kkvetnmafs pfsiaslltq vllgagentk tnlesilsyp 201 kdftcvhqal kgfttkgvts vsqifhspdl airdtfvnas rtlysssprv 251 lsnnsdanle lintwvaknt nnkisrllds lpsdtrlvll naiylsakwk 301 ttfdpkktrm epfhfknsvi kvpmmnskky pvahfidqtl kakvgqlqls 351 hnlslvilvp qnlkhrledm eqalspsvfk aimeklemsk fqptlltlpr 401 ikvttsqdml simekleffd fsydlnlcgl tedpdlqvsa mqhqtvlelt 451 etgveaaaas aisvartllv fevqqpflfv lwdqqhkfpv fmgrvydpra
123577 --------------------------------------------------- Definition 47 KD HEAT SHOCK PROTEIN PRECURSOR (COLLAGEN-BINDING PROTEIN 1) (SERINE PROTEASE INHIBITOR J6). Protein Name: 47 KD HEAT SHOCK PROTEIN 123577: 1..417 PRECURSOR SWISS-PROT Name: HS47_MOUSE, Accession: P19324 NCBI Seq ID: 123577 Comment [FUNCTION] BINDS SPECIFICALLY TO COLLAGEN. COULD BE INVOLVED AS A CHAPERONE IN THE BIOSYNTHETIC PATHWAY OF COLLAGEN. Comment [SUBCELLULAR LOCATION] ENDOPLASMIC RETICULUM LUMEN. Comment [INDUCTION] BY HEAT SHOCK AND BY RETINOIC ACID. Comment [SIMILARITY] WITH SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 51450 Cross-ref NCBI Seq ID: 200966 Cross-ref NCBI Seq ID: 303678 Cross-ref EMBL Accession: X60676 Cross-ref GenBank Accession: J05609 Cross-ref DDBJ Accession: D12907 Cross-ref HSSP P05619 Cross-ref PROSITE PS00014 Cross-ref PROSITE PS00284 Created Nov 1, 1990 Updated Oct 1, 1996 Citation REF [1] H. Takechi, K. Hirayoshi, A. Nakai, H. Kudo, S. Saga & K. Nagata (1992). Molecular cloning of a mouse 47-kDa heat-shock protein (HSP47), a collagen-binding stress protein, and its expression during the differentiation of F9 teratocarcinoma cells. Eur. J. Biochem. 206, 323-329. MEDLINE identifier: 92283255 Citation REF [2] S.Y. Wang & L.J. Gudas (1990). A retinoic acid-inducible mRNA from F9 teratocarcinoma cells encodes a novel protease inhibitor homologue. J. Biol. Chem. 265, 15818-15822. MEDLINE identifier: 90368798 Citation REF [3] S.Y. Wang & L.J. Gudas (1991). A retinoic acid-inducible mRNA from F9 teratocarcinoma cells encodes a novel protease inhibitor homolog. J. Biol. Chem. 266, 14135. MEDLINE identifier: 91310706 Citation REF [4] N. Hosokawa, H. Takechi, S. Yokota, K. Hirayoshi & K. Nagata (1993). Structure of the gene encoding the mouse 47-kDa heat- shock protein (HSP47). Gene 126, 187-193. MEDLINE identifier: 93246243 Signal (experimentally determined) 123577: 1..17 Mature chain 47 KD HEAT SHOCK PROTEIN. 123577: 18..417 (experimentally determined) glycosylation 123577: 119 site glycosylation 123577: 124 site glycosylation 123577: 394 site active site REACTIVE BOND. 123577: 376..377 other site PREVENT SECRETION FROM ER. 123577: 414..417 Conflict A -> P (IN REF. 2). 123577: 176 (experimentally determined) Conflict R -> K (IN REF. 4). 123577: 212 (experimentally determined) Conflict R -> K (IN REF. 4). 123577: 216 (experimentally determined) Conflict MP -> IA (IN REF. 2). 123577: 270..271 (experimentally determined) Conflict L -> S (IN REF. 2). 123577: 277 (experimentally determined) Gene Locus: CBP1 123577: 1..417 Sequence 417 aa 1 mrslllgtlc llavalaaev kkpleaaapg taeklsskat tlaerstgla 51 fslyqamakd qavenillsp lvvasslglv slggkattas qakavlsaek 101 lrdeevhtgl gellrslsns tarnvtwklg srlygpssvs faddfvrssk 151 qhyncehski nfrdkrsalq sinewasqtt dgklpevtkd vertdgallv 201 namffkphwd erfhhrmvdn rgfmvtrsyt vgvtmmhrtg lynyyddeke 251 klqmvempla hklssliilm phhveplerl eklltkeqlk awmgkmqkka 301 vaislpkgvv evthdlqkhl aglglteaid knkadlsrms gkkdlylasv 351 fhatafewdt egnpfdqdiy greelrspkl fyadhpfifl vrdnqsgsll 401 figrlvrpkg dkmrdel
123576 --------------------------------------------------- Definition 47 KD HEAT SHOCK PROTEIN PRECURSOR (COLLAGEN-BINDING PROTEIN 1) (COLLIGIN 1). Protein Name: 47 KD HEAT SHOCK PROTEIN 123576: 1..417 PRECURSOR SWISS-PROT Name: HS47_HUMAN, Accession: P29043 NCBI Seq ID: 123576 Comment [FUNCTION] BINDS SPECIFICALLY TO COLLAGEN. COULD BE INVOLVED AS A CHAPERONE IN THE BIOSYNTHETIC PATHWAY OF COLLAGEN. Comment [SUBCELLULAR LOCATION] ENDOPLASMIC RETICULUM LUMEN. Comment [INDUCTION] BY HEAT SHOCK. Comment [SIMILARITY] WITH SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 30130 Cross-ref EMBL Accession: X61598 Cross-ref HSSP P05619 Cross-ref MIM 600942 Cross-ref PROSITE PS00014 Cross-ref PROSITE PS00284 Created Dec 1, 1992 Updated Oct 1, 1996 Citation REF [1] E.P. Clarke & B.D. Sanwal (1992). Cloning of a human collagen- binding protein, and its homology with rat gp46, chick hsp47 and mouse J6 proteins. Biochim. Biophys. Acta 1129, 246-248. MEDLINE identifier: 92110393 Signal 123576: 1..17 Mature chain 47 KD HEAT SHOCK PROTEIN. 123576: 18..417 (experimentally determined) glycosylation 123576: 119 site glycosylation 123576: 124 site active site REACTIVE BOND. 123576: 376..377 other site PREVENT SECRETION FROM ER. 123576: 414..417 Gene Locus: CBP1 123576: 1..417 Sequence 417 aa 1 mrslllgtlc llavalaaev kkpveaaapg taeklsskat tlaepstgla 51 fslyqamakd qavenilvsp vvvasslglv slggkattas qakavlsaeq 101 lrdeevhagl gellrslsns tarnvtwklg srlygpssvs faddfvrssk 151 qhyncehski nfpdkrsalq sinewaaqtt dgklpevtkd vertdgallv 201 namffkphwd ekfhhkmvdn rgfmvtrsyt vgvtmmhrtg lynyyddeke 251 klqlvempla hklssliilm phhveplerl eklltkeqlk iwmgkmqkka 301 vaislpkgvv evthdlqkhl aglglteaid knkadlsrms gkkdlylasv 351 fhatafeldt dgnpfdqdiy greelrspkl fyadhpfifl vrdtqsgsll 401 figrlvrlkg dkmrdel
121110 --------------------------------------------------- Definition GLIA DERIVED NEXIN PRECURSOR (GDN) (PROTEASE NEXIN I) (PN-1) (PROTEASE INHIBITOR 7). Protein Name: GLIA DERIVED NEXIN PRECURSOR121110: 1..398 SWISS-PROT Name: GDN_HUMAN, Accession: P07093 NCBI Seq ID: 121110 Comment [FUNCTION] THIS GLYCOPROTEIN PROMOTES NEURITE EXTENSION AND IS A SERINE PROTEASE INHIBITOR WITH ACTIVITY TOWARD THROMBIN, TRYPSIN, AND UROKINASE. BINDS HEPARIN. Comment [SUBCELLULAR LOCATION] EXTRACELLULAR. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Comment TWO VARIANTS ARE DERIVED FROM TWO DIFFERENT SUBCLONES. Cross-ref NCBI Seq ID: 183064 Cross-ref GenBank Accession: M17783 Cross-ref HSSP P01008 Cross-ref MIM 177010 Cross-ref PROSITE PS00284 Created Apr 1, 1988 Updated Oct 1, 1996 Citation REF [1] J. Sommer, S.M. Gloor, G.F. Rovelli, J. Hofsteenge, H. Nick, R. Meier & D. Monard (1987). cDNA sequence coding for a rat glia-derived nexin and its homology to members of the serpin superfamily. Biochemistry 26, 6407-6410. MEDLINE identifier: 88107544 Citation REF [2] S. Gloor, K. Odink, J. Guenther, H. Nick & D. Monard (1986). A glia-derived neurite promoting factor with protease inhibitory activity belongs to the protease nexins. Cell 47, 687-693. MEDLINE identifier: 87051740 Citation REF [3] M. MCGROGAN, J. KENNEDY, M.P. LI, C. HSU, R.W. SCOTT, C.C. SIMONSEN & J.B. BAKER (1988)BIO/TECHNOLOGY 6, 172-177. Citation REF [4] R.W. Scott, B.L. Bergman, A. Bajpai, R.T. Hersh, H. Rodriguez, B.N. Jones, C. Barreda, S. Watts & J.B. Baker (1985). Protease nexin. Properties and a modified purification procedure. J. Biol. Chem. 260, 7029-7034. MEDLINE identifier: 85207723 Signal 121110: 1..19 Mature chain GLIA DERIVED NEXIN. 121110: 20..398 (experimentally determined) glycosylation 121110: 118 site glycosylation 121110: 159 site active site REACTIVE BOND. 121110: 365..366 Variant TG -> R. 121110: 329..330 (experimentally determined) Conflict S -> E (IN REF. 2). 121110: 261 (experimentally determined) Gene Locus: PI7 121110: 1..398 Sequence 398 aa 1 mnwhlplfll asvtlpsics hfnplsleel gsntgiqvfn qivksrphdn 51 ivisphgias vlgmlqlgad grtkkqlamv mrygvngvgk ilkkinkaiv 101 skknkdivtv anavfvknas eievpfvtrn kdvfqcevrn vnfedpasac 151 dsinawvkne trdmidnlls pdlidgvltr lvlvnavyfk glwksrfqpe 201 ntkkrtfvaa dgksyqvpml aqlsvfrcgs tsapndlwyn fielpyhges 251 ismlialpte sstplsaiip histktidsw msimvpkrvq vilpkftava 301 qtdlkeplkv lgitdmfdss kanfakittg senlhvshil qkakievsed 351 gtkasaatta iliarssppw fivdrpflff irhnptgavl fmgqinkp
113880 --------------------------------------------------- Definition ANGIOTENSINOGEN PRECURSOR. Protein Name: ANGIOTENSINOGEN PRECURSOR 113880: 1..485 SWISS-PROT Name: ANGT_HUMAN, Accession: P01019 NCBI Seq ID: 113880 Comment [FUNCTION] IN RESPONSE TO LOWERED BLOOD PRESSURE, THE ENZYME RENIN CLEAVES ANGIOTENSIN I, FROM ANGIOTENSINOGEN. ACE (ANGIOTENSIN CONVERTING ENZYME) THEN REMOVES A DIPEPTIDE TO YIELD THE PHYSIOLOGICALLY ACTIVE PEPTIDE ANGIOTENSIN II, THE MOST POTENT PRESSOR SUBSTANCE KNOWN, WHICH HELPS REGULATE VOLUME AND MINERAL BALANCE OF BODY FLUIDS. Comment [TISSUE SPECIFICITY] MADE IN THE LIVER & SECRETED IN THE PLASMA. Comment [SIMILARITY] WITH SERPIN SERINE PROTEASE INHIBITORS. Comment [CAUTION] IT IS UNCERTAIN WHETHER MET-1 OR MET-10 IS THE INITIATOR. Comment [DISEASE] AGT SEEMS TO BE ASSOCIATED WITH A PREDISPOSITION TO ESSENTIAL HYPERTENSION AS WELL AS PREGNANCY-INDUCED HYPERTENSION (PIH) (PREECLAMPSIA). Cross-ref NCBI Seq ID: 178640 Cross-ref NCBI Seq ID: 532198 Cross-ref NCBI Seq ID: 1197497 Cross-ref NCBI Seq ID: 553181 Cross-ref GenBank Accession: K02215 Cross-ref GenBank Accession: M24689 Cross-ref EMBL Accession: X15324 Cross-ref GenBank Accession: M69110 Cross-ref SWISS-2DPAGE P01019 Cross-ref MIM 106150 Cross-ref PROSITE PS00284 Created Jul 21, 1986 Updated Oct 1, 1996 Citation REF [1] I. Gaillard, E. Clauser & P. Corvol (1989). Structure of human angiotensinogen gene. DNA 8, 87-99. MEDLINE identifier: 89170129 Citation REF [2] R. Kageyama, H. Ohkubo & S. Nakanishi (1984). Primary structure of human preangiotensinogen deduced from the cloned cDNA sequence. Biochemistry 23, 3603-3609. MEDLINE identifier: 85000455 Citation REF [3] A. Fukamizu, S. Takahashi, M.S. Seo, M. Tada, K. Tanimoto, S. Uehara & K. Murakami (1990). Structure and expression of the human angiotensinogen gene. Identification of a unique and highly active promoter. J. Biol. Chem. 265, 7576-7582. MEDLINE identifier: 90237063 Citation REF [4] S.P. Kunapuli & A. Kumar (1987). Molecular cloning of human angiotensinogen cDNA and evidence for the presence of its mRNA in rat heart. Circ. Res. 60, 786-790. MEDLINE identifier: 87244745 Citation REF [5] K. Arakawa, A. Minohara, J. Yamada & M. Nakamura (1968). Enzymatic degradation and electrophoresis of human angiotensin I. Biochim. Biophys. Acta 168, 106-112. MEDLINE identifier: 69014170 Citation REF [6] X. JEUNEMAITRE, F. SOUBRIER, Y.V. KOTELEVTSEV, R.P. LIFTON, C.S. WILLIAMS, A. CHARRU, S.C. HUNT, P.N. HOPKINS, R.R. WILLIAMS, J.-M. LALOUEL & P. CORVOL (1992). Molecular basis of human hypertension: role of angiotensinogen. Cell 71, 169- 180. MEDLINE identifier: 93008239 Citation REF [7] K. WARD, A. HATA, X. JEUNEMAITRE, C. HELIN, L. NELSON, C. NAMIKAWA, P.F. FARRINGTON, M. OGASAWARA, K. SUZUMORI, S. TOMODA, S. BERREBI, M. SASAKI, P. CORVOL, R.P. LIFTON & J.-M. LALOUEL (1993). A molecular variant of angiotensinogen associated with preeclampsia. Nature Genet. 4, 59-61. MEDLINE identifier: 93291876 Citation REF [8] J.E. Hixson & P.K. Powers (1995). Detection and characterization of new mutations in the human angiotensinogen gene (AGT). Hum. Genet. 96, 110-112. MEDLINE identifier: 95331754 Signal (experimentally determined) 113880: 1..33 Mature chain ANGIOTENSINOGEN. 113880: 34..485 (experimentally determined) Processed ANGIOTENSIN I. 113880: 34..43 active peptide (experimentally determined) Processed ANGIOTENSIN II. 113880: 34..41 active peptide (experimentally determined) glycosylation 113880: 47 site glycosylation 113880: 170 site glycosylation 113880: 304 site glycosylation 113880: 328 site Variant T -> M. 113880: 207 (experimentally determined) Variant T -> I (IN HYPERTENSION). 113880: 242 (experimentally determined) Variant L -> R (IN HYPERTENSION). 113880: 244 (experimentally determined) Variant M -> T (IN HYPERTENSION). 113880: 268 (experimentally determined) Variant Y -> C (IN HYPERTENSION). 113880: 281 (experimentally determined) Conflict Q -> E (IN REF. 1). 113880: 333 (experimentally determined) Gene Locus: AGT 113880: 1..485 Sequence 485 aa 1 mrkrapqsem apagvslrat ilcllawagl aagdrvyihp fhlvihnest 51 ceqlakanag kpkdptfipa piqaktspvd ekalqdqlvl vaakldtedk 101 lraamvgmla nflgfriygm hselwgvvhg atvlsptavf gtlaslylga 151 ldhtadrlqa ilgvpwkdkn ctsrldahkv lsalqavqgl lvaqgradsq 201 aqlllstvvg vftapglhlk qpfvqglaly tpvvlprsld fteldvaaek 251 idrfmqavtg wktgcslmga svdstlafnt yvhfqgkmkg fsllaepqef 301 wvdnstsvsv pmlsgmgtfq hwsdiqdnfs vtqvpftesa cllliqphya 351 sdldkveglt fqqnslnwmk klsprtihlt mpqlvlqgsy dlqdllaqae 401 lpailhteln lqklsndrir vgevlnsiff eleaderept estqqlnkpe 451 vlevtlnrpf lfavydqsat alhflgrvan plsta
106228 --------------------------------------------------- Definition heparin cofactor II precursor - human Protein Names: heparin cofactor II 106228: [ Whole ] precursor; antithrombin; heparin cofactor A; leuserpin 2 PIR Name: A37924 NCBI Seq ID: 106228 Created Jul 12, 1991 Updated Sep 13, 1996 Citation R. Herzog, S. Lutz, N. Blin, J.C. Marasa, M.A. Blinder & D.M. Tollefsen (1991). Complete nucleotide sequence of the gene for human heparin cofactor II and mapping to chromosomal band 22q11. Biochemistry 30, 1350-1357. MEDLINE identifier: 91120782 Citation M.A. Blinder, J.C. Marasa, C.H. Reynolds, L.L. Deaven & D.M. Tollefsen (1988). Heparin cofactor II: cDNA sequence, chromosome localization, restriction fragment length polymorphism, and expression in Escherichia coli. Biochemistry 27, 752-759. MEDLINE identifier: 88163663 Citation R.C. Inhorn & D.M. Tollefsen (1986). Isolation and characterization of a partial cDNA clone for heparin cofactor II1. Biochem. Biophys. Res. Commun. 137, 431-436. MEDLINE identifier: 86242236 Citation H. Ragg (1986). A new member of the plasma protease inhibitor gene family. Nucleic Acids Res. 14, 1073-1088. MEDLINE identifier: 86120356 Citation H. Ragg & G. Preibisch (1988). Structure and expression of the gene coding for the human serpin hLS2. J. Biol. Chem. 263, 12129-12134. MEDLINE identifier: 88298901 Citation F.C. Church, C.W. Pratt & M. Hoffman (1991). Leukocyte chemoattractant peptides from the serpin heparin cofactor II. J. Biol. Chem. 266, 704-709. MEDLINE identifier: 91093260 Citation F.C. Church, C.M. Noyes & M.J. Griffith (1985). Inhibition of chymotrypsin by heparin cofactor II. Proc. Natl. Acad. Sci. U.S.A. 82, 6431-6434. MEDLINE identifier: 86016716 Citation M.J. Griffith, C.M. Noyes, J.A. Tyndall & F.C. Church (1985). Structural evidence for leucine at the reactive site of heparin cofactor II. Biochemistry 24, 6777-6782. MEDLINE identifier: 86077723 domain signal sequence 106228: 1..19 domain heparin cofactor II 106228: 20..499 region chemotactic 106228: 68..79 region heparin binding 106228: 182..214 binding site carbohydrate (Asn) (covalent) 106228: 49 binding site carbohydrate (Asn) (covalent) 106228: 188 binding site carbohydrate (Asn) (covalent) 106228: 387 binding site sulfate (Tyr) (covalent) 106228: 79 binding site sulfate (Tyr) (covalent) 106228: 92 inhibit site Leu (thrombin, chymotrypsin) 106228: 463 Sequence 499 aa 1 mkhslnalli fliitsawgg skgpldqlek ggetaqsadp qweqlnnknl 51 smpllpadfh kentvtndwi pegeedddyl dlekifsedd dyidivdsls 101 vsptdsdvsa gnilqlfhgk sriqrlniln akfafnlyrv lkdqvntfdn 151 ifiapvgist amgmislglk getheqvhsi lhfkdfvnas skyeittihn 201 lfrklthrlf rrnfgytlrs vndlyiqkqf pilldfktkv reyyfaeaqi 251 adfsdpafis ktnnhimklt kglikdalen idpatqmmil nciyfkgswv 301 nkfpvemthn hnfrlnerev vkvsmmqtkg nflaandqel dcdilqleyv 351 ggismlivvp hkmsgmktle aqltprvver wqksmtnrtr evllpkfkle 401 knynlveslk lmgirmlfdk ngnmagisdq riaidlfkhq gtitvneegt 451 qattvttvgf mplstqvrft vdrpflfliy ehrtscllfm grvanpsrs
1537066 --------------------------------------------------- Definition putative serpin-like protein Protein Description: putative serpin-like 1537066: [ Whole ] protein. NCBI Seq ID: 1537066 Citation F. Petit, S. Bertagnoli, J. Gelfi, F. Fassy, C. Boucraut- Baralon & A. Milon (1996). Characterization of a myxoma virus- encoded serpin-like protein with activity against interleukin- 1 beta-converting enzyme. J. Virol. 70, 5860-5866. MEDLINE identifier: 96323099 Citation Data Submission: F. Petit (1996). Updated Sep 12, 1996 Coding region 1537065: 91..1092 Sequence 333 aa 1 melfkhflqs tasdvfvspv sisavlavll egakgrtaaq lrlaleprys 51 hldkvtvasr vygdwrldik ptfmqvvrdr felvnfnhsp ekikddinrw 101 vaartnnkil navnsispdt kllivadiyf evawrnqfvp ditiegefwv 151 tkdvsktvrm mtlsddfrfv dvrnegikmi elpyeygysm lviipddleq 201 verhlslmkv iswlkmstlr yvhlsfpkfk metsytlnea latsgvtdif 251 ahpnfedmtd dknvavsdif hkayievtef gttaasctyg cvtdfggtmd 301 pvvlkvnkpf ifiikhddtf sllflgrvts pny
2145124 --------------------------------------------------- Protein Name: H14-B 2145124: [ Whole ] NCBI Seq ID: 2145124 Updated Sep 10, 1996 Citation REF [1] C. Upton & R.M.L. Buller. Ectromelia virus HindIII fragment (H14): equivalent to vaccinia virus k HindIII fragment. Unpublished Citation REF [2] Data Submission: C. Upton & R.M.L. Buller (1996). Coding region Comments: HindIII fragment H14; 2145123: c1397..276 similar to vaccinia virus K2L; serpin. Sequence 373 aa 1 miallilsla ctasayrlqg ftnagilayk niqdgneddn ivfspfgysf 51 smfmsllpas gntrvellkt mdlrkrdlgp aftelisgla tlktskytyt 101 dltyqsfvdn tvcikpsyyq qyhrfglyrl nfrrdpvdki nsiverrsgm 151 snvvdstmld dntlwtiint iyfkgtwqcp fdiakthnas ftnkygtktv 201 pmmnvvtklq gntitvddee ydmarlpykd tnismylaig dnmthftdsi 251 taakldywss qlgnkmynlk lprfsienkr diksiaemia pgmfnpdkas 301 fkhmtrdply iykmfqnaki dvdeqgtvae astimvstar ssptelefnt 351 pfvfiirhdi tgfilfmgkv esp
2144573 --------------------------------------------------- Definition alpha-2-antiplasmin precursor - human Protein Names: alpha-2-antiplasmin 2144573: [ Whole ] precursor; alpha-2-PI; alpha-2- plasmin inhibitor precursor PIR Name: ITHUA2 NCBI Seq ID: 2144573 Comment After synthesis in the liver, 30-50% of alpha-2-antiplasmin circulates in plasma with the propeptide uncleaved. The presence of the propeptide does not prevent plasmin inhibition, but does inhibit activated coagulation factor XIII from forming an isopeptide cross-link with fibrin. Created Jul 31, 1989 Updated Sep 6, 1996 Citation S. Hirosawa, Y. Nakamura, O. Miura, Y. Sumi & N. Aoki (1988). Organization of the human alpha 2-plasmin inhibitor gene. Proc. Natl. Acad. Sci. U.S.A. 85, 6836-6840. MEDLINE identifier: 88320531 Citation S. Hirosawa, Y. Nakamura, O. Miura, Y. Sumi & N. Aoki (1989)Proc. Natl. Acad. Sci. U.S.A. 86, 1612-1613. Citation M. Tone, R. Kikuno, A. Kume-Iwaki & T. Hashimoto-Gotoh (1987). Structure of human alpha 2-plasmin inhibitor deduced from the cDNA sequence. J. Biochem. 102, 1033-1041. MEDLINE identifier: 88139254 Citation W.E. Holmes, L. Nelles, H.R. Lijnen & D. Collen (1987). Primary structure of human alpha 2-antiplasmin, a serine protease inhibitor (serpin). J. Biol. Chem. 262, 1659-1664. MEDLINE identifier: 87109313 Citation Y. Sumi, Y. Nakamura, N. Aoki, M. Sakai & M. Muramatsu (1986). Structure of the carboxyl-terminal half of human alpha 2- plasmin inhibitor deduced from that of cDNA. J. Biochem. 100, 1399-1402. MEDLINE identifier: 87137400 Citation T. Koyama, Y. Koike, S. Toyota, F. Miyagi, N. Suzuki & N. Aoki (1994). Different NH2-terminal form with 12 additional residues of alpha 2-plasmin inhibitor from human plasma and culture media of Hep G2 cells. Biochem. Biophys. Res. Commun. 200, 417-422. MEDLINE identifier: 94220119 Citation H.R. Lijnen, W.E. Holmes, B. van Hoef, B. Wiman, H. Rodriguez & D. Collen (1987). Amino-acid sequence of human alpha 2- antiplasmin. Eur. J. Biochem. 166, 565-574. MEDLINE identifier: 87275946 Citation K. Bangert, A.H. Johnsen, U. Christensen & S. Thorsen (1993). Different N-terminal forms of alpha 2-plasmin inhibitor in human plasma. Biochem. J. 291, 623-625. MEDLINE identifier: 93249387 Citation J.J. Enghild, Z. Valnickova, I.B. Thogersen, S.V. Pizzo & G. Salvesen (1993). An examination of the inhibitory mechanism of serpins by analysing the interaction of trypsin and chymotrypsin with alpha 2-antiplasmin. Biochem. J. 291, 933- 938. MEDLINE identifier: 93256910 Citation Y. Sumi, Y. Ichikawa, Y. Nakamura, O. Miura & N. Aoki (1989). Expression and characterization of pro alpha 2-plasmin inhibitor. J. Biochem. 106, 703-707. MEDLINE identifier: 90110073 Citation S. Kimura & N. Aoki (1986). Cross-linking site in fibrinogen for alpha 2-plasmin inhibitor. J. Biol. Chem. 261, 15591- 15595. MEDLINE identifier: 87057190 domain signal sequence 2144573: 1..27 domain propeptide 2144573: 28..39 (experimentally determined) product alpha-2-antiplasmin 2144573: 40..491 (experimentally determined) region amphipathic helix 2144573: 454..465 region cell attachment (R-G-D) motif 2144573: 465..467 cleavage site Pro-Asn (unknown plasma proteinase)2144573: 39..40 (experimentally determined) xlink bond isopeptide (Gln) (interchain to 2144573: 41 bond fibrin alpha chain 322-Lys) (experimentally determined) disulfide bond (experimentally determined) 2144573: 70 bond 152 disulfide bond (experimentally determined) 2144573: 103 bond 143 binding site carbohydrate (Asn) (covalent) 2144573: 126 (experimentally determined) binding site carbohydrate (Asn) (covalent) 2144573: 295 (experimentally determined) binding site carbohydrate (Asn) (covalent) 2144573: 309 (experimentally determined) binding site carbohydrate (Asn) (covalent) 2144573: 316 (experimentally determined) cleavage site Met-Ser (chymotrypsin) (partial) 2144573: 401..402 (experimentally determined) cleavage site Arg-Met (plasmin, trypsin) 2144573: 403..404 (experimentally determined) inhibit site Arg (plasmin) 2144573: 403 cleavage site Met-Ser (chymotrypsin) (partial) 2144573: 404..405 (experimentally determined) inhibit site Met (chymotrypsin) 2144573: 404 binding site carbohydrate (Asn) (covalent) 2144573: 437 Sequence 491 aa 1 mallwgllvl swsclqgpcs vfspvsamep lgrqltsgpn qeqvspltll 51 klgnqepggq talksppgvc srdptpeqth rlarammaft adlfslvaqt 101 stcpnlilsp lsvalalshl algaqnhtlq rlqqvlhags gpclphllsr 151 lcqdlgpgaf rlaarmylqk gfpikedfle qseqlfgakp vsltgkqedd 201 laninqwvke ategkiqefl sglpedtvll llnaihfqgf wrnkfdpslt 251 qrdsfhldeq ftvpvemmqa rtyplrwfll eqpeiqvahf pfknnmsfvv 301 lvpthfewnv sqvlanlswd tlhpplvwer ptkvrlpkly lkhqmdlvat 351 lsqlglqelf qapdlrgise qslvvsgvqh qstlelsevg veaaaatsia 401 msrmslssfs vnrpflffif edttglplfv gsvrnpnpsa prelkeqqds 451 pgnkdflqsl kgfprgdklf gpdlklvppm eedypqfgsp k
2135604 --------------------------------------------------- Definition maspin - human Protein Names: maspin; protease 2135604: [ Whole ] inhibitor 5 PIR Name: A36898 NCBI Seq ID: 2135604 Comment The high likelihood that this serine proteinase inhibitor of normal mammary epithelial cells is lost from mammary carcinoma cells suggests a role as a tumor suppressor. Created Feb 23, 1996 Updated Sep 6, 1996 Citation Z. Zou, A. Anisowicz, M.J. Hendrix, A. Thor, M. Neveu, S. Sheng, K. Rafidi, E. Seftor & R. Sager (1994). Maspin, a serpin with tumor-suppressing activity in human mammary epithelial cells. Science 263, 526-529. MEDLINE identifier: 94120413 Sequence 375 aa 1 mdalqlansa favdlfkqlc ekeplgnvlf spiclstsls laqvgakgdt 51 aneigqvlhf envkdipfgf qtvtsdvnkl ssfyslklik rlyvdkslnl 101 stefisstkr pyakeletvd fkdkleetkg qinnsikdlt dghfenilad 151 nsvndqtkil vvnaayfvgk wmkkfpeset kecpfrlnkt dtkpvqmmnm 201 eatfcmgnid sinckiielp fqnkhlsmfi llpkdvedes tglekiekql 251 nseslsqwtn pstmanakvk lsipkfkvek midpkaclen lglkhifsed 301 tsdfsgmset kgvalsnvih kvcleitedg gdsievpgar ilqhkdelna 351 dhpfiyiirh nktrniiffg kfcsp
2134832 --------------------------------------------------- Definition bomapin - human Protein Names: bomapin; protease 2134832: [ Whole ] inhibitor 10 PIR Name: I39184 NCBI Seq ID: 2134832 Created Mar 1, 1996 Updated Sep 6, 1996 Citation M. Riewald & R.R. Schleef (1995). Molecular cloning of bomapin (protease inhibitor 10), a novel human serpin that is expressed specifically in the bone marrow. J. Biol. Chem. 270, 26754-26757. MEDLINE identifier: 96070759 Sequence 397 aa 1 mdslatsinq falelskkla esaqgkniff sswsistslt ivylgakgtt 51 aaqmaqvlqf nrdqgvkcdp esekkrkmef nlsnseeihs dfqtliseil 101 kpnddyllkt anaiygekty afhnkyledm ktyfgaepqp vnfveasdqi 151 rkdinswver qtegkiqnll pddsvdsttr milvnalyfk giwehqflvq 201 nttekpfrin ettskpvqmm fmkkklhifh iekpkavglq lyyksrdlsl 251 lillpeding leqlekaity eklnewtsad mmelyevqlh lpkfkledsy 301 dlkstlssmg msdafsqska dfsgmssarn lflsnvfhka fveineqgte 351 aaagsgseid irirvpsief nanhpflffi rhnktntilf ygrlcsp
1098627 --------------------------------------------------- Definition 47 kDa heat shock protein Protein Name: 47 kDa heat shock protein 1098627: [ Whole ] NCBI Seq ID: 1098627 Citation Data Submission: D.S. Pearson, W.M. Kulyk & P.H. Krone (1995). Updated Aug 15, 1996 Coding region Comments: member of serpin 1098626: 178..1392 superfamily. Sequence 404 aa 1 mwvsslialc llavavsged kklsthatsm adtsanlafn lyhnvlkkgl 51 enifispvvv asslgmvamg sksstasqvk silkadalkd ehlhtglsel 101 ltevsdpqtr nvtwkisnrl ygpssvsfae dfvknskkhy nyehskinfr 151 dkrsainsin ewaakttdgk lpeitkdvkn tdgamivnam ffkphwdekf 201 hhkmvdnrgf lvtrshtvsv pmmhrtgiyg fyedtenrfl ivsialahkk 251 ssmifimpyh vepldrlenl ltrqqldtwi skleeravai slpkvsmeas 301 hdlqkhlgel glteavdksk adlsnisgkk dlylsnvfha sslewdtegn 351 pfdpsifgse kmrnpklfya dhpfiflvkd nktnsilfig rlvrpkgdkm 401 rdel
110889 --------------------------------------------------- Definition serpin Spi2 (clone 2B1) - mouse (fragment) Protein Names: serpin Spi2 (clone 2B1); 110889: [ Whole ] alpha-1-antichymotrypsin homolog; serine proteinase inhibitor 2 PIR Name: S15636 NCBI Seq ID: 110889 Created Nov 21, 1993 Updated Jul 19, 1996 Citation J.D. Inglis & R.E. Hill (1991). The murine Spi-2 proteinase inhibitor locus: a multigene family with a hypervariable reactive site domain. EMBO J. 10, 255-261. MEDLINE identifier: 91122031 Sequence 66 aa 1 vvhkavldma etgteadaat rfkiaplsak fdivnvnfnr pfniivlsld 51 tqvpfvlvkv lnpkgd
110888 --------------------------------------------------- Definition serpin Spi2 (clone 2B2) - mouse (fragment) Protein Name: serpin Spi2 (clone 2B2) 110888: [ Whole ] PIR Name: S15635 NCBI Seq ID: 110888 Created Nov 21, 1993 Updated Jul 19, 1996 Citation J.D. Inglis & R.E. Hill (1991). The murine Spi-2 proteinase inhibitor locus: a multigene family with a hypervariable reactive site domain. EMBO J. 10, 255-261. MEDLINE identifier: 91122031 Sequence 64 aa 1 vvhkavldva etgteaaaat gvkvnlrcgk iysmtiyfnr pflmiisdin 51 thiavfmakv tnpk
110886 --------------------------------------------------- Definition serpin Spi2 (clone 6C28) - mouse (fragment) Protein Name: serpin Spi2 (clone 6C28) 110886: [ Whole ] PIR Name: S15633 NCBI Seq ID: 110886 Created Nov 21, 1993 Updated Jul 19, 1996 Citation J.D. Inglis & R.E. Hill (1991). The murine Spi-2 proteinase inhibitor locus: a multigene family with a hypervariable reactive site domain. EMBO J. 10, 255-261. MEDLINE identifier: 91122031 Sequence 64 aa 1 vvhkavldva etgteaaaat gvklilccek iysmtiyfnr pflmiisdin 51 thialfmakv tnpk
110884 --------------------------------------------------- Definition serpin Spi2 (clone 1A1) - mouse (fragment) Protein Name: serpin Spi2 (clone 1A1) 110884: [ Whole ] PIR Name: S15631 NCBI Seq ID: 110884 Created Nov 21, 1993 Updated Jul 19, 1996 Citation J.D. Inglis & R.E. Hill (1991). The murine Spi-2 proteinase inhibitor locus: a multigene family with a hypervariable reactive site domain. EMBO J. 10, 255-261. MEDLINE identifier: 91122031 Sequence 61 aa 1 mvhkavldva etgtegvaat gvnfrilsrr tslwfnrtfl mvishtgfqt 51 tlfiakithp k
110882 --------------------------------------------------- Definition serpin Spi2 (clone 2A1) - mouse (fragment) Protein Name: serpin Spi2 (clone 2A1) 110882: [ Whole ] PIR Name: S15629 NCBI Seq ID: 110882 Created Nov 21, 1993 Updated Jul 19, 1996 Citation J.D. Inglis & R.E. Hill (1991). The murine Spi-2 proteinase inhibitor locus: a multigene family with a hypervariable reactive site domain. EMBO J. 10, 255-261. MEDLINE identifier: 91122031 Sequence 66 aa 1 vvhkavldva etgteaaaat gyqnlqccqg viysmkiyfd rpflmiisdt 51 nthialfmak vpnpre
92335 --------------------------------------------------- Definition kallikrein-binding protein precursor - rat Protein Names: kallikrein-binding protein 92335: [ Whole ] precursor; contrapsin-like protease inhibitor; growth hormone-induced proteinase inhibitor; serine proteinase inhibitor PIR Name: B29131 NCBI Seq ID: 92335 Created Mar 31, 1989 Updated Jun 15, 1996 Citation J.B. Yoon, H.C. Towle & S. Seelig (1987). Growth hormone induces two mRNA species of the serine protease inhibitor gene family in rat liver. J. Biol. Chem. 262, 4284-4289. MEDLINE identifier: 87166046 Citation A. Le Cam, G. Pages, P. Auberger, G. Le Cam, P. Leopold, R. Benarous & N. Glaichenhaus (1987). Study of a growth hormone- regulated protein secreted by rat hepatocytes: cDNA cloning, anti-protease activity and regulation of its synthesis by various hormones. EMBO J. 6, 1225-1232. MEDLINE identifier: 87275813 Citation G. Pages, J.F. Rouayrenc, G. Le Cam, M. Mariller & A. Le Cam (1990). Molecular characterization of three rat liver serine- protease inhibitors affected by inflammation and hypophysectomy. Protein and mRNA analysis and cDNA cloning. Eur. J. Biochem. 190, 385-391. MEDLINE identifier: 90306038 Citation Data Submission: A. le Cam (1989). Citation Data Submission: A. le Cam (1989). Citation G. Pages, J.F. Rouayrenc, V. Rossi, G. Le Cam, M. Mariller, J. Szpirer, C. Szpirer, G. Levan & A. Le Cam (1990). Primary structure and assignment to chromosome 6 of three related rat genes encoding liver serine protease inhibitors. Gene 94, 273- 282. MEDLINE identifier: 91078650 Citation K.X. Chai, J.X. Ma, S.R. Murray, J. Chao & L. Chao (1991). Molecular cloning and analysis of the rat kallikrein-binding protein gene. J. Biol. Chem. 266, 16029-16036. MEDLINE identifier: 91340751 Citation J. Chao, K.X. Chai, L.M. Chen, W. Xiong, S. Chao, C. Woodley- Miller, L.X. Wang, H.S. Lu & L. Chao (1990). Tissue kallikrein-binding protein is a serpin. I. Purification, characterization, and distribution in normotensive and spontaneously hypertensive rats. J. Biol. Chem. 265, 16394- 16401. MEDLINE identifier: 90375506 Citation K. Ohkubo, S. Ogata, Y. Misumi, N. Takami & Y. Ikehara (1991). Molecular cloning and characterization of rat contrapsin-like protease inhibitor and related proteins. J. Biochem. 109, 243- 250. MEDLINE identifier: 91324305 Sequence 416 aa 1 mafiaalgll magicpavlc dgilgrdtlp hedqgkgrql hsltlasint 51 dftlslykkl alrnpdknvv fsplsisaal ailslgakds tmeeileglk 101 fnlteiteee ihqgfghllq rlsqpedqae intgsalfid keqpilsefq 151 ektralyqae afvadfkqcn eakkfindyv snqtqgkiae lfselderts 201 mvlvnyllfk gkwkvpfnpn dtfesefyld ekrsvkvpmm kikdlttpyi 251 rdeelscsvl elkytgnasa lfilpdqgkm qqvesslqpe tlkkwkdslr 301 priiselrmp kfsistdynl eevlpelgir kifsqqadls ritgtknlhv 351 sqvvhkavld vdetgtegaa atavtaalks lpqtipllnf nrpfmlvitd 401 nngqsvffmg kvtnpm
19068 --------------------------------------------------- Definition protein Z Protein Name: protein Z 19068: [ Whole ] NCBI Seq ID: 19068 Citation REF [3] A. Brandt, I. Svendsen & J. Hejgaard (1990). A plant serpin gene. Structure, organization and expression of the gene encoding barley protein Z4. Eur. J. Biochem. 194, 499-505. MEDLINE identifier: 91099324 Updated May 8, 1996 Citation REF [1] Data Submission: A. Brandt, J. Hejgaard & I. Svendsen (1990). Coding region 19067: 1079..1495 19067: 1830..2612 Sequence 399 aa 1 mattlatdvr lsiahqtrfa lrlrsaissn peraagnvaf splslhvals 51 litagaaatr dqlvailgdg gagdakelna laeqvvqfvl anesstggpr 101 iafangifvd aslslkpsfe elavcqykak tqsvdfqhkt leavgqvnsw 151 veqvttglik qilppgsvdn ttklilgnal yfkgawdqkf desntkcdsf 201 hlldgssiqt qfmsstkkqy isssdnlkvl klpyakghdk rqfsmyillp 251 gaqdglwsla krlstepefi enhipkqtve vgrfqlpkfk isyqfeassl 301 lralglqlpf seeadlsemv dssqgleish vfhksfvevn eegteagaat 351 vamgvamsmp lkvdlvdfva nhpflflire diagvvvfvg hvtnplisa
871551 --------------------------------------------------- Definition serpin Protein Name: serpin 871551: [ Whole ] Activities: chymotrypsin inhibitor NCBI Seq ID: 871551 Updated May 7, 1996 Citation REF [1] S.K. Rasmussen, S.W. Dahl, A. Norgard & J. Hejgaard (1996). A recombinant wheat serpin with inhibitory activity. Plant Mol. Biol. 30, 673-677. MEDLINE identifier: 96189280 Citation REF [2] I. Rosenkrands, J. Hejgaard, S.K. Rasmussen & S.E. Bjorn (1994). Serpins from wheat grain. FEBS Lett. 343, 75-80. MEDLINE identifier: 94215711 Citation REF [3] Data Submission: S.K. Rasmussen (1995). Coding region 871550: 54..1250 (experimentally determined) Sequence 398 aa 1 mattlatdvr lsiahqtrfa lrlastissn pksaasnaaf spvslysals 51 llaagagsat rdqlvatlgt gkveglhala eqvvqfvlad asstggsacr 101 fangvfvdas lllkpsfqei avckykaetq svdfqtkaae vttqvnswve 151 kvtsgrikdi lppgsidntt klvlanalyf kgawteqfds ygtkndyfyl 201 ldgssvqtpf mssmddqyll ssdglkvlkl pykqggdnrq ffmyillpea 251 pgglsslaek lsaepdfler hiprqrvalr qfklpkfkis fgieasdllk 301 clglqlpfgd eadfsemvds lmpqglrvss vfhqafvevn eqgteaaast 351 aikmvlqqar ppsvmdfiad hpflflvred isgvvlfmgh vvnpllss
421989 --------------------------------------------------- Definition serpin - barley Protein Name: serpin 421989: [ Whole ] PIR Name: S29819 NCBI Seq ID: 421989 Created Dec 2, 1993 Updated May 3, 1996 Citation S.K. Rasmussen (1993). A gene coding for a new plant serpin. Biochim. Biophys. Acta 1172, 151-154. MEDLINE identifier: 93176798 Sequence 398 aa 1 mattdirlsi ahqtrfavrl asaisspsha kgssgnaafs plslhvalsl 51 vaagaaatrd qlaatlgaae kgdaeglhal aeqvvqvvla dasgaggprs 101 fanvfvdssl klkpsfkdlv vgkykgetqs vdfqtkapev agqvnswvek 151 ittglikeil pagsvdsttr lvlgnalyfk gswtekfdas ktkdekfhll 201 dgssvqtpfm sstkkqyiss ydslkvlklp yqqggdkrqf smyillpeaq 251 dglwnlankl stepefmekh mpmqkvpvgq fklpkfkisf gfeasdmlkg 301 lglqlpfsse adlsemvdsp aarslyvssv fhksfvevne egteaaarta 351 rvvtlrslpv epvkvdfvad hpflflired ltgvvlfvgh vfnplvsa
164241 --------------------------------------------------- Definition serpin Protein Name: serpin 164241: [ Whole ] Activities: elastase inhibitor NCBI Seq ID: 164241 Updated Apr 25, 1996 Citation T. Kordula, A. Dubin, H. Schooltink, A. Koj, P.C. Heinrich & S. Rose-John (1993). Molecular cloning and expression of an intracellular serpin: an elastase inhibitor from horse leucocytes. Biochem. J. 293, 187-193. MEDLINE identifier: 93319507 Citation Data Submission: T. Kordula (1992). Coding region Comments: intercellular. 164240: 41..1180 Sequence 379 aa 1 meqlstanth favdlfraln esdptgnifi splsissala miflgtrgnt 51 aaqvskalyf dtvedihsrf qslnadinkp gapyilklan rlygektynf 101 ladflastqk mygaelasvd fqqapedark einewvkgqt egkipellvk 151 gmvdnmtklv lvnaiyfkgn wqekfmkeat rdapfrlnkk dtktvkmmyq 201 kkkfpynyie dlkcrvlelp yqgkelsmii llpddiedes tglekiekql 251 tleklrewtk penlylaevn vhlprfklee sydltshlar lgvqdlfnrg 301 kadlsgmsga rdlfvskiih ksfvdlneeg teaaaatagt imlamlmpee 351 nfnadhpfif firhnpsani lflgrfssp
625491 --------------------------------------------------- Definition antithrombin III - bovine Protein Name: antithrombin III 625491: [ Whole ] PIR Name: A61435 NCBI Seq ID: 625491 Comment This serpin inhibits thrombin and other clotting factors in the presence of heparin and is the principal inhibitor of the coagulation cascade. Created Oct 7, 1994 Updated Apr 12, 1996 Citation H. Mejdoub, M. Le Ret, Y. Boulanger, M. Maman, J. Choay & J. Reinbolt (1991). The complete amino acid sequence of bovine antithrombin (ATIII). J. Protein Chem. 10, 205-212. MEDLINE identifier: 92029517 disulfide bond 625491: 9 bond 129 disulfide bond 625491: 22 bond 96 disulfide bond 625491: 248 bond 431 binding site carbohydrate (Asn) (covalent) 625491: 97 (experimentally determined) binding site carbohydrate (Asn) (covalent) 625491: 136 (experimentally determined) binding site carbohydrate (Asn) (covalent) 625491: 156 (experimentally determined) binding site carbohydrate (Asn) (covalent) 625491: 193 (experimentally determined) inhibit site Arg (thrombin) 625491: 394 (experimentally determined) Sequence 433 aa 1 hrspvedvct akprdipvnp mciyrssekk ategqgseqk ipgatnrrvw 51 elskanshfa tafyqhlads knnndnifls plsistafam tklgacnntl 101 tqlmevfkfd tisektsdqi hfffaklncr lyrkanksse lvsanrlfgd 151 ksitfnetyq disevvygak lqpldfkgna eqsrltinqw isnktegrit 201 dvippqaine ftvlvlvnti yfkglwkskf spentrkelf ykadgescsv 251 lmmyqeskfr yrrvaestqv lelpfkgddi tmvlilpkle ktlakveqel 301 tpdmlqewld eltetllvvh mprfriedsf svkeqlqdmg ledlfspeks 351 rlpgivaegr sdlyvsdafh kaflevneeg seaaastvis iagrslnsdr 401 vtfkanrpfl vlirevalnt iifmgrvanp cvd
100558 --------------------------------------------------- Definition 39K seed protein - barley (fragments) Protein Name: 39K seed protein 100558: [ Whole ] PIR Name: A35274 NCBI Seq ID: 100558 Created Oct 5, 1990 Updated Apr 12, 1996 Citation R. Lundgard & B. Svensson (1989). A 39 kD barley seed protein of the serpin superfamily inhibits alpha-chymotrypsin. Carlsberg Res. Commun. 54, 173-180. MEDLINE identifier: 90315014 Sequence 36 aa 1 qfsmyillpe ahdglsrslp irmdfvanhp flired
93218 --------------------------------------------------- Definition serpin - Ectromelia virus Protein Name: serpin 93218: [ Whole ] PIR Name: S24676 NCBI Seq ID: 93218 Created Feb 20, 1995 Updated Apr 12, 1996 Citation Data Submission: T. Senkevich (1992). Sequence 344 aa 1 mstwhvvivv ytnmdifkel ilkyndesvl ispvsilstl silhhgaags 51 taeqlskyie nvnenvsedk ddnnddmdvd ipycatlata nkiygsdsie 101 fhasflqkik ddfqtvnfnn anqtkeline wvktmtngki nslltsplpi 151 ntrmavvsav hfkamwkypf skhltytdkf yisknivtsv dmmvstendl 201 qyvhinelfg gfsiidipye gnssmviilp ddiegiynie knitdenfkk 251 wcgmlstksi dlympkfkve mtepynlvpi lenlgltnif gyyadfskmc 301 netitvenfl httfidvnee yteasavtgv fmttfrwyiv rrst
90404 --------------------------------------------------- Definition contrapsin precursor - mouse Protein Name: contrapsin precursor 90404: [ Whole ] PIR Name: JX0129 NCBI Seq ID: 90404 Comment Contrapsin is a plasma glycoprotein belonging to the serpin superfamily which specifically inactivates serine proteinases of the trypsin type but not of the chymotrypsin type. Created Jun 30, 1992 Updated Apr 12, 1996 Citation Y. Suzuki, K. Yamamoto & H. Sinohara (1990). Molecular cloning and sequence analysis of full-length cDNA coding for mouse contrapsin. J. Biochem. 108, 344-346. MEDLINE identifier: 91115777 Citation R.E. Hill, P.H. Shaw, P.A. Boyd, H. Baumann & N.D. Hastie (1984). Plasma protease inhibitors in mouse and man: divergence within the reactive centre regions. Nature 311, 175-177. MEDLINE identifier: 84295637 Citation K. Ohkubo, S. Ogata, Y. Misumi, N. Takami, H. Sinohara & Y. Ikehara (1991). Cloning, structure and expression of cDNA for mouse contrapsin and a related protein. Biochem. J. 276, 337- 342. MEDLINE identifier: 91264784 Citation Data Submission: K. Yoshida, Y. Suzuki & H. Sinohara (1990). domain signal sequence 90404: 1..21 domain propeptide 90404: 22..29 product contrapsin 90404: 30..418 (experimentally determined) binding site carbohydrate (Asn) (covalent) 90404: 39 binding site carbohydrate (Asn) (covalent) 90404: 105 binding site carbohydrate (Asn) (covalent) 90404: 185 binding site carbohydrate (Asn) (covalent) 90404: 270 Sequence 418 aa 1 mafivamgmi lmagicpavl cfpdgtkemd ivfhehqdng tqddsltlas 51 vntdfafsly kklalknpdt nivfsplsis aalalvslga kgktmeeile 101 glkfnltetp eadihqgfgn llqslsqped qdqinignam fiekdlqila 151 efhektraly qteaftadfq qpteaknlin dyvsnqtqgm ikeliselde 201 rtlmvlvnyi yfkgkwkisf dpqdtfesef yldekrsvkv pmmkmklltt 251 rhfrdeelsc svlelkytgn asallilpdq grmqqveasl qpetlrkwrk 301 tlfpsqieel nlpkfsiasn yrleedvlpe mgikevfteq adlsgitetk 351 klsvsqvvhk avldvaetgt eaaaatgvig girkailpav hfnrpflfvi 401 yhtsaqsilf makvnnpk
89125 --------------------------------------------------- Definition elastase inhibitor, leukocyte - horse (fragment) Protein Name: elastase inhibitor, 89125: [ Whole ] leukocyte PIR Name: A28060 NCBI Seq ID: 89125 Created Aug 28, 1989 Updated Apr 12, 1996 Citation J. Potempa, A. Dubin, W. Watorek & J. Travis (1988). An elastase inhibitor from equine leukocyte cytosol belongs to the serpin superfamily. Further characterization and amino acid sequence of the reactive center. J. Biol. Chem. 263, 7364-7369. MEDLINE identifier: 88213423 Sequence 18 aa 1 lamlmpeenf nadhpfif
1016710 --------------------------------------------------- Definition MEC-9L Protein Name: MEC-9L 1016710: [ Whole ] NCBI Seq ID: 1016710 Updated Apr 9, 1996 Citation H Du, G Gu, C William & M Chalfie (1996). Extracellular proteins needed for C. elegans mechanosensation. Neuron 16, 183-194. MEDLINE identifier: 96158934 Citation Data Submission: G. Gu, C. Williams & M. Chalfie (1995). Coding region Comments: needed for 1016709: 16..2532 mechanosensation; extracellular protein with mutiple EGF-like repeats and Kunitz serpin domains. Sequence 838 aa 1 mflppphklf pfflvflnlv dtkdepvfvk nnedicledv dpgpcqyyqv 51 qwfwdkqvee ckefhyggcm gtknrfsskq qcvkqckykm fnpvavpdlc 101 lldadqghcg dernghwwyf fnqesgecek ffyygcggnd nkfyslhmcr 151 kvcgerlspq iacdhcdlrt sfcksnskfn ytcecrsgye knqygecidi 201 decrgykavc drnawcvnei gsykcecmas yrgdgkhcty vglgrssidc 251 kdcsmhatcm ngvcqckegy egdgfnctdv neclrrpemc nknaecinre 301 gsfictcleg yagngynctv sknscldkfd hdykdtcgne nwrphfffnh 351 qtrmceqfwy dgcrgrsrni fseydtcttm ceetnvltra evcwdkfdmn 401 yrnqcmngqw qqryyfdhas ltcrqfwfdg crsdsrnifd deltcqwlce 451 sqpmyksrsc ledfdeglkk ecnggrwrhq wyfdkgskkc fsfwydgckg 501 anenifqdel sclhtcenpa kkdpkkpwhn ndkfkmkeii gdiykpnltd 551 tclaknpckn ngtcifvwkk dthyckcqpg fhgnncdkvv dydpcaekpc 601 lngatcqiky ndddvdekpt fecfcaagfg rpkcdqrpce snpclnngtc 651 rttkgystyf cecangfggk ncdvsigntp peekfgknve qissgkeewi 701 aqmrqrlket gggiggasgs glksengtmg gssgeksgek ksgknkkska 751 tqvadepykd patrkreree rekkeaeiqa aeeeekqrke yeedaqrkka 801 eemeleakka leaanfglkt dfsmslltil mafvlref
1683577 ---------------------------------------------------
Definition serpin=45 kda monocyte/neutrophil elastase inhibitor {internal
fragment} [human, epidermal carcinoma cell line A431 cells,
Peptide Partial, 67 aa 3 segments]
Segments 1245789 serpin=45 kda monocyte/neutrophil elastase
inhibitor {internal fragment} [human, epidermal
carcinoma cell line A431 cells, Peptide
Partial, 19 aa, segment 1 of 3]
1245790 serpin=45 kda monocyte/neutrophil elastase
inhibitor {internal fragment} [human, epidermal
carcinoma cell line A431 cells, Peptide
Partial, 29 aa, segment 2 of 3]
1245791 serpin=45 kda monocyte/neutrophil elastase
inhibitor {internal fragment} [human, epidermal
carcinoma cell line A431 cells, Peptide
Partial, 19 aa, segment 3 of 3]
NCBI Journal Scan Mol ID: 380809
NCBI Seq ID: 1683577
Updated Apr 1, 1996
Citation Packard,B.Z., Lee,S.S., Remold-O'Donnell,E. & Komoriya,A.
(1995). A serpin from human tumor cells with direct lymphoid
immunomodulatory activity: mitogenic stimulation of human
tumor-infiltrating lymphocytes. Biochim. Biophys. Acta 1269,
41-50. MEDLINE identifier: 96049524
Protein Name: serpin 1245789: 1..19
Description: 45 kda [ Gap ]
monocyte/neutrophil elastase 1245790: 1..29
inhibitor. [ Gap ]
*: Partial 1245791: 1..19
1245789 ---------------------------------------------------
Definition serpin=45 kda monocyte/neutrophil elastase inhibitor {internal
fragment} [human, epidermal carcinoma cell line A431 cells,
Peptide Partial, 19 aa, segment 1 of 3]
NCBI Journal Scan Seq ID: 174561
NCBI Seq ID: 1245789
Created Apr 1, 1996
Citation MEDLINE identifier: 96049524
Figure Table 2, "serpin seg-1"
Numbered from 1
Sequence 19 aa
1 tygadlasvd fqhasedar
1245790 ---------------------------------------------------
Definition serpin=45 kda monocyte/neutrophil elastase inhibitor {internal
fragment} [human, epidermal carcinoma cell line A431 cells,
Peptide Partial, 29 aa, segment 2 of 3]
NCBI Journal Scan Seq ID: 174563
NCBI Seq ID: 1245790
Created Apr 1, 1996
Citation MEDLINE identifier: 96049524
Figure Table 2, "serpin seg-2"
Numbered from 1
Sequence 29 aa
1 vlelpyqgee lsmvillpdd iedestglk
1245791 ---------------------------------------------------
Definition serpin=45 kda monocyte/neutrophil elastase inhibitor {internal
fragment} [human, epidermal carcinoma cell line A431 cells,
Peptide Partial, 19 aa, segment 3 of 3]
NCBI Journal Scan Seq ID: 174565
NCBI Seq ID: 1245791
Created Apr 1, 1996
Citation MEDLINE identifier: 96049524
Figure Table 2, "serpin seg-3"
Numbered from 1
Sequence 19 aa
1 lhewtkpenl dfievnvlp
1083081 --------------------------------------------------- Definition serpin EI - bovine Protein Names: serpin EI; proteinase 1083081: [ Whole ] inhibitor Inh2 PIR Name: S50033 NCBI Seq ID: 1083081 Comment This protein inhibits trypsin and human neutrophil elastase. Created Aug 1, 1995 Updated Feb 23, 1996 Citation S. Christensen & L. Sottrup-Jensen (1994). Characterization of two serpins from bovine plasma and milk. Biochem. J. 303, 383-390. MEDLINE identifier: 95071234 Citation D. Sinha, X. Yang, F. Emig & E.P. Kirby (1994). Isolation and characterization of two protease inhibitors from bovine plasma. J. Biochem. 115, 387-391. MEDLINE identifier: 94334275 Sequence 60 aa 1 lpenvtpeeq hkgtsvdgxv ldvgeegteg aavtavvmat lsvllhtltv 51 sfnrpfllsi
1655809 --------------------------------------------------- Definition pigment epithelium-derived factor precursor Protein Comments: PEDF; secreted 1655809: 21..416 glycoprotein; neurotrophic region, homologous serpin reactive site. Protein 1655809: 1..20 Protein Name: pigment epithelium-derived 1655809: [ Whole ] factor precursor NCBI Seq ID: 1655809 Updated Feb 20, 1996 Citation REF [1] L. Perez-Mediavilla, C. Chew, P. Campochiaro, D.J. Zack & S.P. Becerra. Expression of bovine PEDF. Unpublished Citation REF [2] Data Submission: S.P. Becerra (1996). Coding region function: neurotrophic factor, 1655808: 12..1262 serpin. Comments: PEDF. (experimentally determined) Sequence 416 aa 1 mqalvlllwt gallgfgrcq nagqeagslt pestgapvee edpffkvpvn 51 klaaavsnfg ydlyrvrsge sptanvllsp lsvatalsal slgaeqrtes 101 nihralyydl isnpdihgty kdllasvtap qknlksasri iferklrika 151 sfippleksy gtrpriltgn srvdlqeinn wvqaqmkgkv arstrempse 201 isifllgvay fkgqwvtkfd srktsledfy ldeertvkvp mmsdpqavlr 251 ygldsdlnck iaqlpltgst siifflpqkv tqnltliees ltsefihdid 301 relktvqavl tipklklsye geltksvqel klqslfdapd fskitgkpik 351 ltqvehrvgf ewnedgagtn sspgvqparl tfpldyhlnq pfifvlrdtd 401 tgallfigki ldprgt
575677 --------------------------------------------------- Definition putative serine proteinase inhibitor Protein Name: putative serine proteinase 575677: [ Whole ] inhibitor NCBI Seq ID: 575677 Updated Feb 15, 1996 Citation REF [1] Z. Liang & K. Soderhall (1995). Isolation of cDNA encoding a novel serpin of crayfish hemocytes. Comp. Biochem. Physiol. Biochem. Mol. Biol. 112, 385-391. Citation REF [2] Data Submission: Z. Liang (1994). Coding region 575676: 82..1371 Sequence 429 aa 1 mklavvllvg lagvvppqci shndtlalps spdlahitpf gvdlfkelnp 51 tgttsnfffs pysiwnslvl ayfgssggtr qqlqkvlrlg dpahtlatyr 101 alshlyaerq antsdyvidl anrvyvdekf plrecvkgvl fqevqaidfg 151 qaeeaaarin qlvnettrgk ipelvtardv sgvpmvlvna ayfkglwsna 201 feasetvpek ffsspdqhtf vpmmklisaf kigeseelga tvlempykgk 251 aasmfvllpy ttvtttrvdd ttanntttac nattgkattp ldamllrlts 301 dtlrtglasr ekqevelqlp kfkleqtiin elvdalqrqg ikdlftsnad 351 ltiydpsgrl rvskgihkav vevneegsea aagtglivtf slppkpkkfv 401 cnhpfvfliq dnhtnnilfl gvyrkpqid
1683575 ---------------------------------------------------
Definition Pigment epithelium-derived factor, PEDF {internal fragment}
[cattle, eyes, Peptide Partial, 47 aa 2 segments]
Segments 1176450 Pigment epithelium-derived factor, PEDF
{internal fragment} [cattle, eyes, Peptide
Partial, 27 aa, segment 1 of 2]
1176451 Pigment epithelium-derived factor, PEDF
{internal fragment} [cattle, eyes, Peptide
Partial, 20 aa, segment 2 of 2]
NCBI Journal Scan Mol ID: 377810
NCBI Seq ID: 1683575
Updated Feb 2, 1996
Citation Becerra,S.P., Sagasti,A., Spinella,P. & Notario,V. (1995).
Pigment epithelium-derived factor behaves like a noninhibitory
serpin. Neurotrophic activity does not require the serpin
reactive loop. J. Biol. Chem. 270, 25992-9. MEDLINE
identifier: 96029704
Protein Names: Pigment epithelium-derived 1176450: 1..27
factor; PEDF [ Gap ]
*: Partial 1176451: 1..20
1176450 ---------------------------------------------------
Definition Pigment epithelium-derived factor, PEDF {internal fragment}
[cattle, eyes, Peptide Partial, 27 aa, segment 1 of 2]
NCBI Journal Scan Seq ID: 171927
NCBI Seq ID: 1176450
Created Feb 2, 1996
Citation MEDLINE identifier: 96029704
Figure Fig. 7, "PEDF"
Numbered from 1
Sequence 27 aa
1 dagqeagslt pesxgapvee edpffrv
1176451 ---------------------------------------------------
Definition Pigment epithelium-derived factor, PEDF {internal fragment}
[cattle, eyes, Peptide Partial, 20 aa, segment 2 of 2]
NCBI Journal Scan Seq ID: 171929
NCBI Seq ID: 1176451
Created Feb 2, 1996
Citation MEDLINE identifier: 96029704
Figure Fig. 7, "PEDF"
Numbered from 1
Sequence 20 aa
1 ltfpldyhln qpfifvlxdt
1352735 --------------------------------------------------- Definition PIGMENT EPITHELIUM-DERIVED FACTOR PRECURSOR (PEDF) (EPC-1). Protein Name: PIGMENT EPITHELIUM-DERIVED 1352735: 1..418 FACTOR PRECURSOR SWISS-PROT Name: PEDF_HUMAN, Accession: P36955 NCBI Seq ID: 1352735 Comment [FUNCTION] NEUROTROPHIC PROTEIN; INDUCES EXTENSIVE NEURONAL DIFFERENTIATION IN RETINOBLASTOMA CELLS. DOES NOT SEEM TO HAVE A INHIBITORY ACTION ON PROTEASES. Comment [SUBCELLULAR LOCATION] EXTRACELLULAR. Comment [TISSUE SPECIFICITY] RETINAL PIGMENT EPITHELIAL CELLS. Comment [DEVELOPMENTAL STAGE] EXPRESSED IN QUIESCENT CELLS. Comment [SIMILARITY] WITH SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 189778 Cross-ref NCBI Seq ID: 291990 Cross-ref GenBank Accession: M76979 Cross-ref GenBank Accession: M90439 Cross-ref HSSP P01008 Cross-ref MIM 172860 Cross-ref PROSITE PS00284 Created Jun 1, 1994 Updated Feb 1, 1996 Citation REF [1] F.R. Steele, G.J. Chader, L.V. Johnson & J. Tombran-Tink (1993). Pigment epithelium-derived factor: neurotrophic activity and identification as a member of the serine protease inhibitor gene family. Proc. Natl. Acad. Sci. U.S.A. 90, 1526- 1530. MEDLINE identifier: 93165728 Citation REF [2] R.J. Pignolo, V.J. Cristofalo & M.O. Rotenberg (1993). Senescent WI-38 cells fail to express EPC-1, a gene induced in young cells upon entry into the G0 state. J. Biol. Chem. 268, 8949-8957. MEDLINE identifier: 93232057 Citation REF [3] S.P. Becerra, I. Palmer, A. Kumar, F. Steele, J. Shiloach, V. Notario & G.J. Chader (1993). Overexpression of fetal human pigment epithelium-derived factor in Escherichia coli. A functionally active neurotrophic factor. J. Biol. Chem. 268, 23148-23156. MEDLINE identifier: 94043097 Signal 1352735: 1..17 Mature chain PIGMENT EPITHELIUM-DERIVED FACTOR. 1352735: 18..418 (experimentally determined) glycosylation 1352735: 285 site Conflict DE -> EQ (IN REF. 2). 1352735: 97..98 (experimentally determined) Gene Locus: PEDF 1352735: 1..418 Sequence 418 aa 1 mqalvlllci gallghsscq npasppeegs pdpdstgalv eeedpffkvp 51 vnklaaavsn fgydlyrvrs smspttnvll splsvatals alslgadert 101 esiihralyy dlisspdihg tykelldtvt apqknlksas rivfekklri 151 kssfvaplek sygtrprvlt gnprldlqei nnwvqaqmkg klarstkeip 201 deisilllgv ahfkgqwvtk fdsrktsled fyldeertvr vpmmsdpkav 251 lrygldsdls ckiaqlpltg smsiifflpl kvtqnltlie esltsefihd 301 idrelktvqa vltvpklkls yegevtkslq emklqslfds pdfskitgkp 351 ikltqvehra gfewnedgag ttpspglqpa hltfpldyhl nqpfifvlrd 401 tdtgallfig kildprgp
1352712 --------------------------------------------------- Definition PLASMINOGEN ACTIVATOR INHIBITOR-2, PLACENTAL (PAI-2) (MONOCYTE ARG-SERPIN) (UROKINASE INHIBITOR). Protein Name: PLASMINOGEN ACTIVATOR 1352712: 1..415 INHIBITOR-2, PLACENTAL SWISS-PROT Name: PAI2_HUMAN, Accession: P05120 NCBI Seq ID: 1352712 Comment [FUNCTION] PAI-2 INHIBITS UROKINASE-TYPE PLASMINOGEN ACTIVATOR. THE MONOCYTE DERIVED PAI-2 IS DISTINCT FROM THE ENDOTHELIAL CELL-DERIVED PAI-1. Comment [PTM] THE SIGNAL SEQUENCE IS NOT CLEAVED. Comment [SUBCELLULAR LOCATION] CYTOPLASMIC OR EXTRACELLULAR. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. BELONGS TO THE OV-SERPIN SUBFAMILY. Cross-ref NCBI Seq ID: 189545 Cross-ref NCBI Seq ID: 189563 Cross-ref NCBI Seq ID: 35268 Cross-ref NCBI Seq ID: 386995 Cross-ref NCBI Seq ID: 189547 Cross-ref NCBI Seq ID: 340154 Cross-ref NCBI Seq ID: 641357 Cross-ref NCBI Seq ID: 641374 Cross-ref GenBank Accession: J02685 Cross-ref GenBank Accession: M18082 Cross-ref EMBL Accession: Y00630 Cross-ref GenBank Accession: M24657 Cross-ref GenBank Accession: J03603 Cross-ref GenBank Accession: M31551 Cross-ref EMBL Accession: A21238 Cross-ref EMBL Accession: A21254 Cross-ref HSSP P01008 Cross-ref AARHUS/GHENT-2DPAGE 6314 Cross-ref MIM 173390 Cross-ref PROSITE PS00284 Created Aug 13, 1987 Updated Feb 1, 1996 Citation REF [1] R.D. Ye, T.C. Wun & J.E. Sadler (1987). cDNA cloning and expression in Escherichia coli of a plasminogen activator inhibitor from human placenta. J. Biol. Chem. 262, 3718-3725. MEDLINE identifier: 87137674 Citation REF [2] W.D. Schleuning, R.L. Medcalf, C. Hession, R. Rothenbuhler, A. Shaw & E.K. Kruithof (1987). Plasminogen activator inhibitor 2: regulation of gene transcription during phorbol ester- mediated differentiation of U-937 human histiocytic lymphoma cells. Mol. Cell. Biol. 7, 4564-4567. MEDLINE identifier: 88142852 Citation REF [3] R.D. Ye, S.M. Ahern, M.M. Le Beau, R.V. Lebo & J.E. Sadler (1989). Structure of the gene for human plasminogen activator inhibitor-2. The nearest mammalian homologue of chicken ovalbumin. J. Biol. Chem. 264, 5495-5502. MEDLINE identifier: 89174589 Citation REF [4] A.C. Webb, K.L. Collins, S.E. Snyder, S.J. Alexander, L.J. Rosenwasser, R.L. Eddy, T.B. Shows & P.E. Auron (1987). Human monocyte Arg-Serpin cDNA. Sequence, chromosomal assignment, and homology to plasminogen activator-inhibitor. J. Exp. Med. 166, 77-94. MEDLINE identifier: 87252928 Citation REF [5] T.M. Antalis, M.A. Clark, T. Barnes, P.R. Lehrbach, P.L. Devine, G. Schevzov, N.H. Goss, R.W. Stephens & P. Tolstoshev (1988). Cloning and expression of a cDNA coding for a human monocyte-derived plasminogen activator inhibitor. Proc. Natl. Acad. Sci. U.S.A. 85, 985-989. MEDLINE identifier: 88125032 Citation REF [6] J.A. Samia, S.J. Alexander, K.W. Horton, P.E. Auron, M.G. Byers, T.B. Shows & A.C. Webb (1990). Chromosomal organization and localization of the human urokinase inhibitor gene: perfect structural conservation with ovalbumin. Genomics 6, 159-167. MEDLINE identifier: 90152678 Citation REF [7] H.H. Rasmussen, J. van Damme, M. Puype, B. Gesser, J.E. Celis & J. Vandekerckhove (1992). Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. Electrophoresis 13, 960-969. MEDLINE identifier: 93162043 Signal NOT CLEAVED. 1352712: 1..415 * Partial (experimentally determined) glycosylation 1352712: 75 site glycosylation 1352712: 115 site glycosylation 1352712: 339 site active site REACTIVE BOND. 1352712: 380..381 (experimentally determined) Conflict N -> D (IN REF. 1 AND 2). 1352712: 120 (experimentally determined) Conflict N -> K (IN REF. 1 AND 2). 1352712: 404 (experimentally determined) Conflict S -> C (IN REF. 1 AND 2). 1352712: 413 (experimentally determined) Gene Locus: PAI2 1352712: 1..415 Sequence 415 aa 1 medlcvantl falnlfkhla kasptqnlfl spwsisstma mvymgsrgst 51 edqmakvlqf nevganavtp mtpenftscg fmqqiqkgsy pdailqaqaa 101 dkihssfrsl ssainastgn yllesvnklf geksasfree yirlcqkyys 151 sepqavdfle caeearkkin swvktqtkgk ipnllpegsv dgdtrmvlvn 201 avyfkgkwkt pfekklngly pfrvnsaqrt pvqmmylrek lnigyiedlk 251 aqilelpyag dvsmflllpd eiadvstgle lleseitydk lnkwtskdkm 301 aedevevyip qfkleehyel rsilrsmgme dafnkgranf sgmserndlf 351 lsevfhqamv dvneegteaa agtggvmtgr tghggpqfva dhpflflimh 401 kitncilffg rfssp
1351236 ---------------------------------------------------
Definition THYROXINE-BINDING GLOBULIN PRECURSOR (T4-BINDING GLOBULIN).
Protein Name: THYROXINE-BINDING GLOBULIN 1351236: 1..415
PRECURSOR
SWISS-PROT Name: THBG_HUMAN, Accession: P05543
NCBI Seq ID: 1351236
Comment [FUNCTION] MAJOR THYROID HORMONE TRANSPORT PROTEIN IN SERUM.
Comment [SUBCELLULAR LOCATION] EXTRACELLULAR.
Comment [TISSUE SPECIFICITY] SYNTHESIZED IN THE LIVER; FOUND IN PLASMA.
Comment [DISEASE] DEFECTS IN TBG ARE THE CAUSE OF A WHOLE SPECTRUM OF
TBG DEFICIENCIES CHARACTERIZED BY DECREASED BINDING AFFINITY
FOR THYROXINE (T4) AND TRIIODOTHYRONINE (T3) WHICH RESULTS IN
LOW SERUM T4 AND T3 LEVELS.
Comment [POLYMORPHISM] TWO QUALITATIVE TBG VARIANTS OCCUR IN
PARTICULAR POPULATIONS. TBG-A IS FOUND IN 40% OF AUSTRALIAN
ABORIGINES, IT HAS REDUCED AFFINITY FOR THYROXINE AND
TRIIODOTHYROXINE AND INCREASED SUSCEPTIBILITY TO INACTIVATION
BY HEAT OR ACID. TBG-S ('S' FOR SLOW SHIFT ON ISOELECTIC
FOCUSING) IS FOUND IN BLACKS, ESKIMOS, MELANESIANS,
POLYNESIANS AND INDONESIANS, BUT NOT IN CAUCASIANS; TBG-S IS
SLIGHTLY MORE THERMOLABILE.
Comment [SIMILARITY] WITH SERPIN SERINE PROTEASE INHIBITORS.
Cross-ref NCBI Seq ID: 338697
Cross-ref NCBI Seq ID: 37142
Cross-ref NCBI Seq ID: 405514
Cross-ref GenBank Accession: M14091
Cross-ref EMBL Accession: X64171
Cross-ref GenBank Accession: L13470
Cross-ref HSSP P01011
Cross-ref MIM 188600
Cross-ref MIM 314200
Cross-ref PROSITE PS00284
Created Nov 1, 1988
Updated Feb 1, 1996
Citation REF [1]
I.L. Flink, T.J. Bailey, T.A. Gustafson, B.E. Markham & E.
Morkin (1986). Complete amino acid sequence of human
thyroxine-binding globulin deduced from cloned DNA: close
homology to the serine antiproteases. Proc. Natl. Acad. Sci.
U.S.A. 83, 7708-7712. MEDLINE identifier: 87017018
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M.T. Akbari, A. Kapadi, M.J. Farmer, N.J. Fitch, K.P. McCann,
S. Kordestani, I.L. Flink, M.C. Sheppard & D.B. Ramsden
(1993). The structure of the human thyroxine binding globulin
(TBG) gene. Biochim. Biophys. Acta 1216, 446-454. MEDLINE
identifier: 94092738
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Y. Hayashi, Y. Mori, O.E. Janssen, T. Sunthornthepvarakul,
R.E. Weiss, K. Takeda, M. Weinberg, H. Seo, G.I. Bell & S.
Refetoff (1993). Human thyroxine-binding globulin gene:
complete sequence and transcriptional regulation. Mol.
Endocrinol. 7, 1049-1060. MEDLINE identifier: 94049804
Citation REF [4]
S.Y. Cheng (1977). Partial amino acid sequence of human
thyroxine-binding globulin. Further evidence for a single
polypeptide chain. Biochem. Biophys. Res. Commun. 79, 1212-
1218. MEDLINE identifier: 78103214
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O.E. JANSSEN, R. BERTENSHAW, K. TAKEDA, R. WEISS & S. REFETOFF
(1992)TRENDS ENDOCRINOL. METAB. 3, 49-53.
Citation REF [6]
Y. Mori, K. Takeda, M. Charbonneau & S. Refetoff (1990).
Replacement of Leu227 by Pro in thyroxine-binding globulin
(TBG) is associated with complete TBG deficiency in three of
eight families with this inherited defect. J. Clin.
Endocrinol. Metab. 70, 804-809. MEDLINE identifier: 90171204
Citation REF [7]
Y. Mori, S. Seino, K. Takeda, I.L. Flink, Y. Murata, G.I. Bell
& S. Refetoff (1989). A mutation causing reduced biological
activity and stability of thyroxine-binding globulin probably
as a result of abnormal glycosylation of the molecule. Mol.
Endocrinol. 3, 575-579. MEDLINE identifier: 89313802
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T. Shirotani, H. Kishikawa, N. Wake, N. Miyamura, Y.
Hashimoto, S. Motoyoshi, K. Yamaguchi & M. Shichiri (1992).
Thyroxine-binding globulin variant (TBG-Kumamoto):
identification of a point mutation and genotype analysis of
its family. Endocrinol. Jpn. 39, 577-584. MEDLINE
identifier: 93193648
Citation REF [9]
O.E. Janssen, K. Takeda & S. Refetoff (1991). Sequence of the
variant thyroxine-binding globulin (TBG) in a Montreal family
with partial TBG deficiency. Hum. Genet. 87, 119-122.
MEDLINE identifier: 91293773
Citation REF [10]
R. Bertenshaw, K. Takeda & S. Refetoff (1991). Sequencing of
the variant thyroxine-binding globulin (TBG)-Quebec reveals
two nucleotide substitutions. Am. J. Hum. Genet. 48, 741-744.
MEDLINE identifier: 91196732
Citation REF [11]
R. Bertenshaw, D. Sarne, J. Tornari, M. Weinberg & S. Refetoff
(1992). Sequencing of the variant thyroxine-binding globulin
(TBG)-San Diego reveals two nucleotide substitutions.
Biochim. Biophys. Acta 1139, 307-310. MEDLINE identifier:
92385494
Citation REF [12]
K. Takeda, Y. Mori, S. Sobieszczyk, H. Seo, M. Dick, F.
Watson, I.L. Flink, S. Seino, G.I. Bell & S. Refetoff (1989).
Sequence of the variant thyroxine-binding globulin of
Australian aborigines. Only one of two amino acid replacements
is responsible for its altered properties. J. Clin. Invest.
83, 1344-1348. MEDLINE identifier: 89198092
Citation REF [13]
M.R. Waltz, T.N. Pullman, K. Takeda, P. Sobieszczyk & S.
Refetoff (1990). Molecular basis for the properties of the
thyroxine-binding globulin-slow variant in American blacks.
J. Endocrinol. Invest. 13, 343-349. MEDLINE identifier:
90317289
Signal (experimentally determined) 1351236: 1..20
Mature chain THYROXINE-BINDING GLOBULIN. 1351236: 21..415
(experimentally determined)
glycosylation (experimentally determined) 1351236: 36
site
glycosylation (experimentally determined) 1351236: 99
site
glycosylation IN VARIANT GARY. 1351236: 116
site
glycosylation (experimentally determined) 1351236: 165
site
glycosylation (experimentally determined) 1351236: 253
site
Variant S -> T (IN SAN DIEGO; PARTIAL TBG 1351236: 43
DEFICIENCY).
(experimentally determined)
Variant I -> N (IN GARY; SEVERE TBG 1351236: 116
DEFICIENCY).
(experimentally determined)
Variant A -> P (IN MONTREAL/TBG-M; PARTIAL 1351236: 133
TBG DEFICIENCY).
(experimentally determined)
Variant D -> N (IN TBG-S/SLOW). 1351236: 191
(experimentally determined)
Variant A -> T (IN TBG-A/ABORIGINE). 1351236: 211
(experimentally determined)
Variant L -> P (IN CD5; COMPLETE TBG 1351236: 247
DEFICIENCY).
(experimentally determined)
Variant L -> F (COMMON POLYMORPHISM). 1351236: 303
(experimentally determined)
Variant H -> Y (IN QUEBEC; PARTIAL TBG 1351236: 351
DEFICIENCY).
(experimentally determined)
Variant P -> L (IN KUMAMOTO; TBG 1351236: 383
DEFICIENCY).
(experimentally determined)
Conflict CH -> DS (IN REF. 4). 1351236: 30..31
(experimentally determined)
Conflict T -> S (IN REF. 4). 1351236: 38
(experimentally determined)
Conflict I -> T (IN REF. 1). 1351236: 197
(experimentally determined)
Gene Locus: TBG 1351236: 1..415
Sequence 415 aa
1 mspflylvll vlglhatihc aspegkvtac hssqpnatly kmssinadfa
51 fnlyrrftve tpdkniffsp vsisaalvml sfgaccstqt eivetlgfnl
101 tdtpmveiqh gfqhlicsln fpkkelelqi gnalfigkhl kplakflndv
151 ktlyetevfs tdfsnisaak qeinshvemq tkgkvvgliq dlkpntimvl
201 vnyihfkaqw anpfdpskte dsssflidkt ttvqvpmmhq meqyyhlvdm
251 elnctvlqmd ysknalalfv lpkegqmesv eaamssktlk kwnrllqkgw
301 vdlfvpkfsi satydlgatl lkmgiqhays enadfsglte dnglklsnaa
351 hkavlhigek gteaaavpev elsdqpentf lhpiiqidrs fmllilerst
401 rsilflgkvv nptea
1346272 --------------------------------------------------- Definition HEPARIN COFACTOR II PRECURSOR (HC-II). Protein Name: HEPARIN COFACTOR II 1346272: 1..480 PRECURSOR SWISS-PROT Name: HEP2_RABIT, Accession: P47776 NCBI Seq ID: 1346272 Comment [FUNCTION] THROMBIN INHIBITOR ACTIVATED BY THE GLYCOSAMINOGLYCANS, HEPARIN OR DERMATAN SULFATE. IN THE PRESENCE OF THE LATTER, HC-II BECOMES THE PREDOMINANT THROMBIN INHIBITOR IN PLACE OF ANTITHROMBIN III (AT). Comment [PTM] DIFFERENT COMPOSITION OF THE N-LINKED OLIGOSACCHARIDES APPEARS TO LEAD TO THE 2 FORMS OF THIS PROTEIN (56 AND 60 KD). Comment [DOMAIN] THE N-TERMINAL ACIDIC REPEAT REGION MEDIATES, IN PART, THE GLYCOSAMINOGLYCAN-ACCELERATED THROMBIN INHIBITION (BY SIMILARITY). Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 688191 Cross-ref GenBank Accession: S73493 Created Feb 1, 1996 Updated Feb 1, 1996 Citation REF [1] W.P. Sheffield, P.D. Schuyler & M.A. Blajchman (1994). Molecular cloning and expression of rabbit heparin cofactor II: a plasma thrombin inhibitor highly conserved between species. Thromb. Haemost. 71, 778-782. MEDLINE identifier: 95064663 Signal 1346272: 1..19 Mature chain HEPARIN COFACTOR II. 1346272: 20..480 (experimentally determined) Domain 2 X 11 AA APPROXIMATE REPEATS, 1346272: 56..80 ASP/GLU- RICH (ACIDIC) (HIRUDIN- LIKE). (experimentally determined) Repetitive 1. 1346272: 56..66 region (experimentally determined) Repetitive 2. 1346272: 70..80 region (experimentally determined) Domain GLYCOSAMINOGLYCAN-BINDING SITE. 1346272: 173..193 active site REACTIVE BOND. 1346272: 444..445 glycosylation 1346272: 32 site glycosylation 1346272: 169 site glycosylation 1346272: 368 site glycosylation 1346272: 404 site modified site SULFATION. 1346272: 62 modified site SULFATION. 1346272: 75 Gene Locus: HCF2 1346272: 1..480 Sequence 480 aa 1 mqhrphllli sltimsvcgg sngltdqlnn knltmpllpi efhkentvtn 51 dwipegeedd dyldleklls edddyidiid avsptdseas agnilqlfqg 101 ksriqrlnil nakfafslyr alkdqanafd nifiapvgis tamgmislgl 151 kgetheqvhs vlhfrdfvna sskyeiltih nlfrklthrl frrnfgytlr 201 svndlyvqkq fpiredfkak vreyyfaeaq aadfsdpafi skannhilkv 251 tkglikeale nvdpatqmmi lnciyfkgtw vnkfpvemth nhnfrlnere 301 vvkvsmmqtk gnflaandqe lacdvlqley vggismlivv phklsgmktl 351 eaqltpqvve rwqksmtnrt revllpkfkl eknynlveal ksmgvtelfd 401 kngnmsgisd qgitmdlfkh qgtitvneeg tqaaavttvg fmplstqvrf 451 tvdrpflflv yehrtscllf mgkvanpvrs
1346271 --------------------------------------------------- Definition HEPARIN COFACTOR II PRECURSOR (HC-II). Protein Name: HEPARIN COFACTOR II 1346271: 1..478 PRECURSOR SWISS-PROT Name: HEP2_MOUSE, Accession: P49182 NCBI Seq ID: 1346271 Comment [FUNCTION] THROMBIN INHIBITOR ACTIVATED BY THE GLYCOSAMINOGLYCANS, HEPARIN OR DERMATAN SULFATE. IN THE PRESENCE OF THE LATTER, HC-II BECOMES THE PREDOMINANT THROMBIN INHIBITOR IN PLACE OF ANTITHROMBIN III (AT). ALSO INHIBITS CHYMOTRYPSIN, BUT IN A GLYCOSAMINOGLYCAN-INDEPENDENT MANNER. Comment [TISSUE SPECIFICITY] EXPRESSED PREDOMINANTLY IN LIVER. Comment [PTM] DIFFERENT COMPOSITION OF THE N-LINKED OLIGOSACCHARIDES APPEARS TO LEAD TO 2 FORMS OF THIS PROTEIN (68 AND 72 KD). Comment [DOMAIN] THE N-TERMINAL ACIDIC REPEAT REGION MEDIATES, IN PART, THE GLYCOSAMINOGLYCAN-ACCELERATED THROMBIN INHIBITION (BY SIMILARITY). Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 466374 Cross-ref GenBank Accession: U07425 Created Feb 1, 1996 Updated Feb 1, 1996 Citation REF [1] G.S. Zhang, J.H. Mehringer, V.M. Van Deerlin, C.A. Kozak & D.M. Tollefsen (1994). Murine heparin cofactor II: purification, cDNA sequence, expression, and gene structure. Biochemistry 33, 3632-3642. MEDLINE identifier: 94190883 Signal (experimentally determined) 1346271: 1..23 Mature chain HEPARIN COFACTOR II. 1346271: 24..478 (experimentally determined) Domain 2 X 11 AA APPROXIMATE REPEATS, 1346271: 54..78 ASP/GLU- RICH (ACIDIC) (HIRUDIN- LIKE). (experimentally determined) Repetitive 1. 1346271: 54..64 region (experimentally determined) Repetitive 2. 1346271: 68..78 region (experimentally determined) Domain GLYCOSAMINOGLYCAN-BINDING SITE. 1346271: 171..191 active site REACTIVE BOND. 1346271: 442..443 modified site SULFATION. 1346271: 60 modified site SULFATION. 1346271: 73 glycosylation 1346271: 30 site glycosylation 1346271: 167 site glycosylation 1346271: 366 site glycosylation 1346271: 402 site Gene Locus: HCF2 1346271: 1..478 Sequence 478 aa 1 mkhplctlls litfmcigsk glaeqltnen lttsflpanf hkentvtndw 51 ipegeededy ldlekllged ddyiyiidav sptdsessag nilqlfqgks 101 riqrlnilna kfafnlyrvl kdqattsdnl fiapvgista mgmislglrg 151 etheevhsvl hfrdfvnass kyevttihnl frklthrlfr rnfgytlrsv 201 nglyiqkqfp iredfkaamr efyfaeaqea nfpdpafisk annhilkltk 251 glikealeni dpatqmliln ciyfkgtwvn kfpvemthnh nfrlnerevv 301 kvsmmqtkgn flaandqeld cdilqleyvg gismlivvpr klsgmktlea 351 qltpqvverw qksmtnrtre vllpkfklek nynlvevlks mgitklfnkn 401 gnmsgisdqr iaidlfkhqs titvneegtq aaavttvgfm plstqvrftv 451 drpflflvye hrtscllfmg kvtnpaks
547892 --------------------------------------------------- Definition MASPIN PRECURSOR (PROTEASE INHIBITOR 5). Protein Name: MASPIN PRECURSOR 547892: 1..375 SWISS-PROT Name: MASP_HUMAN, Accession: P36952 NCBI Seq ID: 547892 Comment [FUNCTION] MAY HAVE A BIOLOGICAL ROLE IN BENIGN BREAST TISSUE AND A POTENTIALLY PIVOTAL ALTERATION IN EXPRESSION IS SEEN DURING PROGRESSION OF BREAST CANCER. SEEMS TO FUNCTION AS TUMOR SUPRESSOR. Comment [SUBCELLULAR LOCATION] EXTRACELLULAR. Comment [TISSUE SPECIFICITY] NORMAL MAMMARY EPITHELIAL CELLS. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. BELONGS TO THE OV-SERPIN SUBFAMILY. Cross-ref NCBI Seq ID: 453369 Cross-ref GenBank Accession: U04313 Cross-ref HSSP P05619 Cross-ref MIM 154790 Cross-ref PROSITE PS00284 Created Jun 1, 1994 Updated Feb 1, 1996 Citation REF [1] Z. Zou, A. Anisowicz, M.J. Hendrix, A. Thor, M. Neveu, S. Sheng, K. Rafidi, E. Seftor & R. Sager (1994). Maspin, a serpin with tumor-suppressing activity in human mammary epithelial cells. Science 263, 526-529. MEDLINE identifier: 94120413 Signal * Partial 547892: 1..375 Mature chain MASPIN. 547892: 1..375 * Partial (experimentally determined) active site REACTIVE BOND. 547892: 340..341 glycosylation 547892: 99 site glycosylation 547892: 133 site glycosylation 547892: 188 site glycosylation 547892: 361 site Gene Locus: PI5 547892: 1..375 Sequence 375 aa 1 mdalqlansa favdlfkqlc ekeplgnvlf spiclstsls laqvgakgdt 51 aneigqvlhf envkdipfgf qtvtsdvnkl ssfyslklik rlyvdkslnl 101 stefisstkr pyakeletvd fkdkleetkg qinnsikdlt dghfenilad 151 nsvndqtkil vvnaayfvgk wmkkfpeset kecpfrlnkt dtkpvqmmnm 201 eatfcmgnid sinckiielp fqnkhlsmfi llpkdvedes tglekiekql 251 nseslsqwtn pstmanakvk lsipkfkvek midpkaclen lglkhifsed 301 tsdfsgmset kgvalsnvih kvcleitedg gdsievpgar ilqhkdelna 351 dhpfiyiirh nktrniiffg kfcsp
464798 --------------------------------------------------- Definition SERINE PROTEINASE INHIBITOR 2. Protein Name: SERINE PROTEINASE INHIBITOR 464798: 1..344 2 SWISS-PROT Name: SPI2_VARV, Accession: P33830 NCBI Seq ID: 464798 Comment [FUNCTION] MAY BE INVOLVED IN THE REGULATION OF THE COMPLEMENT CASCADE. Comment [SUBCELLULAR LOCATION] CYTOPLASMIC (POTENTIAL). Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Comment [SIMILARITY] HIGHEST WITH COWPOX VIRUS CRMA. Cross-ref NCBI Seq ID: 457072 Cross-ref NCBI Seq ID: 516432 Cross-ref NCBI Seq ID: 439090 Cross-ref NCBI Seq ID: 885841 Cross-ref EMBL Accession: X69198 Cross-ref EMBL Accession: X67117 Cross-ref GenBank Accession: L22579 Cross-ref GenBank Accession: U18341 Cross-ref HSSP P05619 Cross-ref PROSITE PS00284 Created Feb 1, 1994 Updated Feb 1, 1996 Citation REF [1] S.N. Shchelkunov, V.M. Blinov & L.S. Sandakhchiev (1993). Genes of variola and vaccinia viruses necessary to overcome the host protective mechanisms. FEBS Lett. 319, 80-83. MEDLINE identifier: 93202281 Citation REF [2] R.F. MASSUNG, J.J. ESPOSITO, L. LIU, J. QI, T.R. UTTERBACK, J.C. KNIGHT, L. AUBIN, T.E. YURAN, J.M. PARSONS, V.N. LOPAREV, N.A. SELIVANOV, K.F. CAVALLARO, A.R. KERLAVAGE, B.W.J. MAHY & C.J. VENTER (1993). Potential virulence determinants in terminal regions of variola smallpox virus genome. Nature 366, 748-751. MEDLINE identifier: 94088747 Citation REF [3] Data Submission: R.F. MASSUNG, V.N. LOPAREV, J.C. KNIGHT, V.E. CHIZHIKOV, J.M. PARSONS, A.V. TOTMENIN, S.N. SHCHELKUNOV & J.J. ESPOSITO (1994). active site REACTIVE BOND. 464798: 306..307 Gene Locus: B13R 464798: 1..344 Sequence 344 aa 1 mdifreiass tkgenvfisp atissvltil yygangstae qlskyvekee 51 tmdkvsaqni sfksmnkvyg rysavfknsf lgkigdnfqt vdftdcrtid 101 ainkcvdvft egkinpllte qlspntclla isavyfkakw lipfkkefts 151 dypfyvspte mvdvsmmsmy gesfnyasvk esfgnfsiie lpyvgntsmm 201 vilpdkidgl esikqnltdt nfkkwcnsle atfidvhipk fkvtgsynlv 251 dtlvklgltd vfystgdysn mcnsdvsvda mihktyidvn eeyteaaaat 301 svlvadcast vtnefcadhp fiyvirhvdg kilfvgrycs pttn
464797 --------------------------------------------------- Definition SERINE PROTEINASE INHIBITOR 1. Protein Name: SERINE PROTEINASE INHIBITOR 464797: 1..357 1 SWISS-PROT Name: SPI1_VARV, Accession: P33829 NCBI Seq ID: 464797 Comment [FUNCTION] THIS VIRAL PROTEIN MAY BE INVOLVED IN THE REGULATION OF THE COMPLEMENT CASCADE. Comment [SUBCELLULAR LOCATION] CYTOPLASMIC (POTENTIAL). Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 457084 Cross-ref NCBI Seq ID: 516443 Cross-ref NCBI Seq ID: 439099 Cross-ref NCBI Seq ID: 885852 Cross-ref EMBL Accession: X69198 Cross-ref EMBL Accession: X67117 Cross-ref GenBank Accession: L22579 Cross-ref GenBank Accession: U18341 Cross-ref HSSP P05619 Cross-ref PROSITE PS00284 Created Feb 1, 1994 Updated Feb 1, 1996 Citation REF [1] S.N. Shchelkunov, V.M. Blinov & L.S. Sandakhchiev (1993). Genes of variola and vaccinia viruses necessary to overcome the host protective mechanisms. FEBS Lett. 319, 80-83. MEDLINE identifier: 93202281 Citation REF [2] R.F. MASSUNG, J.J. ESPOSITO, L. LIU, J. QI, T.R. UTTERBACK, J.C. KNIGHT, L. AUBIN, T.E. YURAN, J.M. PARSONS, V.N. LOPAREV, N.A. SELIVANOV, K.F. CAVALLARO, A.R. KERLAVAGE, B.W.J. MAHY & C.J. VENTER (1993). Potential virulence determinants in terminal regions of variola smallpox virus genome. Nature 366, 748-751. MEDLINE identifier: 94088747 Citation REF [3] Data Submission: R.F. MASSUNG, V.N. LOPAREV, J.C. KNIGHT, V.E. CHIZHIKOV, J.M. PARSONS, A.V. TOTMENIN, S.N. SHCHELKUNOV & J.J. ESPOSITO (1994). active site REACTIVE BOND. 464797: 322..323 Gene Locus: SPI-1 464797: 1..357 Sequence 357 aa 1 mdifkelilk ypdenvlisp vsilstlsil nhgaagstae qlskyienvn 51 entpddkkdd nndmdvdvpy catlaianki ycsdsiefha sflqkikddf 101 qtvnfnnanq tkelinewvk tmtngkinsl ltsplpintr mtvvsavhfk 151 amwkypfskh ltytdkfyis knivtsvdmm vstendlqyv hinelfggfs 201 iidipyegns smviilpddi eglyniekhi teenfkkwcg klytksidly 251 mpkfklkmte synlvpilen lgltnifgyy adfskmcnet itvekflhkt 301 fidvneeyte asaitgvfmt nfsmvyrtkv yinhpfiymi kdntgrilfi 351 gkycypq
462410 --------------------------------------------------- Definition LEUKOCYTE ELASTASE INHIBITOR (LEI). Protein Name: LEUKOCYTE ELASTASE INHIBITOR462410: 1..379 SWISS-PROT Name: ILEU_HORSE, Accession: P05619 NCBI Seq ID: 462410 Comment [FUNCTION] THIS INHIBITOR IS THOUGHT TO BE INVOLVED IN THE CONTROL OF INTRACELULAR PROTEIN TURNOVER. BINDS TO THYMOSIN BETA-4. Comment [SUBCELLULAR LOCATION] CYTOPLASMIC. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. BELONGS TO THE OV-SERPIN SUBFAMILY. Cross-ref NCBI Seq ID: 164241 Cross-ref GenBank Accession: M91161 Cross-ref PDB Molecule: 1HLE, Chain: (space) Cross-ref PROSITE PS00284 Created Nov 1, 1988 Updated Feb 1, 1996 Citation REF [1] T. Kordula, A. Dubin, H. Schooltink, A. Koj, P.C. Heinrich & S. Rose-John (1993). Molecular cloning and expression of an intracellular serpin: an elastase inhibitor from horse leucocytes. Biochem. J. 293, 187-193. MEDLINE identifier: 93319507 Citation REF [2] A. Dubin, J. Travis, J.J. Enghild & J. Potempa (1992). Equine leukocyte elastase inhibitor. Primary structure and identification as a thymosin-binding protein. J. Biol. Chem. 267, 6576-6583. MEDLINE identifier: 92202200 Citation REF [3] J. Potempa, A. Dubin, W. Watorek & J. Travis (1988). An elastase inhibitor from equine leukocyte cytosol belongs to the serpin superfamily. Further characterization and amino acid sequence of the reactive center. J. Biol. Chem. 263, 7364-7369. MEDLINE identifier: 88213423 Citation REF [4] U. Baumann, W. Bode, R. Huber, J. Travis & J. Potempa (1992). Crystal structure of cleaved equine leucocyte elastase inhibitor determined at 1.95 A resolution. J. Mol. Biol. 226, 1207-1218. MEDLINE identifier: 92389327 blocked site (WITH AN UNKNOWN CHEMICAL GROUP). 462410: 1 (experimentally determined) active site REACTIVE BOND. 462410: 344..345 (experimentally determined) Helical region (experimentally determined) 462410: 2..22 Beta-strand (experimentally determined) 462410: 28..30 region Helical region (experimentally determined) 462410: 32..44 Hydrogen (experimentally determined) 462410: 45 bonded turn Helical region (experimentally determined) 462410: 48..58 Hydrogen (experimentally determined) 462410: 59 bonded turn Helical region (experimentally determined) 462410: 60..62 Hydrogen (experimentally determined) 462410: 64..65 bonded turn Helical region (experimentally determined) 462410: 66..77 Hydrogen (experimentally determined) 462410: 78 bonded turn Beta-strand (experimentally determined) 462410: 85..95 region Hydrogen (experimentally determined) 462410: 96..97 bonded turn Helical region (experimentally determined) 462410: 102..112 Beta-strand (experimentally determined) 462410: 115..119 region Hydrogen (experimentally determined) 462410: 121..123 bonded turn Helical region (experimentally determined) 462410: 125..139 Hydrogen (experimentally determined) 462410: 140..142 bonded turn Hydrogen (experimentally determined) 462410: 150..151 bonded turn Hydrogen (experimentally determined) 462410: 155..156 bonded turn Beta-strand (experimentally determined) 462410: 157..171 region Helical region (experimentally determined) 462410: 177..179 Beta-strand (experimentally determined) 462410: 181..186 region Beta-strand (experimentally determined) 462410: 192..209 region Helical region (experimentally determined) 462410: 210..212 Hydrogen (experimentally determined) 462410: 213 bonded turn Beta-strand (experimentally determined) 462410: 214..221 region Hydrogen (experimentally determined) 462410: 222..223 bonded turn Beta-strand (experimentally determined) 462410: 226..233 region Helical region (experimentally determined) 462410: 244..248 Hydrogen (experimentally determined) 462410: 249 bonded turn Helical region (experimentally determined) 462410: 252..259 Helical region (experimentally determined) 462410: 261..263 Beta-strand (experimentally determined) 462410: 265..274 region Beta-strand (experimentally determined) 462410: 276..283 region Helical region (experimentally determined) 462410: 285..291 Hydrogen (experimentally determined) 462410: 292 bonded turn Helical region (experimentally determined) 462410: 295..297 Hydrogen (experimentally determined) 462410: 299..301 bonded turn Helical region (experimentally determined) 462410: 305..308 Beta-strand (experimentally determined) 462410: 313..326 region Beta-strand (experimentally determined) 462410: 330..343 region Beta-strand (experimentally determined) 462410: 350..353 region Beta-strand (experimentally determined) 462410: 358..364 region Hydrogen (experimentally determined) 462410: 365..368 bonded turn Beta-strand (experimentally determined) 462410: 369..376 region Gene Locus: ELANH2 462410: 1..379 Sequence 379 aa 1 meqlstanth favdlfraln esdptgnifi splsissala miflgtrgnt 51 aaqvskalyf dtvedihsrf qslnadinkp gapyilklan rlygektynf 101 ladflastqk mygaelasvd fqqapedark einewvkgqt egkipellvk 151 gmvdnmtklv lvnaiyfkgn wqekfmkeat rdapfrlnkk dtktvkmmyq 201 kkkfpynyie dlkcrvlelp yqgkelsmii llpddiedes tglekiekql 251 tleklrewtk penlylaevn vhlprfklee sydltshlar lgvqdlfnrg 301 kadlsgmsga rdlfvskiih ksfvdlneeg teaaaatagt imlamlmpee 351 nfnadhpfif firhnpsani lflgrfssp
417185 --------------------------------------------------- Definition LEUKOCYTE ELASTASE INHIBITOR (LEI) (LEUCOCYTE NEUTRAL PROTEINASE INHIBITOR) (LNPI). Protein Name: LEUKOCYTE ELASTASE INHIBITOR417185: 1..378 SWISS-PROT Name: ILEU_PIG, Accession: P80229 NCBI Seq ID: 417185 Comment [SUBCELLULAR LOCATION] CYTOPLASMIC. Comment [SUBUNIT] HOMODIMER, LINKED BY A DISULFIDE BOND. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. BELONGS TO THE OV-SERPIN SUBFAMILY. Cross-ref HSSP P01008 Cross-ref PROSITE PS00284 Created Oct 1, 1993 Updated Feb 1, 1996 Citation REF [1] W.F. Teschauer, R. Mentele & C.P. Sommerhoff (1993). Primary structure of a porcine leukocyte serpin. Eur. J. Biochem. 217, 519-526. MEDLINE identifier: 94039085 blocked site (experimentally determined) 417185: 1 disulfide bond INTERCHAIN. 417185: 80 bond active site REACTIVE BOND. 417185: 343..344 Gene Locus: ELANH2 417185: 1..378 Sequence 378 aa 1 meqlsaantr faldlfraln esnpagnifi spfsissala millgtrgnt 51 eaqmskalhf dtvkdihsrf qslnadinkc gasyilklan rlfgektyhf 101 lpeflastqk tygaelasvd flraseeark ainewvkeqt egkipellas 151 gvvdsatklv lvnaiyfkgs wqekfmteat kdapfrlnkk dsktvkmmyq 201 kkkfpfgyik elkcrvlelp yqgkdlsmvi llpdsiedes tglrkieqhl 251 tleklnewtk pdnlellevn vhlprfrlee sydlnaplar lgvqdlfgsr 301 adltgmsear dlfiskvvhk afvevneegt eaaaatagia vfamlmpeed 351 fiadhpfiff irhnpssnil flgrlssp
266407 --------------------------------------------------- Definition KALLIKREIN-BINDING PROTEIN PRECURSOR (KBP) (GROWTH HORMONE- REGULATED PROTEINASE INHIBITOR) (SERINE PROTEASE INHIBITOR 2) (SPI-2) (GHR-P63) (SPI-2.3) (THYROID HORMONE-REGULATED PROTEIN). Protein Name: KALLIKREIN-BINDING PROTEIN 266407: 1..416 PRECURSOR SWISS-PROT Name: KBP_RAT, Accession: P05545 NCBI Seq ID: 266407 Comment [FUNCTION] BINDS TO AND INHIBITS KALLIKREINS. Comment [TISSUE SPECIFICITY] LIVER. Comment [INDUCTION] BY GROWTH HORMONE, THYROID HORMONE AND SEX HORMONES. ITS EXPRESSION IS REDUCED BY INFLAMMATION. IN MALE RATS, ITS LEVEL IS SEVERALFOLD HIGHER THAN IN FEMALE RATS. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 57233 Cross-ref NCBI Seq ID: 207044 Cross-ref NCBI Seq ID: 57237 Cross-ref NCBI Seq ID: 57294 Cross-ref GenBank Accession: M67496 Cross-ref EMBL Accession: X16358 Cross-ref GenBank Accession: M15916 Cross-ref EMBL Accession: X16362 Cross-ref EMBL Accession: X05348 Cross-ref HSSP P01008 Cross-ref PROSITE PS00284 Created Nov 1, 1988 Updated Feb 1, 1996 Citation REF [1] K.X. Chai, J.X. Ma, S.R. Murray, J. Chao & L. Chao (1991). Molecular cloning and analysis of the rat kallikrein-binding protein gene. J. Biol. Chem. 266, 16029-16036. MEDLINE identifier: 91340751 Citation REF [2] G. Pages, J.F. Rouayrenc, G. Le Cam, M. Mariller & A. Le Cam (1990). Molecular characterization of three rat liver serine- protease inhibitors affected by inflammation and hypophysectomy. Protein and mRNA analysis and cDNA cloning. Eur. J. Biochem. 190, 385-391. MEDLINE identifier: 90306038 Citation REF [3] J.B. Yoon, H.C. Towle & S. Seelig (1987). Growth hormone induces two mRNA species of the serine protease inhibitor gene family in rat liver. J. Biol. Chem. 262, 4284-4289. MEDLINE identifier: 87166046 Citation REF [4] A. Le Cam, G. Pages, P. Auberger, G. Le Cam, P. Leopold, R. Benarous & N. Glaichenhaus (1987). Study of a growth hormone- regulated protein secreted by rat hepatocytes: cDNA cloning, anti-protease activity and regulation of its synthesis by various hormones. EMBO J. 6, 1225-1232. MEDLINE identifier: 87275813 Citation REF [5] Data Submission: A. LE CAM (1987). Citation REF [6] J. Chao, K.X. Chai, L.M. Chen, W. Xiong, S. Chao, C. Woodley- Miller, L.X. Wang, H.S. Lu & L. Chao (1990). Tissue kallikrein-binding protein is a serpin. I. Purification, characterization, and distribution in normotensive and spontaneously hypertensive rats. J. Biol. Chem. 265, 16394- 16401. MEDLINE identifier: 90375506 Signal * Partial 266407: 1..416 (experimentally determined) Mature chain KALLIKREIN-BINDING PROTEIN. 266407: 1..416 * Partial (experimentally determined) active site REACTIVE BOND. 266407: 379..380 glycosylation 266407: 102 site glycosylation 266407: 182 site glycosylation 266407: 220 site glycosylation 266407: 267 site Variant E -> D. 266407: 326 (experimentally determined) Conflict V -> G (IN REF. 3). 266407: 98 (experimentally determined) Conflict H -> HH (IN REF. 2). 266407: 112 (experimentally determined) Conflict L -> P (IN REF. 2). 266407: 387 (experimentally determined) Sequence 416 aa 1 mafiaalgll magicpavlc dgilgrdtlp hedqgkgrql hsltlasint 51 dftlslykkl alrnpdknvv fsplsisaal ailslgakds tmeeilevlk 101 fnlteiteee ihqgfghllq rlsqpedqae intgsalfid keqpilsefq 151 ektralyqae afvadfkqcn eakkfindyv snqtqgkiae lfselderts 201 mvlvnyllfk gkwkvpfnpn dtfesefyld ekrsvkvpmm kikdlttpyi 251 rdeelscsvl elkytgnasa lfilpdqgkm qqvesslqpe tlkkwkdslr 301 priiselrmp kfsistdynl eevlpelgir kifsqqadls ritgtknlhv 351 sqvvhkavld vdetgtegaa atavtaalks lpqtipllnf nrpfmlvitd 401 nngqsvffmg kvtnpm
134436 --------------------------------------------------- Definition ALASERPIN PRECURSOR (SERPIN 1). Protein Name: ALASERPIN PRECURSOR 134436: 1..392 SWISS-PROT Name: SERA_MANSE, Accession: P14754 NCBI Seq ID: 134436 Comment [FUNCTION] INHIBITS ELASTASE. Comment [SUBCELLULAR LOCATION] EXTRACELLULAR. Comment [TISSUE SPECIFICITY] HEMOLYMPH. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Comment [ALTERNATIVE PRODUCTS] VARIOUS FORMS ARE PRODUCED BY ALTERNATIVE SPLICING. Cross-ref NCBI Seq ID: 159542 Cross-ref NCBI Seq ID: 431337 Cross-ref GenBank Accession: M23438 Cross-ref GenBank Accession: L20792 Cross-ref HSSP P01008 Cross-ref PROSITE PS00284 Created Apr 1, 1990 Updated Feb 1, 1996 Citation REF [1] M.R. Kanost, S.V. Prasad & M.A. Wells (1989). Primary structure of a member of the serpin superfamily of proteinase inhibitors from an insect, Manduca sexta. J. Biol. Chem. 264, 965-972. MEDLINE identifier: 89093172 Citation REF [2] H. Jiang, Y. Wang & M.R. Kanost (1994). Mutually exclusive exon use and reactive center diversity in insect serpins. J. Biol. Chem. 269, 55-58. MEDLINE identifier: 94103270 Signal 134436: 1..16 Mature chain ALASERPIN. 134436: 17..392 (experimentally determined) glycosylation 134436: 85 site active site REACTIVE BOND. 134436: 359..360 Sequence 392 aa 1 mkiimcifgl aalamagetd lqkilresnd qftaqmfsev vkanpgqnvv 51 lsafsvlppl gqlalasvge shdellrala lpndnvtkdv fadlnrgvra 101 vkgvdlkmas kiyvakglel nddfaavsrd vfgsevqnvd fvksveaaga 151 inkwvedqtn nriknlvdpd aldettrsvl vnaiyfkgsw kdkfvkertm 201 drdfhvskdk tikvptmigk kdvryadvpe ldakmiemsy egdqasmiii 251 lpnqvdgita leqklkdpka lsraeerlyn teveiylpkf kietttdlke 301 vlsnmnikkl ftpgaarlen llktkeslyv daaiqkafie vneegaeaaa 351 anafgivpas lilypevhid rpfyfelkid gipmfngkvi ep
129293 --------------------------------------------------- Definition OVALBUMIN (PLAKALBUMIN) (ALLERGEN GAL D II). Protein Name: OVALBUMIN 129293: 1..386 SWISS-PROT Name: OVAL_CHICK, Accession: P01012 NCBI Seq ID: 129293 Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. BELONGS TO THE OV-SERPIN SUBFAMILY. Cross-ref NCBI Seq ID: 212505 Cross-ref NCBI Seq ID: 808974 Cross-ref NCBI Seq ID: 808969 Cross-ref NCBI Seq ID: 212503 Cross-ref GenBank Accession: J00895 Cross-ref EMBL Accession: V00438 Cross-ref EMBL Accession: V00383 Cross-ref GenBank Accession: M34352 Cross-ref PDB Molecule: 1OVA, Chain: (space) Cross-ref PROSITE PS00284 Created Jul 21, 1986 Updated Feb 1, 1996 Citation REF [1] S.L. Woo, W.G. Beattie, J.F. Catterall, A. Dugaiczyk, R. Staden, G.G. Brownlee & B.W. O'Malley (1981). Complete nucleotide sequence of the chicken chromosomal ovalbumin gene and its biological significance. Biochemistry 20, 6437-6446. MEDLINE identifier: 82069038 Citation REF [2] L. McReynolds, B.W. O'Malley, A.D. Nisbet, J.E. Fothergill, D. Givol, S. Fields, M. Robertson & G.G. Brownlee (1978). Sequence of chicken ovalbumin mRNA. Nature 273, 723-728. MEDLINE identifier: 78199842 Citation REF [3] J.F. Catterall, B.W. O'Malley, M.A. Robertson, R. Staden, Y. Tanaka & G.G. Brownlee (1978). Nucleotide sequence homology at 12 intron--exon junctions in the chick ovalbumin gene. Nature 275, 510-513. MEDLINE identifier: 79010682 Citation REF [4] R.D. Palmiter, J. Gagnon & K.A. Walsh (1978). Ovalbumin: a secreted protein without a transient hydrophobic leader sequence. Proc. Natl. Acad. Sci. U.S.A. 75, 94-98. MEDLINE identifier: 78116057 Citation REF [5] E.O. Thompson & W.K. Fisher (1978). A correction and extension of the acetylated amino terminal sequence of ovalbumin. Aust. J. Biol. Sci. 31, 443-446. MEDLINE identifier: 79186958 Citation REF [6] E.O. Thompson & W.K. Fisher (1978). Amino acid sequences containing half-cystine residues in ovalbumin. Aust. J. Biol. Sci. 31, 433-442. MEDLINE identifier: 79186957 Citation REF [7] P.E. Stein, A.G. Leslie, J.T. Finch, W.G. Turnell, P.J. McLaughlin & R.W. Carrell (1990). Crystal structure of ovalbumin as a model for the reactive centre of serpins. Nature 347, 99-102. MEDLINE identifier: 90370102 Citation REF [8] P.E. Stein, A.G. Leslie, J.T. Finch & R.W. Carrell (1991). Crystal structure of uncleaved ovalbumin at 1.95 A resolution. J. Mol. Biol. 221, 941-959. MEDLINE identifier: 92046044 Citation REF [9] H.T. Wright, H.X. Qian & R. Huber (1990). Crystal structure of plakalbumin, a proteolytically nicked form of ovalbumin. Its relationship to the structure of cleaved alpha-1- proteinase inhibitor. J. Mol. Biol. 213, 513-528. MEDLINE identifier: 90278960 acetylation (experimentally determined) 129293: 2 site phosphorylation(experimentally determined) 129293: 69 site disulfide bond (experimentally determined) 129293: 74 bond 121 glycosylation (experimentally determined) 129293: 293 site phosphorylation(experimentally determined) 129293: 345 site active site REACTIVE BOND HOMOLOG. 129293: 353..354 (experimentally determined) Variant N -> D (IN A MINOR COMPONENT). 129293: 312 (experimentally determined) Conflict A -> T (IN REF. 2). 129293: 188 (experimentally determined) Helical region (experimentally determined) 129293: 4..22 Hydrogen (experimentally determined) 129293: 24..25 bonded turn Beta-strand (experimentally determined) 129293: 28..30 region Helical region (experimentally determined) 129293: 32..43 Hydrogen (experimentally determined) 129293: 44..45 bonded turn Helical region (experimentally determined) 129293: 48..58 Hydrogen (experimentally determined) 129293: 59 bonded turn Hydrogen (experimentally determined) 129293: 61..62 bonded turn Hydrogen (experimentally determined) 129293: 64..65 bonded turn Helical region (experimentally determined) 129293: 68..71 Hydrogen (experimentally determined) 129293: 72..73 bonded turn Helical region (experimentally determined) 129293: 74..76 Hydrogen (experimentally determined) 129293: 78..81 bonded turn Helical region (experimentally determined) 129293: 82..92 Beta-strand (experimentally determined) 129293: 98..109 region Hydrogen (experimentally determined) 129293: 110..111 bonded turn Beta-strand (experimentally determined) 129293: 114 region Helical region (experimentally determined) 129293: 116..125 Beta-strand (experimentally determined) 129293: 130..133 region Hydrogen (experimentally determined) 129293: 136..138 bonded turn Helical region (experimentally determined) 129293: 139..153 Hydrogen (experimentally determined) 129293: 154..156 bonded turn Hydrogen (experimentally determined) 129293: 164..165 bonded turn Hydrogen (experimentally determined) 129293: 169..170 bonded turn Beta-strand (experimentally determined) 129293: 173..183 region Beta-strand (experimentally determined) 129293: 185..187 region Helical region (experimentally determined) 129293: 191..193 Beta-strand (experimentally determined) 129293: 195..202 region Hydrogen (experimentally determined) 129293: 203..204 bonded turn Beta-strand (experimentally determined) 129293: 205..223 region Helical region (experimentally determined) 129293: 224..226 Hydrogen (experimentally determined) 129293: 227 bonded turn Beta-strand (experimentally determined) 129293: 228..235 region Hydrogen (experimentally determined) 129293: 236..237 bonded turn Beta-strand (experimentally determined) 129293: 240..247 region Hydrogen (experimentally determined) 129293: 250..251 bonded turn Helical region (experimentally determined) 129293: 253..259 Helical region (experimentally determined) 129293: 262..268 Hydrogen (experimentally determined) 129293: 269 bonded turn Hydrogen (experimentally determined) 129293: 271..273 bonded turn Beta-strand (experimentally determined) 129293: 275..284 region Beta-strand (experimentally determined) 129293: 286..293 region Helical region (experimentally determined) 129293: 294..301 Hydrogen (experimentally determined) 129293: 302 bonded turn Helical region (experimentally determined) 129293: 305..307 Hydrogen (experimentally determined) 129293: 309..310 bonded turn Hydrogen (experimentally determined) 129293: 314..316 bonded turn Beta-strand (experimentally determined) 129293: 317 region Hydrogen (experimentally determined) 129293: 320..321 bonded turn Beta-strand (experimentally determined) 129293: 326..335 region Beta-strand (experimentally determined) 129293: 339..341 region Helical region (experimentally determined) 129293: 345..354 Beta-strand (experimentally determined) 129293: 358..360 region Beta-strand (experimentally determined) 129293: 365..371 region Hydrogen (experimentally determined) 129293: 372..374 bonded turn Beta-strand (experimentally determined) 129293: 377..383 region Sequence 386 aa 1 mgsigaasme fcfdvfkelk vhhanenify cpiaimsala mvylgakdst 51 rtqinkvvrf dklpgfgdsi eaqcgtsvnv hsslrdilnq itkpndvysf 101 slasrlyaee rypilpeylq cvkelyrggl epinfqtaad qarelinswv 151 esqtngiirn vlqpssvdsq tamvlvnaiv fkglwekafk dedtqampfr 201 vteqeskpvq mmyqiglfrv asmasekmki lelpfasgtm smlvllpdev 251 sgleqlesii nfekltewts snvmeerkik vylprmkmee kynltsvlma 301 mgitdvfsss anlsgissae slkisqavha ahaeineagr evvgsaeagv 351 daasvseefr adhpflfcik hiatnavlff grcvsp
123055 --------------------------------------------------- Definition HEPARIN COFACTOR II PRECURSOR (HC-II) (PROTEASE INHIBITOR LEUSERPIN 2) (HLS2). Protein Name: HEPARIN COFACTOR II 123055: 1..499 PRECURSOR SWISS-PROT Name: HEP2_HUMAN, Accession: P05546 NCBI Seq ID: 123055 Comment [FUNCTION] THROMBIN INHIBITOR ACTIVATED BY HEPARIN. ALSO INHIBITS CHYMOTRYPSIN. Comment [FUNCTION] THROMBIN INHIBITOR ACTIVATED BY THE GLYCOSAMINOGLYCANS, HEPARIN OR DERMATAN SULFATE. IN THE PRESENCE OF THE LATTER, HC-II BECOMES THE PREDOMINANT THROMBIN INHIBITOR IN PLACE OF ANTITHROMBIN III (AT). ALSO INHIBITS CHYMOTRYPSIN, BUT IN A GLYCOSAMINOGLYCAN-INDEPENDENT MANNER. Comment [FUNCTION] PEPTIDES AT THE N-TERMINAL OF HC-II HAVE CHEMOTACTIC ACTIVITY FOR BOTH MONOCYTES AND NEUTROPHILS. Comment [TISSUE SPECIFICITY] EXPRESSED PREDOMINANTLY IN LIVER. Comment [DOMAIN] THE N-TERMINAL ACIDIC REPEAT REGION MEDIATES, IN PART, THE GLYCOSAMINOGLYCAN-ACCELERATED THROMBIN INHIBITION. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Comment [DISEASE] DEFECTS IN HCF2 ARE ASSOCIATED WITH THROMBOSIS (THROMBOPHILIA). Cross-ref NCBI Seq ID: 183908 Cross-ref NCBI Seq ID: 1335104 Cross-ref NCBI Seq ID: 183910 Cross-ref NCBI Seq ID: 187236 Cross-ref GenBank Accession: M58600 Cross-ref EMBL Accession: X03498 Cross-ref GenBank Accession: M12849 Cross-ref GenBank Accession: M33660 Cross-ref HSSP P01008 Cross-ref MIM 142360 Cross-ref MIM 151580 Cross-ref PROSITE PS00284 Created Nov 1, 1988 Updated Feb 1, 1996 Citation REF [1] R. Herzog, S. Lutz, N. Blin, J.C. Marasa, M.A. Blinder & D.M. Tollefsen (1991). Complete nucleotide sequence of the gene for human heparin cofactor II and mapping to chromosomal band 22q11. Biochemistry 30, 1350-1357. MEDLINE identifier: 91120782 Citation REF [2] M.A. Blinder, J.C. Marasa, C.H. Reynolds, L.L. Deaven & D.M. Tollefsen (1988). Heparin cofactor II: cDNA sequence, chromosome localization, restriction fragment length polymorphism, and expression in Escherichia coli. Biochemistry 27, 752-759. MEDLINE identifier: 88163663 Citation REF [3] H. Ragg (1986). A new member of the plasma protease inhibitor gene family. Nucleic Acids Res. 14, 1073-1088. MEDLINE identifier: 86120356 Citation REF [4] R.C. Inhorn & D.M. Tollefsen (1986). Isolation and characterization of a partial cDNA clone for heparin cofactor II1. Biochem. Biophys. Res. Commun. 137, 431-436. MEDLINE identifier: 86242236 Citation REF [5] M.J. Griffith, C.M. Noyes, J.A. Tyndall & F.C. Church (1985). Structural evidence for leucine at the reactive site of heparin cofactor II. Biochemistry 24, 6777-6782. MEDLINE identifier: 86077723 Citation REF [6] H. Ragg & G. Preibisch (1988). Structure and expression of the gene coding for the human serpin hLS2. J. Biol. Chem. 263, 12129-12134. MEDLINE identifier: 88298901 Citation REF [7] F.C. Church, C.W. Pratt & M. Hoffman (1991). Leukocyte chemoattractant peptides from the serpin heparin cofactor II. J. Biol. Chem. 266, 704-709. MEDLINE identifier: 91093260 Citation REF [8] V.M. Van Deerlin & D.M. Tollefsen (1991). The N-terminal acidic domain of heparin cofactor II mediates the inhibition of alpha-thrombin in the presence of glycosaminoglycans. J. Biol. Chem. 266, 20223-20231. MEDLINE identifier: 92041850 Citation REF [9] M.A. Blinder & D.M. Tollefsen (1990). Site-directed mutagenesis of arginine 103 and lysine 185 in the proposed glycosaminoglycan-binding site of heparin cofactor II. J. Biol. Chem. 265, 286-291. MEDLINE identifier: 90094412 Citation REF [10] M.A. Blinder, T.R. Andersson, U. Abildgaard & D.M. Tollefsen (1989). Heparin cofactor IIOslo. Mutation of Arg-189 to His decreases the affinity for dermatan sulfate. J. Biol. Chem. 264, 5128-5133. MEDLINE identifier: 89174798 Signal (experimentally determined) 123055: 1..19 Mature chain HEPARIN COFACTOR II. 123055: 20..499 (experimentally determined) Domain CHEMOTACTIC ACTIVITY. 123055: 68..79 (experimentally determined) Domain 2 X 11 AA APPROXIMATE REPEATS, 123055: 73..97 ASP/GLU- RICH (ACIDIC) (HIRUDIN- LIKE). (experimentally determined) Repetitive 1. 123055: 73..83 region (experimentally determined) Repetitive 2. 123055: 87..97 region (experimentally determined) Domain GLYCOSAMINOGLYCAN-BINDING SITE. 123055: 192..212 (experimentally determined) modified site SULFATION. 123055: 79 modified site SULFATION. 123055: 92 glycosylation 123055: 49 site glycosylation 123055: 188 site glycosylation 123055: 387 site active site REACTIVE BOND. 123055: 463..464 Variant R -> H (IN OSLO; HCF2 DEFICIENCY; 123055: 208 DECREASED AFFINITY FOR DERMATAN SULFATE). (experimentally determined) mutagenized R->L: NORMAL THROMBIN INHIBITION 123055: 122 site AND GLYCOSAMINOGLYCAN AFFINITY. (experimentally determined) mutagenized R->Q: GREATLY REDUCED THROMBIN 123055: 122 site INHIBITION. NORMAL GLYCOSAMINOGLYCAN AFFINITY. (experimentally determined) mutagenized R->W: GREATLY REDUCED THROMBIN 123055: 122 site INHIBITION. NORMAL GLYCOSAMINOGLYCAN AFFINITY. (experimentally determined) mutagenized K->M: REDUCED HEPARIN- AND NO 123055: 204 site DERMATAN SULFATE-ACTIVATED INHIBITION. (experimentally determined) mutagenized K->N: REDUCED HEPARIN- AND NO 123055: 204 site DERMATAN SULFATE-ACTIVATED INHIBITION. (experimentally determined) mutagenized K->T: REDUCED HEPARIN- AND NO 123055: 204 site DERMATAN SULFATE-ACTIVATED INHIBITION. (experimentally determined) Conflict MISSING (IN REF. 5). 123055: 49 (experimentally determined) Conflict K -> R (IN REF. 2). 123055: 237 (experimentally determined) Conflict R -> P (IN REF. 5). 123055: 483 (experimentally determined) Conflict C -> T (IN REF. 5). 123055: 486 (experimentally determined) Conflict S -> Q (IN REF. 5). 123055: 499 (experimentally determined) Gene Locus: HCF2 123055: 1..499 Sequence 499 aa 1 mkhslnalli fliitsawgg skgpldqlek ggetaqsadp qweqlnnknl 51 smpllpadfh kentvtndwi pegeedddyl dlekifsedd dyidivdsls 101 vsptdsdvsa gnilqlfhgk sriqrlniln akfafnlyrv lkdqvntfdn 151 ifiapvgist amgmislglk getheqvhsi lhfkdfvnas skyeittihn 201 lfrklthrlf rrnfgytlrs vndlyiqkqf pilldfktkv reyyfaeaqi 251 adfsdpafis ktnnhimklt kglikdalen idpatqmmil nciyfkgswv 301 nkfpvemthn hnfrlnerev vkvsmmqtkg nflaandqel dcdilqleyv 351 ggismlivvp hkmsgmktle aqltprvver wqksmtnrtr evllpkfkle 401 knynlveslk lmgirmlfdk ngnmagisdq riaidlfkhq gtitvneegt 451 qattvttvgf mplstqvrft vdrpflfliy ehrtscllfm grvanpsrs
121111 --------------------------------------------------- Definition GLIA DERIVED NEXIN PRECURSOR (GDN) (PROTEASE NEXIN I) (PN-1). Protein Name: GLIA DERIVED NEXIN PRECURSOR121111: 1..397 SWISS-PROT Name: GDN_RAT, Accession: P07092 NCBI Seq ID: 121111 Comment [FUNCTION] THIS GLYCOPROTEIN PROMOTES NEURITE EXTENSION AND IS A SERINE PROTEASE INHIBITOR WITH ACTIVITY TOWARD THROMBIN, TRYPSIN, AND UROKINASE. BINDS HEPARIN. Comment [SUBCELLULAR LOCATION] EXTRACELLULAR. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 204284 Cross-ref GenBank Accession: M17784 Cross-ref HSSP P01008 Cross-ref PROSITE PS00284 Created Apr 1, 1988 Updated Feb 1, 1996 Citation REF [1] J. Sommer, S.M. Gloor, G.F. Rovelli, J. Hofsteenge, H. Nick, R. Meier & D. Monard (1987). cDNA sequence coding for a rat glia-derived nexin and its homology to members of the serpin superfamily. Biochemistry 26, 6407-6410. MEDLINE identifier: 88107544 Signal 121111: 1..19 Mature chain GLIA DERIVED NEXIN. 121111: 20..397 (experimentally determined) glycosylation 121111: 159 site active site REACTIVE BOND. 121111: 364..365 Gene Locus: PI7 121111: 1..397 Sequence 397 aa 1 mnwhfpffil ttvtlssvys qlnslsleel gsdtgiqvfn qiiksqphen 51 vvisphgias ilgmlqlgad grtkkqlstv mrynvngvgk vlkkinkaiv 101 skknkdivtv anavfvrngf kvevpfaarn kevfqcevqs vnfqdpasac 151 dainfwvkne trgmidnlls pnlidsaltk lvlvnavyfk glwksrfqpe 201 ntkkrtfvag dgksyqvpml aqlsvfrsgs tktpnglwyn fielpyhges 251 ismlialpte sstplsaiip histktinsw mntmvpkrmq lvlpkftala 301 qtdlkeplka lgitemfeps kanfakitrs eslhvshilq kakievsedg 351 tkaavvttai liarssppwf ivdrpflfci rhnptgailf lgqvnkp
115852 --------------------------------------------------- Definition CORTICOSTEROID-BINDING GLOBULIN (CBG) (TRANSCORTIN). Protein Name: CORTICOSTEROID-BINDING 115852: 1..383 GLOBULIN SWISS-PROT Name: CBG_RABIT, Accession: P23775 NCBI Seq ID: 115852 Comment [FUNCTION] MAJOR TRANSPORT PROTEIN FOR GLUCOCORTICOIDS AND PROGESTINS IN THE BLOOD OF ALMOST ALL VERTEBRATE SPECIES. Comment [SUBCELLULAR LOCATION] EXTRACELLULAR. Comment [TISSUE SPECIFICITY] PRODUCED AND SECRETED BY HEPATOCYTES, BUT HAS ALSO BEEN IDENTIFIED IN A NUMBER OF GLYCOCORTICOID RESPONSIVE CELLS (IT IS FOUND IN MATERNAL LUNG, SPLEEN, AND OVARY AND FETAL KIDNEY). Comment [SIMILARITY] WITH SERPIN SERINE PROTEASE INHIBITORS. Cross-ref HSSP P01008 Cross-ref PROSITE PS00284 Created Nov 1, 1991 Updated Feb 1, 1996 Citation REF [1] G.E. Seralini, C.L. Smith & G.L. Hammond (1990). Rabbit corticosteroid-binding globulin: primary structure and biosynthesis during pregnancy. Mol. Endocrinol. 4, 1166-1172. MEDLINE identifier: 91155949 glycosylation 115852: 74 site glycosylation 115852: 154 site glycosylation 115852: 238 site glycosylation 115852: 308 site other site CONSERVED CYSTEINE WITHIN STEROID 115852: 228 BINDING DOMAIN. Gene Locus: CBG 115852: 1..383 Sequence 383 aa 1 adppggdist rspprglapa nvdfafslyr qlvssapdrn icispvsvsm 51 alamlslgas ghtrtqllqg lgfnltempe aeihqgfqyl hhllgesdts 101 lemtmgnalf ldhslelles fsadirryye sealatdfqd wpracrqine 151 yienktqgki adlflglenp aililvnyif fkgtwahpfd pqsteeksfy 201 vddtttvmvp mmfqsstvky lhdpvlpcrl vqldyvgngt affilpdkgk 251 vdtviaalsr dtiqrwsksl tyrlvhlyip kasisgayel rgalaamgia 301 dlftnqanfs sisqegplkv skvlhkavlq ldehggveva atggplqlvs 351 epltlnfnrp flilifddft wsslflgkvv ipa
113936 --------------------------------------------------- Definition ANTITHROMBIN-III PRECURSOR (ATIII). Protein Name: ANTITHROMBIN-III PRECURSOR 113936: 1..464 SWISS-PROT Name: ANT3_HUMAN, Accession: P01008 NCBI Seq ID: 113936 Comment [FUNCTION] MOST IMPORTANT SERINE PROTEASE INHIBITOR IN PLASMA THAT REGULATES THE BLOOD COAGULATION CASCADE. AT-III INHIBITS THROMBIN AS WELL AS FACTORS IXA, XA AND XIA. ITS INHIBITORY ACTIVITY IS GREATLY ENHANCED IN THE PRESENCE OF HEPARIN. Comment [SUBCELLULAR LOCATION] EXTRACELLULAR. Comment [TISSUE SPECIFICITY] PLASMA. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Comment [DISEASE] INDIVIDUALS WITH A DEFICIENCY IN ATIII ARE PRONE TO SERIOUS SPONTANEOUS THROMBOSIS (THROMBOPHILIA). AT DEFICIENCY IS CLASSIFIED INTO 4 TYPES: TYPE I: CHARACTERIZED BY A 50% DECREASE IN ANTIGENIC AND FUNCTIONAL LEVELS. TYPE II: HAS DEFECTS AFFECTING THE THROMBIN-BINDING DOMAIN. TYPE III: ALTERATION OF THE HEPARIN-BINDING DOMAIN. PLASMA AT ANTIGEN LEVELS ARE NORMAL IN TYPE II AND III. TYPE IV: CONSISTS OF MISCELLANEOUS GROUP OF UNCLASSIFIABLE MUTATIONS. Comment [DISEASE] ATIII BASEL, TOURS/ALGER/AMIENS/TOYAMA, ROUEN-1, -2, -3 AND -4 HAVE DECREASED (OR LACK) HEPARIN-BINDING PROPERTIES. Comment [DISEASE] ATIII HAMILTON, GLASCOW/SHEFFIELD/CHICAGO, NORTHWICK- PARK /MILANO-1, PESCARA, DENVER/MILANO-2, AND UTAH ARE DEPRIVED OF INHIBITORY ACTIVITY. Cross-ref NCBI Seq ID: 179161 Cross-ref NCBI Seq ID: 179130 Cross-ref NCBI Seq ID: 28907 Cross-ref GenBank Accession: M21642 Cross-ref GenBank Accession: L00190 Cross-ref GenBank Accession: L00185 Cross-ref EMBL Accession: X68793 Cross-ref PDB Molecule: 1ANT, Chain: (space) Cross-ref PDB Molecule: 1ATH, Chain: (space) Cross-ref SWISS-2DPAGE P01008 Cross-ref MIM 107300 Cross-ref PROSITE PS00284 Created Jul 21, 1986 Updated Feb 1, 1996 Citation REF [1] S.C. Bock, K.L. Wion, G.A. Vehar & R.M. Lawn (1982). Cloning and expression of the cDNA for human antithrombin III. Nucleic Acids Res. 10, 8113-8125. MEDLINE identifier: 83143280 Citation REF [2] T. Chandra, R. Stackhouse, V.J. Kidd & S.L. Woo (1983). Isolation and sequence characterization of a cDNA clone of human antithrombin III. Proc. Natl. Acad. Sci. U.S.A. 80, 1845-1848. MEDLINE identifier: 83169777 Citation REF [3] R.J. Olds, D.A. Lane, V. Chowdhury, V. De Stefano, G. Leone & S.L. Thein (1993). Complete nucleotide sequence of the antithrombin gene: evidence for homologous recombination causing thrombophilia. Biochemistry 32, 4216-4224. MEDLINE identifier: 93237227 Citation REF [4] E.V. Prochownik, A.F. Markham & S.H. Orkin (1983). Isolation of a cDNA clone for human antithrombin III. J. Biol. Chem. 258, 8389-8394. MEDLINE identifier: 83238456 Citation REF [5] T.E. PETERSEN, G. DUDEK-WOJCIECHOWSKA, L. SOTTRUP-JENSEN & S. MAGNUSSON (1979) THE PHYSIOLOGICAL INHIBITORS OF BLOOD COAGULATION AND FIBRINOLYSIS; D. COLLEN, B. WIMAN & M. VERSTRAETE; ELSEVIER/NORTH HOLLAND BIOMEDICAL PRESS, AMSTERDAM; 3-54. Citation REF [6] I. Bjork, A. Danielsson, J.W. Fenton & Jornvall (1981). The site in human antithrombin for functional proteolytic cleavage by human thrombin. FEBS Lett. 126, 257-260. MEDLINE identifier: 81212814 Citation REF [7] M.N. Blackburn, R.L. Smith, J. Carson & C.C. Sibley (1984). The heparin-binding site of antithrombin III. Identification of a critical tryptophan in the amino acid sequence. J. Biol. Chem. 259, 939-941. MEDLINE identifier: 84111578 Citation REF [8] R.C. Austin, R.A. Rachubinski & M.A. Blajchman (1991). Site- directed mutagenesis of alanine-382 of human antithrombin III. FEBS Lett. 280, 254-258. MEDLINE identifier: 91192143 Citation REF [9] R.W. Carrell, P.E. Stein, G. Fermi & M.R. Wardell (1994). Biological implications of a 3 A structure of dimeric antithrombin. Structure 2, 257-270. MEDLINE identifier: 94373498 Citation REF [10] H.A. Schreuder, B. de Boer, R. Dijkema, J. Mulders, H.J. Theunissen, P.D. Grootenhuis & W.G. Hol (1994). The intact and cleaved human antithrombin III complex as a model for serpin-proteinase interactions. Nat. Struct. Biol. 1, 48-54. MEDLINE identifier: 95384753 Citation REF [11] L. Mourey, J.P. Samama, M. Delarue, J. Choay, J.C. Lormeau, M. Petitou & D. Moras (1990). Antithrombin III: structural and functional aspects. Biochimie 72, 599-608. MEDLINE identifier: 91129302 Citation REF [12] D.A. Lane, R.J. Olds, M. Boisclair, V. Chowdhury, S.L. Thein, D.N. Cooper, M. Blajchman, D. Perry, J. Emmerich & M. Aiach (1993). Antithrombin III mutation database: first update. For the Thrombin and its Inhibitors Subcommittee of the Scientific and Standardization Committee of the International Society on Thrombosis and Haemostasis. Thromb. Haemost. 70, 361-369. MEDLINE identifier: 94054329 Citation REF [13] P.E. Stein & R.W. Carrell (1995). What do dysfunctional serpins tell us about molecular mobility and disease?. Nat. Struct. Biol. 2, 96-113. MEDLINE identifier: 95269065 Citation REF [14] D.J. Perry & R.W. Carrell (1996). Molecular genetics of human antithrombin deficiency. Hum. Mutat. 7, 7-22. MEDLINE identifier: 96263733 Citation REF [15] S.C. Bock, J.A. Marrinan & E. Radziejewska (1988). Antithrombin III Utah: proline-407 to leucine mutation in a highly conserved region near the inhibitor reactive site. Biochemistry 27, 6171-6178. MEDLINE identifier: 89050967 Citation REF [16] T. Koide, S. Odani, K. Takahashi, T. Ono & N. Sakuragawa (1984). Antithrombin III Toyama: replacement of arginine-47 by cysteine in hereditary abnormal antithrombin III that lacks heparin-binding ability. Proc. Natl. Acad. Sci. U.S.A. 81, 289-293. MEDLINE identifier: 84119472 Citation REF [17] J.Y. Chang & T.H. Tran (1986). Antithrombin III Basel. Identification of a Pro-Leu substitution in a hereditary abnormal antithrombin with impaired heparin cofactor activity. J. Biol. Chem. 261, 1174-1176. MEDLINE identifier: 86111754 Citation REF [18] A.W. Stephens, B.S. Thalley & C.H. Hirs (1987). Antithrombin- III Denver, a reactive site variant. J. Biol. Chem. 262, 1044- 1048. MEDLINE identifier: 87109210 Citation REF [19] R. Devraj-Kizuk, D.H. Chui, E.V. Prochownik, C.J. Carter, F.A. Ofosu & M.A. Blajchman (1988). Antithrombin-III-Hamilton: a gene with a point mutation (guanine to adenine) in codon 382 causing impaired serine protease reactivity. Blood 72, 1518- 1523. MEDLINE identifier: 89027076 Citation REF [20] H. Erdjument, D.A. Lane, M. Panico, V. Di Marzo & H.R. Morris (1988). Single amino acid substitutions in the reactive site of antithrombin leading to thrombosis. Congenital substitution of arginine 393 to cysteine in antithrombin Northwick Park and to histidine in antithrombin Glasgow. J. Biol. Chem. 263, 5589-5593. MEDLINE identifier: 88186869 Citation REF [21] H. Erdjument, D.A. Lane, M. Panico, V. Di Marzo, H.R. Morris, K. Bauer & R.D. Rosenberg (1989). Antithrombin Chicago, amino acid substitution of arginine 393 to histidine. Thromb. Res. 54, 613-619. MEDLINE identifier: 89388698 Citation REF [22] J.Y. Borg, S.O. Brennan, R.W. Carrell, P. George, D.J. Perry & J. Shaw (1990). Antithrombin Rouen-IV 24 Arg----Cys. The amino-terminal contribution to heparin binding. FEBS Lett. 266, 163-166. MEDLINE identifier: 90306344 Citation REF [23] M. Daly, D. Bruce, D.J. Perry, J. Price, P.L. Harper, A. O'Meara & R.W. Carrell (1990). Antithrombin Dublin (-3 Val---- Glu): an N-terminal variant which has an aberrant signal peptidase cleavage site. FEBS Lett. 273, 87-90. MEDLINE identifier: 91032211 Citation REF [24] S. Gandrille, M. Aiach, D.A. Lane, D. Vidaud, P. Molho- Sabatier, R. Caso, P. de Moerloose, J.N. Fiessinger & E. Clauser (1990). Important role of arginine 129 in heparin- binding site of antithrombin III. Identification of a novel mutation arginine 129 to glutamine. J. Biol. Chem. 265, 18997- 19001. MEDLINE identifier: 91035423 Citation REF [25] D.J. Perry, M. Daly, P.L. Harper, R.C. Tait, J. Price, I.D. Walker & R.W. Carrell (1991). Antithrombin Cambridge II, 384 Ala to Ser. Further evidence of the role of the reactive centre loop in the inhibitory function of the serpins. FEBS Lett. 285, 248-250. MEDLINE identifier: 91309742 Citation REF [26] R.J. Olds, D.A. Lane, M. Boisclair, G. Sas, S.C. Bock & S.L. Thein (1992). Antithrombin Budapest 3. An antithrombin variant with reduced heparin affinity resulting from the substitution L99F. FEBS Lett. 300, 241-246. MEDLINE identifier: 92209716 Citation REF [27] M.A. Blajchman, F. Fernandez-Rachubinski, W.P. Sheffield, R.C. Austin & S. Schulman (1992). Antithrombin-III-Stockholm: a codon 392 (Gly----Asp) mutation with normal heparin binding and impaired serine protease reactivity. Blood 79, 1428-1434. MEDLINE identifier: 92190477 Citation REF [28] K. Okajima, H. Abe, S. Maeda, M. Motomura, M. Tsujihata, S. Nagataki, H. Okabe & K. Takatsuki (1993). Antithrombin III Nagasaki (Ser116-Pro): a heterozygous variant with defective heparin binding associated with thrombosis. Blood 81, 1300- 1305. MEDLINE identifier: 93184324 Citation REF [29] R.J. Olds, D.A. Lane, C.H. Beresford, U. Abildgaard, P.M. Hughes & S.L. Thein (1993). A recurrent deletion in the antithrombin gene, AT106-108(-6 bp), identified by DNA heteroduplex detection. Genomics 16, 298-299. MEDLINE identifier: 93252405 Citation REF [30] D.S. Millar, A.I. Wacey, J. Ribando, E. Melissari, B. Laursen, P. Woods, V.V. Kakkar & D.N. Cooper (1994). Three novel missense mutations in the antithrombin III (AT3) gene causing recurrent venous thrombosis. Hum. Genet. 94, 509-512. MEDLINE identifier: 95048284 Citation REF [31] K. Jochmans, W. Lissens, R. Vervoort, S. Peeters, M. De Waele & I. Liebaers (1994). Antithrombin-Gly 424 Arg: a novel point mutation responsible for type 1 antithrombin deficiency and neonatal thrombosis. Blood 83, 146-151. MEDLINE identifier: 94100527 Citation REF [32] D.S. Millar, A.I. Wacey, J. Ribando, E. Melissari, B. Laursen, P. Woods, V.V. Kakkar & D.N. Cooper (1994). Three novel missense mutations in the antithrombin III (AT3) gene causing recurrent venous thrombosis. Hum. Genet. 94, 509-512. MEDLINE identifier: 95048284 Citation REF [33] D. Bruce, D.J. Perry, J.Y. Borg, R.W. Carrell & M.R. Wardell (1994). Thromboembolic disease due to thermolabile conformational changes of antithrombin Rouen-VI (187 Asn-- >Asp). J. Clin. Invest. 94, 2265-2274. MEDLINE identifier: 95081409 Citation REF [34] V. CHOWDHURY, R.J. OLDS, D.A. LANE, B. MILLE, I. PABINGER & S.L. THEIN (1994)NOUV. REV. FR. HEMATOL. 86, 268-268. Citation REF [35] J. Emmerich, G. Chadeuf, M. Alhenc-Gelas, M. Gouault-Heilman, P. Toulon, J.N. Fiessinger & M. Aiach (1994). Molecular basis of antithrombin type I deficiency: the first large in-frame deletion and two novel mutations in exon 6. Thromb. Haemost. 72, 534-539. MEDLINE identifier: 95184178 Citation REF [36] K. Okajima, H. Abe, M. Wagatsuma, H. Okabe & K. Takatsuki (1995). Antithrombin III Kumamoto II; a single mutation at Arg393-His increased the affinity of antithrombin III for heparin. Am. J. Hematol. 48, 12-18. MEDLINE identifier: 95133579 Signal (experimentally determined) 113936: 1..32 Mature chain ANTITHROMBIN-III. 113936: 33..464 (experimentally determined) binding site HEPARIN. 113936: 81 (experimentally determined) binding site HEPARIN. 113936: 161 (experimentally determined) binding site HEPARIN. 113936: 177 (experimentally determined) active site REACTIVE BOND. 113936: 425..426 (experimentally determined) disulfide bond (experimentally determined) 113936: 40 bond 160 disulfide bond (experimentally determined) 113936: 53 bond 127 disulfide bond (experimentally determined) 113936: 279 bond 462 glycosylation (experimentally determined) 113936: 128 site glycosylation (experimentally determined) 113936: 167 site glycosylation (experimentally determined) 113936: 187 site glycosylation (experimentally determined) 113936: 224 site Variant V -> E (IN DUBLIN). 113936: 30 (experimentally determined) Variant I -> N (IN ROUEN-3; TYPE-II). 113936: 39 (experimentally determined) Variant M -> T (IN WHITECHAPEL; TYPE-II). 113936: 52 (experimentally determined) Variant R -> C (IN ROUEN-4; TYPE-II). 113936: 56 (experimentally determined) Variant P -> L (IN 113936: 73 BASEL/FRANCONVILLE/CLICHY-1/ CLICHY-2/DUBLIN-2; TYPE-II). (experimentally determined) Variant R -> C (IN 113936: 79 TOURS/ALGER/AMIENS/TOYAMA/ PARIS- 1/PARIS-2/PADUA-2/BARCELONA-2/ KUMAMOTO; LACKS HEPARIN-BINDING ABILITY). (experimentally determined) Variant R -> H (IN ROUEN-1/PADUA-1/BLIGNY/ 113936: 79 BUDAPEST-2; TYPE-II). (experimentally determined) Variant R -> S (IN ROUEN-2; TYPE-II). 113936: 79 (experimentally determined) Variant MISSING (IN TYPE-I). 113936: 87 (experimentally determined) Variant R -> C (IN TYPE-I). 113936: 89 (experimentally determined) Variant F -> L (IN BUDAPEST-6; TYPE-I). 113936: 90 (experimentally determined) Variant MISSING (IN TYPE-I). 113936: 108..109 (experimentally determined) Variant P -> T (IN TYPE-I). 113936: 112 (experimentally determined) Variant L -> F (IN BUDAPEST-3/BUDAPEST-7; 113936: 131 TYPE-II). (experimentally determined) Variant L -> V (IN SOUTHPORT). 113936: 131 (experimentally determined) Variant Q -> K (IN TYPE I). 113936: 133 (experimentally determined) Variant MISSING (IN TYPE-I). 113936: 138..139 (experimentally determined) Variant S -> P (IN NAGASAKI; DEFECTIVE 113936: 148 HEPARIN BINDING ASSOCIATED WITH THROMBOSIS). (experimentally determined) Variant Q -> P (IN VIENNA). 113936: 150 (experimentally determined) Variant H -> Y (IN TYPE-I). 113936: 152 (experimentally determined) Variant MISSING (IN TYPE-I). 113936: 153 (experimentally determined) Variant L -> P (IN TYPE-I). 113936: 158 (experimentally determined) Variant R -> Q (IN GENEVA; TYPE-II). 113936: 161 (experimentally determined) Variant Y -> C (IN POPULATION OF 113936: 190 SCANDINAVIAN ORIGIN). (experimentally determined) Variant Y -> C (IN WHITECHAPEL; TYPE-I AND 113936: 198 -II). (experimentally determined) Variant S -> Y (IN TYPE-I). 113936: 214 (experimentally determined) Variant N -> K (IN GLASGOW-3; TYPE-II). 113936: 219 (experimentally determined) Variant N -> D (IN ROUEN-6; TYPE-II; 113936: 219 INCREASES AFFINITY FOR HEPARIN). (experimentally determined) Variant E -> K (IN TRURO; TYPE-II; 113936: 269 INCREASES AFFINITY FOR HEPARIN). (experimentally determined) Variant MISSING (IN TYPE-I). 113936: 273..307 (experimentally determined) Variant M -> I (IN TYPE-II). 113936: 283 (experimentally determined) Variant L -> P (IN TYPE-I). 113936: 302 (experimentally determined) Variant I -> N (IN HASLAR/WHITECHAPEL; 113936: 316 TYPE-II). (experimentally determined) Variant E -> K (IN TYPE-II). 113936: 334 (experimentally determined) Variant MISSING (IN TYPE-I). 113936: 344 (experimentally determined) Variant S -> P (IN TYPE-I). 113936: 381 (experimentally determined) Variant R -> Q. 113936: 391 (experimentally determined) Variant A -> T (IN HAMILTON/GLASGOW-2; 113936: 414 TYPE-II). (experimentally determined) Variant A -> P (IN 113936: 416 CHARLEVILLE/SUDBURY/VICENZA/ CAMBRIDGE-1; TYPE-II). (experimentally determined) Variant A -> S (IN CAMBRIDGE-2; TYPE-II). 113936: 416 (experimentally determined) Variant A -> V (IN TYPE-I). 113936: 419 (experimentally determined) Variant G -> D (IN STOCKHOLM; TYPE-II). 113936: 424 (experimentally determined) Variant R -> H (IN 113936: 425 GLASCOW/SHEFFIELD/CHICAGO/ AVRANCHES/KUMAMOTO-2; TYPE-II; INCREASES AFFINITY FOR HEPARIN). (experimentally determined) Variant R -> C (IN NORTHWICK-PARK/MILANO- 113936: 425 1/ FRANKFURT-1; TYPE-II). (experimentally determined) Variant R -> P (IN PESCARA; TYPE-II). 113936: 425 (experimentally determined) Variant S -> L (IN DENVER/MILANO-2; TYPE- 113936: 426 II). (experimentally determined) Variant F -> C (IN ROSNY; TYPE-II). 113936: 434 (experimentally determined) Variant F -> S (IN TORINO; TYPE-II). 113936: 434 (experimentally determined) Variant F -> L (IN MAISON LAFFITE; TYPE- 113936: 434 II). (experimentally determined) Variant A -> T (IN OSLO/PARIS-3; TYPE-II). 113936: 436 (experimentally determined) Variant N -> K (IN LA ROCHELLE; TYPE-II). 113936: 437 (experimentally determined) Variant R -> M (IN KYOTO; TYPE-II). 113936: 438 (experimentally determined) Variant P -> L (IN UTAH; TYPE-II). 113936: 439 (experimentally determined) Variant P -> T (IN BUDAPEST-5; TYPE-II). 113936: 439 (experimentally determined) Variant I -> Y (IN TYPE-I). 113936: 453 (experimentally determined) Variant G -> R (IN TYPE-I). 113936: 456 (experimentally determined) Variant R -> T (IN TYPE-II). 113936: 457 (experimentally determined) Variant MISSING (IN TYPE-I). 113936: 459..461 (experimentally determined) Variant A -> D (IN TYPE-I). 113936: 459 (experimentally determined) Variant P -> L (IN BUDAPEST; TYPE-II). 113936: 461 (experimentally determined) Variant C -> F (IN TYPE-I). 113936: 462 (experimentally determined) Conflict EQ -> QE (IN REF. 5). 113936: 69..70 (experimentally determined) Conflict H -> R (IN REF. 4). 113936: 97 (experimentally determined) Conflict MISSING (IN REF. 5). 113936: 247..249 (experimentally determined) Gene Locus: AT3 113936: 1..464 Sequence 464 aa 1 mysnvigtvt sgkrkvylls llligfwdcv tchgspvdic takprdipmn 51 pmciyrspek katedegseq kipeatnrrv welskansrf attfyqhlad 101 skndndnifl splsistafa mtklgacndt lqqlmevfkf dtisektsdq 151 ihfffaklnc rlyrkankss klvsanrlfg dksltfnety qdiselvyga 201 klqpldfken aeqsraaink wvsnktegri tdvipseain eltvlvlvnt 251 iyfkglwksk fspentrkel fykadgescs asmmyqegkf ryrrvaegtq 301 vlelpfkgdd itmvlilpkp ekslakveke ltpevlqewl deleemmlvv 351 hmprfriedg fslkeqlqdm glvdlfspek sklpgivaeg rddlyvsdaf 401 hkaflevnee gseaaastav viagrslnpn rvtfkanrpf lvfirevpln 451 tiifmgrvan pcvk
113879 --------------------------------------------------- Definition ANGIOTENSINOGEN. Protein Name: ANGIOTENSINOGEN 113879: 1..14 *: Partial SWISS-PROT Name: ANGT_HORSE, Accession: P01016 NCBI Seq ID: 113879 Comment [FUNCTION] IN RESPONSE TO LOWERED BLOOD PRESSURE, THE ENZYME RENIN CLEAVES ANGIOTENSIN I, FROM ANGIOTENSINOGEN. ACE (ANGIOTENSIN CONVERTING ENZYME) THEN REMOVES A DIPEPTIDE TO YIELD THE PHYSIOLOGICALLY ACTIVE PEPTIDE ANGIOTENSIN II, THE MOST POTENT PRESSOR SUBSTANCE KNOWN, WHICH HELPS REGULATE VOLUME AND MINERAL BALANCE OF BODY FLUIDS. Comment [TISSUE SPECIFICITY] MADE IN THE LIVER & SECRETED IN THE PLASMA. Comment [SIMILARITY] WITH SERPIN SERINE PROTEASE INHIBITORS. Cross-ref PROSITE PS00284 Created Jul 21, 1986 Updated Feb 1, 1996 Citation REF [1] L.T. JR. SKEGGS, J.R. KAHN, K. LENTZ & N.P. SHUMWAY (1957)J. EXP. MED. 106, 439-453. Processed ANGIOTENSIN I. 113879: 1..10 active peptide (experimentally determined) Processed ANGIOTENSIN II. 113879: 1..8 active peptide (experimentally determined) Gene Locus: AGT 113879: 1..14 Sequence 14 aa 1 drvyihpfhl lvys
1168082 ---------------------------------------------------
Definition SPI-3=serpin-like cell-cell fusion inhibitor glycoprotein {C-
terminal} [cowpox virus CPV, Brighton Red, Peptide Partial, 58
aa]
Protein Name: SPI-3 1168082: 316..373
Description: serpin-like cell-
cell fusion inhibitor glycoprotein.
*: Partial
NCBI Journal Scan Seq ID: 170987
NCBI Seq ID: 1168082
Updated Jan 27, 1996
Created Jan 27, 1996
Citation MEDLINE identifier: 95395930
Figure Fig. 6B, "CPV SPI-3"
Numbered from 316
Citation Turner,P.C. & Moyer,R.W. (1995). Orthopoxvirus fusion
inhibitor glycoprotein SPI-3 (open reading frame K2L) contains
motifs characteristic of serine proteinase inhibitors that are
not required for control of cell fusion. J. Virol. 69, 5978-
87. MEDLINE identifier: 95395930
Sequence 58 aa
316 qnakidvdeq gtvaeastim vatarsspeq lefntpfvfi irhditgfil
366 fmgkvesp
1253607 --------------------------------------------------- Definition Sequence 8 from patent US 5470970 PATENT US 5470970 [8] NCBI Seq ID: 1253607 Updated Nov 30, 1995 Citation Patent: US 5470970-A Nov 28, 1995 Ruth Sager, Anthony Anisowicz & Zhiqiang Zou. Maspin, a serpin with tumor suppresing activity. Sequence 375 aa 1 meqlstanth favdlfraln esdptgnifi splsissala miflgtrgnt 51 aaqvskalyf dtvedihsrf qslnadinkp gapyilklan rlygektynf 101 ladflastqk mygaelasvd fqqapedark einewvkgqt egkipellvk 151 gmvdnmtklv lvnaiyfkgn wqekfmkeat rdapfrlnkk dtktvkmmyq 201 kkkfpynyie dlkcrvlelp yqgkelsmii llpddiedes tglekiekql 251 tleklrewtk penlylaevn vhlprfklee sydltshlar lgvqdlfnrg 301 kadlsgmsga rdlfvskiih ksfvdlneeg teaaaatagt imlamlmpee 351 nfnadhpfif firhnpsani lflgr
1253606 --------------------------------------------------- Definition Sequence 7 from patent US 5470970 PATENT US 5470970 [7] NCBI Seq ID: 1253606 Updated Nov 30, 1995 Citation Patent: US 5470970-A Nov 28, 1995 Ruth Sager, Anthony Anisowicz & Zhiqiang Zou. Maspin, a serpin with tumor suppresing activity. Sequence 405 aa 1 medlcvantl falnlfkhla kasptqnlfl spwsisstma mvymgsrgst 51 edqmakvlqf nevganavtp mtpenftscg fmqqiqkgsy pdailqaqaa 101 dkihssfrsl ssainastgd yllesvnklf geksasfree yirlcqkyys 151 sepqavdfle caeearkkin swvktqtkgk ipnllpegsv dgdtrmvlvn 201 avyfkgkwkt pfekklngly pfrvnsaqrt pvqmmylrek lnigyiedlk 251 aqilelpyag dvsmflllpd eiadvstgle lleseitydk lnkwtskdkm 301 aedevevyip qfkleehyel rsilrsmgme dafnkgranf sgmserndlf 351 lsevfhqamv dvneegteaa agtggvmtgr tghggpqfva dhpflflimh 401 kitkc
1253605 --------------------------------------------------- Definition Sequence 6 from patent US 5470970 PATENT US 5470970 [6] NCBI Seq ID: 1253605 Updated Nov 30, 1995 Citation Patent: US 5470970-A Nov 28, 1995 Ruth Sager, Anthony Anisowicz & Zhiqiang Zou. Maspin, a serpin with tumor suppresing activity. Sequence 390 aa 1 mqmspaltcl vlglaivfge gsavhhppsy vahlasdfgv rvfqqvaqas 51 kdrnvvfspy gvasvlamlq lttggetqqq iqaamgfkid dkgmapalrh 101 lykelmgpwn kdeisttdai fvqrdlklvq gfmphffrlf rstvkqvdfs 151 everarfiin dwvkthtkgm isnllgkgav dqltrlvlvn alyfngqwkt 201 pfpdssthrr lfhksdgstv svpmmaqtnk fnytefttpd ghyydilelp 251 yhgdtlsmfi aapyekevpl saltnilsaq lishwkgnmt rlprllvlpk 301 fsletevdlr kplenlgmtd mfrqfqadft slsdqeplhv aqalqkvkie 351 vnesgtvass stavivsarm apeeiimdrp flfvvrhnpt
1253604 --------------------------------------------------- Definition Sequence 5 from patent US 5470970 PATENT US 5470970 [5] NCBI Seq ID: 1253604 Updated Nov 30, 1995 Citation Patent: US 5470970-A Nov 28, 1995 Ruth Sager, Anthony Anisowicz & Zhiqiang Zou. Maspin, a serpin with tumor suppresing activity. Sequence 375 aa 1 gsigaasmef cfdvfkelkv hhanenifyc piaimsalam vylgakdstr 51 tqinkvvrfd klpgfgdsie aqcgtsvnvh sslrdilnqi tkpndvysfs 101 lasrlyaeer ypilpeylqc vkelyrggle pinfqtaadq arelinswve 151 sqtngiirnv lqpssvdsqt amvlvnaivf kglwekafkd edtqampfrv 201 teqeskpvqm myqiglfrva smasekmkil elpfasgtms mlvllpdevs 251 gleqlesiin fekltewtss nvmeerkikv ylprmkmeek ynltsvlmam 301 gitdvfsssa nlsgissaes lkisqavhaa haeineagre vvgsaeagvd 351 aasvseefra dhpflfcikh iatna
1253603 --------------------------------------------------- Definition Sequence 4 from patent US 5470970 PATENT US 5470970 [4] NCBI Seq ID: 1253603 Updated Nov 30, 1995 Citation Patent: US 5470970-A Nov 28, 1995 Ruth Sager, Anthony Anisowicz & Zhiqiang Zou. Maspin, a serpin with tumor suppresing activity. Sequence 379 aa 1 meqlssantr faldlflals ennpagnifi spfsissama mvflgtrgnt 51 aaqlsktfhf ntveevhsrf qslnadinkr gasyilklan rlygektynf 101 lpeflvstqk tygadlasvd fqhasedark tinqwvkgqt egkipellas 151 gmvdnmtklv lvnaiyfkgn wkdkfmkeat tnapfrlnkk drktvkmmyq 201 kkkfaygyie dlkcrvlelp yqgeelsmvi llpddiedes tglkkieeql 251 tleklhewtk penldfievn vslprfklee sytlnsdlar lgvqdlfnss 301 kadlsgmsga rdifiskivh ksfvevneeg teaaaatagi atfcmlmpee 351 nftadhpflf firhnssgsi lflgrfssp
1253602 --------------------------------------------------- Definition Sequence 3 from patent US 5470970 PATENT US 5470970 [3] NCBI Seq ID: 1253602 Updated Nov 30, 1995 Citation Patent: US 5470970-A Nov 28, 1995 Ruth Sager, Anthony Anisowicz & Zhiqiang Zou. Maspin, a serpin with tumor suppresing activity. Sequence 418 aa 1 mpssvswgil llaglcclvp vslaedpqgd aaqktdtshh dqdhptfnki 51 tpnlaefafs lyrqlahqsn stniffspvs iatafamlsl gtkadthdei 101 leglnfnlte ipeaqihegf qellrtlnqp dsqlqlttgn glflseglkl 151 vdkfledvkk lyhseaftvn fgdteeakkq indyvekgtq gkivdlvkel 201 drdtvfalvn yiffkgkwer pfevkdteee dfhvdqvttv kvpmmkrlgm 251 fniqhckkls swvllmkylg nataifflpd egklqhlene lthdiitkfl 301 enedrrsasl hlpklsitgt ydlksvlgql gitkvfsnga dlsgvteeap 351 lklskavhka vltidekgte aagamfleai pmsippevkf nkpfvflmie 401 qntksplfmg kvvnptqk
1253601 --------------------------------------------------- Definition Sequence 2 from patent US 5470970 PATENT US 5470970 [2] NCBI Seq ID: 1253601 Updated Nov 30, 1995 Citation Patent: US 5470970-A Nov 28, 1995 Ruth Sager, Anthony Anisowicz & Zhiqiang Zou. Maspin, a serpin with tumor suppresing activity. Sequence 375 aa 1 mdalqlansa favdlfkqlc ekeplgnvlf spiclstsls laqvgakgdt 51 aneigqvlhf envkdipfgf qtvtsdvnkl ssfyslklik rlyvdkslnl 101 stefisstkr pyakeletvd fkdkleetkg qinnsikdlt dghfenilad 151 nsvndqtkil vvnaayfvgk wmkkfpeset kecpfrlnkt dtkpvqmmnm 201 eatfcmgnid sinckiielp fqnkhlsmfi llpkdvedes tglekiekql 251 nseslsqwtn pstmanakvk lsipkfkvek midpkaclen lglkhifsed 301 tsdfsgmset kgvalsnvih kvcleitedg gdsievpgar ilqhkdelna 351 dhpfiyiirh nktrniiffg kfcsp
1065409 --------------------------------------------------- Definition bomapin Protein Name: bomapin 1065409: [ Whole ] NCBI Seq ID: 1065409 Updated Nov 15, 1995 Citation REF [1] M. Riewald & R.R. Schleef (1995). Molecular cloning of bomapin (protease inhibitor 10), a novel human serpin that is expressed specifically in the bone marrow. J. Biol. Chem. 270, 26754-26757. MEDLINE identifier: 96070759 Citation REF [2] Data Submission: M. Riewald (1995). Coding region 1065408: 1..1194 (experimentally determined) Sequence 397 aa 1 mdslatsinq falelskkla esaqgkniff sswsistslt ivylgakgtt 51 aaqmaqvlqf nrdqgvkcdp esekkrkmef nlsnseeihs dfqtliseil 101 kpnddyllkt anaiygekty afhnkyledm ktyfgaepqp vnfveasdqi 151 rkdinswver qtegkiqnll pddsvdsttr milvnalyfk giwehqflvq 201 nttekpfrin ettskpvqmm fmkkklhifh iekpkavglq lyyksrdlsl 251 lillpeding leqlekaity eklnewtsad mmelyevqlh lpkfkledsy 301 dlkstlssmg msdafsqska dfsgmssarn lflsnvfhka fveineqgte 351 aaagsgseid irirvpsief nanhpflffi rhnktntilf ygrlcsp
887465 --------------------------------------------------- Definition leupin Protein Name: leupin 887465: [ Whole ] *: Partial NCBI Seq ID: 887465 Updated Nov 3, 1995 Citation REF [1] Data Submission: M.D. Worrall (1995). Citation REF [2] R.C. Barnes & D.M. Worrall (1995). Identification of a novel human serpin gene; cloning sequencing and expression of leupin. FEBS Lett. 373, 61-65. MEDLINE identifier: 96013887 Coding region * Partial 887464: 1..1170 (experimentally determined) Sequence 390 aa 1 mnslseantk fmfdlfqqfr kskennifys pisitsalgm vllgakdnta 51 qqiskvlhfd qvtentteka atyhvdrsgn vhhqfqkllt efnkstdaye 101 lkianklfge ktyqflqeyl daikkfyqts vestdfanap eesrkkinsw 151 vesqtnekik nlfpdgtign dttlvlvnai yfkgqwenkf kkentkeekf 201 wpnkntyksv qmmrqynsfn falledvqak vleipykgkd lsmivllpne 251 idglqkleek ltaeklmewt slqnmretcv dlhlprfkme esydlkdtlr 301 tmgmvnifng dadlsgmtws hglsvskvlh kafvevteeg veaaaatavv 351 vvelsspstn eefccnhpfl ffirqnktns ilfygrfssp
283798 --------------------------------------------------- Definition estrogen-regulated protein Ep45 - African clawed frog Protein Names: estrogen-regulated protein 283798: [ Whole ] Ep45; nickel-binding protein PIR Name: A42440 NCBI Seq ID: 283798 Created Mar 4, 1993 Updated Nov 3, 1995 Citation L.J. Holland, C. Suksang, A.A. Wall, L.R. Roberts, D.R. Moser & A. Bhattacharya (1992). A major estrogen-regulated protein secreted from the liver of Xenopus laevis is a member of the serpin superfamily. Nucleotide sequence of cDNA and hormonal induction of mRNA. J. Biol. Chem. 267, 7053-7059. MEDLINE identifier: 92202269 Citation Data Submission: F.W. Sunderman Jr., B.L. Beck, D. Henjum, K. Antonijczuk, O. Zaharia, G. Korza, J. Ozols, S.M. Hopfer & A.M. Barber (1992). Sequence 436 aa 1 mhllvylslf falalasvte isldnkhrhr heqqghhdsa khghqkdkqq 51 qeqikndegk ltkeekilse ensdfsvnlf nqlsteskrs prkniffspi 101 sisaafymla lgaksethqq ilkglsfnkk klsesqvhea fkrliedsnn 151 pmkahqftig nalfveqtvn ilkgfeenvk hyyqagvfpm nfkdpdnakk 201 qlnnyvkdkt hgviqemire ldsntemvlv nyvlykgewa nnfnptltqk 251 slfsvdkntn vtvqmmnrlg lyrtyqdddc kiielpyknd tamllvfpql 301 gkiqelvlts klinhwyesl atsivdlymp tfsisgkvvl kdtlrkmgis 351 diftdkadlt giseqiklkv smashnavln vnefgteavg atsaqasptk 401 lfppflidsp flvmiysrtl gsqlfmgkvm dptnaq
1174914 --------------------------------------------------- Definition UTERINE MILK PROTEIN PRECURSOR (UTMP). Protein Name: UTERINE MILK PROTEIN 1174914: 1..459 PRECURSOR SWISS-PROT Name: UTMP_BOVIN, Accession: P46201 NCBI Seq ID: 1174914 Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. BELONGS TO THE UTMP SUBFAMILY. Cross-ref NCBI Seq ID: 438481 Cross-ref GenBank Accession: L22095 Cross-ref PROSITE PS00284 Created Nov 1, 1995 Updated Nov 1, 1995 Citation REF [1] Data Submission: N. MATHIALAGAN, T. HANSEN & M.R. ROBERTS (XXX- 1994). Signal 1174914: 1..25 Mature chain UTERINE MILK PROTEIN. 1174914: 26..459 (experimentally determined) active site REACTIVE BOND. 1174914: 420..421 glycosylation 1174914: 268 site Sequence 459 aa 1 mshgrmnlal slvfilcglf nsifcekqqh sqkhmnlvll kkisalsqkm 51 eahpkdfaqe lfkaliiedp rkniifspma mtttlatlsl gikstmrthh 101 pedlklepkl ldvhkylqpl vhvgrelvkq kvlkhqhilf inrkmmvnqm 151 llqqisklqg mdiqmidftd iekakktish hvaekthtki tnlitdlnpe 201 tilclvnhif fkgilkrafq pkltqkevff vndqtkvqvd mmrktermly 251 srseelhatm vkmpckgnvs ltlmlpdagq fdtdlkkmta kraklqkisd 301 frlvrlilpk lkisfkinfk hllpkidpkh iltataisqa itskaplpnl 351 ealhqaeiel sehaltvdta ihtdnllkvp vkakevpavv kvpmkakevp 401 avvkvpmntk evpvvvkvpm ntkevpvvvk vnrpfllfve dektqrdlfv 451 gkvlnpqve
1174843 --------------------------------------------------- Definition UTEROFERRIN-ASSOCIATED BASIC PROTEIN 2 PRECURSOR (UABP-2). Protein Name: UTEROFERRIN-ASSOCIATED 1174843: 1..420 BASIC PROTEIN 2 PRECURSOR SWISS-PROT Name: UAB2_PIG, Accession: P46202 NCBI Seq ID: 1174843 Comment [SUBCELLULAR LOCATION] EXTRACELLULAR (POTENTIAL). Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. BELONGS TO THE UTMP SUBFAMILY. Cross-ref NCBI Seq ID: 2144 Cross-ref EMBL Accession: X62845 Cross-ref PROSITE PS00284 Created Nov 1, 1995 Updated Nov 1, 1995 Citation REF [1] Data Submission: N. MATHIALAGAN, P.V. MALATHY & R.M. ROBERTS (1991). Signal 1174843: 1..25 Mature chain UTEROFERRIN-ASSOCIATED BASIC 1174843: 26..420 PROTEIN 2. (experimentally determined) active site REACTIVE BOND. 1174843: 381..382 glycosylation 1174843: 225 site glycosylation 1174843: 271 site glycosylation 1174843: 343 site Sequence 420 aa 1 mshgkmplvl slvlilcglf nsiscekqqt spktitpvsf kriaalsqkm 51 eanykafaqe lfktlliedp rknmifspvs isislatlsl glrsatrtna 101 idvlerdlrn lrvwdkhqal qhlvemlhel ekkkqlkhkd iffidrnkkm 151 nqmflkeidr vykvdiqmid fkdkektkka inqfvadkid kkaknlithl 201 dpqtllclvn yvffkgiler afqtnltkke dffvnektiv qvdmmrkter 251 miysrseell atmvkmpcke nasiilvlpd tgkfdfalke maakrarlqk 301 tnelqigals caqdqdhlqd rfkhllpkig indifttkav twnttrtsti 351 leavhhavie vkedgltkna akdkdfwkvp vdkkevpvvv kfdrpfflfv 401 edeitrrdlf vakvfnpkte
1174422 --------------------------------------------------- Definition SERINE PROTEINASE INHIBITOR 2. Protein Name: SERINE PROTEINASE INHIBITOR 1174422: 1..345 2 SWISS-PROT Name: SPI2_RABPU, Accession: P42926 NCBI Seq ID: 1174422 Comment [FUNCTION] MAY BE INVOLVED IN THE REGULATION OF THE COMPLEMENT CASCADE. INVOLVED IN RED POCK FORMATION. Comment [SUBCELLULAR LOCATION] CYTOPLASMIC (POTENTIAL). Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Comment [SIMILARITY] HIGHEST WITH COWPOX VIRUS CRMA. Cross-ref NCBI Seq ID: 476326 Cross-ref GenBank Accession: U07763 Cross-ref PROSITE PS00284 Created Nov 1, 1995 Updated Nov 1, 1995 Citation REF [1] A.N. Ali, P.C. Turner, M.A. Brooks & R.W. Moyer (1994). The SPI-1 gene of rabbitpox virus determines host range and is required for hemorrhagic pock formation. Virology 202, 305- 314. MEDLINE identifier: 94279153 active site REACTIVE BOND. 1174422: 306..307 Gene Locus: SPI-2 1174422: 1..345 Sequence 345 aa 1 mdifreiass mkgenvfisp asissvltil yygangstae qlskyvekee 51 nmdkvsaqni sfksinkvyg rysavfkdsf lrkigdkfqt vdftdcrtid 101 ainkcvdift egkinpllde qlspdtclla isavyfkakw ltpfekefts 151 dypfyvspte mvdvsmmsmy gkafnhasvk esfgnfsiie lpyvgdtsmm 201 vilpdkidgl esieqnltdt nfkkwcnsle atfidvhipk fkvtgsynlv 251 dtlvksglte vfgstgdysn mcnldvsvda mihktyidvn eeyteaaaat 301 svlvadcast vtnefcadhp fiyvirhvdg kilfvgrycs pttnc
1174421 --------------------------------------------------- Definition PUTATIVE SERINE PROTEASE INHIBITOR. Protein Name: PUTATIVE SERINE PROTEASE 1174421: 1..320 INHIBITOR SWISS-PROT Name: SPI1_SPVKA, Accession: Q08519 NCBI Seq ID: 1174421 Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 347189 Cross-ref GenBank Accession: L21931 Created Nov 1, 1995 Updated Nov 1, 1995 Citation REF [1] R.F. Massung, V. Jayarama & R.W. Moyer (1993). DNA sequence analysis of conserved and unique regions of swinepox virus: identification of genetic elements supporting phenotypic observations including a novel G protein-coupled receptor homologue. Virology 197, 511-528. MEDLINE identifier: 94069924 Gene Locus: K1R 1174421: 1..320 Sequence 320 aa 1 mdvflkllqk dgnivyspvs islsidmiis kkgyihrpls pytnynedti 51 siasriygdc nslnkdpcic mdcigdmfvl vdfdknhkdi iddinkwvse 101 rtnnhidtii dnigdntkll ivnaayfkss wedefikeyt siekfwynst 151 efilvpmmsn kdiysygyik dsdikiieip ykdrrfsmfi pitkvyktlc 201 niitidklam wtstmnlyev dikiprfkve ssyelkdiig cinmeyyire 251 gtelntpsgf rhksvievne dgttasastc ccvadsvsnk efyayspfif 301 yikdnttsdf lfvgkiispm
1174420 --------------------------------------------------- Definition SERINE PROTEINASE INHIBITOR 1. Protein Name: SERINE PROTEINASE INHIBITOR 1174420: 1..357 1 SWISS-PROT Name: SPI1_RABPU, Accession: P42928 NCBI Seq ID: 1174420 Comment [FUNCTION] THIS VIRAL PROTEIN MAY BE INVOLVED IN THE REGULATION OF THE COMPLEMENT CASCADE. INVOLVED IN RED POCK FORMATION. Comment [SUBCELLULAR LOCATION] CYTOPLASMIC (POTENTIAL). Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 476328 Cross-ref GenBank Accession: U07766 Cross-ref PROSITE PS00284 Created Nov 1, 1995 Updated Nov 1, 1995 Citation REF [1] A.N. Ali, P.C. Turner, M.A. Brooks & R.W. Moyer (1994). The SPI-1 gene of rabbitpox virus determines host range and is required for hemorrhagic pock formation. Virology 202, 305- 314. MEDLINE identifier: 94279153 active site REACTIVE BOND. 1174420: 322..323 Gene Locus: SPI-1 1174420: 1..357 Sequence 357 aa 1 mdifkelilk hpdenvlisp vsilstlsil nhgaagstae qlskyienvn 51 entpddkkdd nndmdvdipy catlatanki ycsdsiefha sflqkikdgf 101 qtvnfnnanq tkelinewvk tmtngkinsl ltsplsintr mtvvsavhfk 151 amwkypfskh ltytdkfyis knivtsvdmm vstendlqyv hinelfggfs 201 iidipyegns smviilpddi egiyniekni tdekfkkwcg mlstksidly 251 mpkfkvemte pynlvpilen lgltnifgyy adfskmcnet itvekflhtt 301 fidvneeyte asavtgvfmt nfsmvyrtkv yinhpfmymi kdntgrilfi 351 gkycypq
1174419 --------------------------------------------------- Definition SERINE PROTEINASE INHIBITOR 1. Protein Name: SERINE PROTEINASE INHIBITOR 1174419: 1..355 1 SWISS-PROT Name: SPI1_COWPX, Accession: P42927 NCBI Seq ID: 1174419 Comment [FUNCTION] THIS VIRAL PROTEIN MAY BE INVOLVED IN THE REGULATION OF THE COMPLEMENT CASCADE. Comment [SUBCELLULAR LOCATION] CYTOPLASMIC (POTENTIAL). Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 476330 Cross-ref GenBank Accession: U07767 Cross-ref PROSITE PS00284 Created Nov 1, 1995 Updated Nov 1, 1995 Citation REF [1] A.N. Ali, P.C. Turner, M.A. Brooks & R.W. Moyer (1994). The SPI-1 gene of rabbitpox virus determines host range and is required for hemorrhagic pock formation. Virology 202, 305- 314. MEDLINE identifier: 94279153 active site REACTIVE BOND. 1174419: 320..321 Gene Locus: SPI-1 1174419: 1..355 Sequence 355 aa 1 mdifkelilk htdenvlisp vsilstlsil nhgaagstae qlskyienkn 51 tpkddkddnn dmdvdipyca tlatankiyc sdsiefhasf lqkikddfqt 101 vnfnnanqtk elinewvktm tngkinsllt tplpintrmt vvsavhfkam 151 wkypfskhlt ytdkfyiskn ivtsvdmmvs tkndlqyvhi nelfggfsii 201 dipyegnssm viilpddieg lyniekhitd enfkkwcskl stksidlymp 251 kfkvemtepy nlvpilenlg ltnifgyysd fskmcnetit vekflhktfi 301 dvneeyteas aitgvfmtnf smvyrtkvyi nhpfmymikd ntgrilfigk 351 ycypq
1170351 --------------------------------------------------- Definition HIBERNATION SPECIFIC PLASMA PROTEIN HP-55 (HIBERNATOR-SPECIFIC BLOOD COMPLEX, 55 KD SUBUNIT). Segments 1170342 [Segment 1 of 9] HIBERNATION SPECIFIC PLASMA PROTEIN HP-55 (HIBERNATOR-SPECIFIC BLOOD COMPLEX, 55 KD SUBUNIT). 1170343 [Segment 2 of 9] HIBERNATION SPECIFIC PLASMA PROTEIN HP-55 (HIBERNATOR-SPECIFIC BLOOD COMPLEX, 55 KD SUBUNIT). 1170344 [Segment 3 of 9] HIBERNATION SPECIFIC PLASMA PROTEIN HP-55 (HIBERNATOR-SPECIFIC BLOOD COMPLEX, 55 KD SUBUNIT). 1170345 [Segment 4 of 9] HIBERNATION SPECIFIC PLASMA PROTEIN HP-55 (HIBERNATOR-SPECIFIC BLOOD COMPLEX, 55 KD SUBUNIT). 1170346 [Segment 5 of 9] HIBERNATION SPECIFIC PLASMA PROTEIN HP-55 (HIBERNATOR-SPECIFIC BLOOD COMPLEX, 55 KD SUBUNIT). 1170347 [Segment 6 of 9] HIBERNATION SPECIFIC PLASMA PROTEIN HP-55 (HIBERNATOR-SPECIFIC BLOOD COMPLEX, 55 KD SUBUNIT). 1170348 [Segment 7 of 9] HIBERNATION SPECIFIC PLASMA PROTEIN HP-55 (HIBERNATOR-SPECIFIC BLOOD COMPLEX, 55 KD SUBUNIT). 1170349 [Segment 8 of 9] HIBERNATION SPECIFIC PLASMA PROTEIN HP-55 (HIBERNATOR-SPECIFIC BLOOD COMPLEX, 55 KD SUBUNIT). 1170350 [Segment 9 of 9] HIBERNATION SPECIFIC PLASMA PROTEIN HP-55 (HIBERNATOR-SPECIFIC BLOOD COMPLEX, 55 KD SUBUNIT). SWISS-PROT Name: HP55_TAMAS, Accession: Q09055 NCBI Seq ID: 1170351 Comment [FUNCTION] PLASMA PROTEINS HP-20, HP-25, HP-27 AND HP-55 FORM A 140-KD COMPLEX VIA DISULPHIDE BONDS IN THE PLASMA AND ARE HIBERNATION SPECIFIC. HP-55 MAY BE INVOLVED IN THE REGULATION OF PROTEASE ACTIVITIES OR THE TRANSPORT OF CERTAIN HORMONES. Comment [TISSUE SPECIFICITY] PLASMA; SYNTHESIZED IN THE LIVER. Comment [SUBCELLULAR LOCATION] EXTRACELLULAR. Comment [PTM] THE N-TERMINUS IS BLOCKED. Comment [DEVELOPMENTAL STAGE] THE PROTEIN COMPLEX DISAPPEARS FROM THE PLASMA AT ONSET OF HIBERNATION AND REAPPEARS AS HIBERNATION CEASES. Comment [SIMILARITY] WITH SERPIN SERINE PROTEASE INHIBITORS. HIGH, TO ALPHA-1-ANTITRYPSIN. Citation REF [1] N. Kondo & J. Kondo (1992). Identification of novel blood proteins specific for mammalian hibernation. J. Biol. Chem. 267, 473-478. MEDLINE identifier: 92112696 Protein Name: HIBERNATION SPECIFIC PLASMA 1170342: 1..20 PROTEIN HP-55 [ Gap ] *: Partial 1170343: 1..38 [ Gap ] 1170344: 1..37 [ Gap ] 1170345: 1..8 [ Gap ] 1170346: 1..14 [ Gap ] 1170347: 1..41 [ Gap ] 1170348: 1..21 [ Gap ] 1170349: 1..15 [ Gap ] 1170350: 1..6 Created Feb 1, 1995 Updated Nov 1, 1995 1170342 --------------------------------------------------- Definition [Segment 1 of 9] HIBERNATION SPECIFIC PLASMA PROTEIN HP-55 (HIBERNATOR-SPECIFIC BLOOD COMPLEX, 55 KD SUBUNIT). SWISS-PROT Name: HP55_TAMAS_1 NCBI Seq ID: 1170342 Sequence 20 aa 1 qdqehpashr iaphlxxfxl 1170343 --------------------------------------------------- Definition [Segment 2 of 9] HIBERNATION SPECIFIC PLASMA PROTEIN HP-55 (HIBERNATOR-SPECIFIC BLOOD COMPLEX, 55 KD SUBUNIT). SWISS-PROT Name: HP55_TAMAS_2 NCBI Seq ID: 1170343 Sequence 38 aa 1 gdthtqileg ldfxltemae adihqgkqnl lqtlnqpn 1170344 --------------------------------------------------- Definition [Segment 3 of 9] HIBERNATION SPECIFIC PLASMA PROTEIN HP-55 (HIBERNATOR-SPECIFIC BLOOD COMPLEX, 55 KD SUBUNIT). SWISS-PROT Name: HP55_TAMAS_3 NCBI Seq ID: 1170344 Sequence 37 aa 1 flenikslyh sgafptxftn teearqqins yveqgxq 1170345 --------------------------------------------------- Definition [Segment 4 of 9] HIBERNATION SPECIFIC PLASMA PROTEIN HP-55 (HIBERNATOR-SPECIFIC BLOOD COMPLEX, 55 KD SUBUNIT). SWISS-PROT Name: HP55_TAMAS_4 NCBI Seq ID: 1170345 Sequence 8 aa 1 gkivelvk 1170346 --------------------------------------------------- Definition [Segment 5 of 9] HIBERNATION SPECIFIC PLASMA PROTEIN HP-55 (HIBERNATOR-SPECIFIC BLOOD COMPLEX, 55 KD SUBUNIT). SWISS-PROT Name: HP55_TAMAS_5 NCBI Seq ID: 1170346 Sequence 14 aa 1 mqhledtist eily 1170347 --------------------------------------------------- Definition [Segment 6 of 9] HIBERNATION SPECIFIC PLASMA PROTEIN HP-55 (HIBERNATOR-SPECIFIC BLOOD COMPLEX, 55 KD SUBUNIT). SWISS-PROT Name: HP55_TAMAS_6 NCBI Seq ID: 1170347 Sequence 41 aa 1 yqvyfprvsi sgtydlkdvl sslgitrvfs rvadltgvte d 1170348 --------------------------------------------------- Definition [Segment 7 of 9] HIBERNATION SPECIFIC PLASMA PROTEIN HP-55 (HIBERNATOR-SPECIFIC BLOOD COMPLEX, 55 KD SUBUNIT). SWISS-PROT Name: HP55_TAMAS_7 NCBI Seq ID: 1170348 Sequence 21 aa 1 avldmdeegt eaaggtvlga e 1170349 --------------------------------------------------- Definition [Segment 8 of 9] HIBERNATION SPECIFIC PLASMA PROTEIN HP-55 (HIBERNATOR-SPECIFIC BLOOD COMPLEX, 55 KD SUBUNIT). SWISS-PROT Name: HP55_TAMAS_8 NCBI Seq ID: 1170349 Sequence 15 aa 1 fdrpflvviy ehntk 1170350 --------------------------------------------------- Definition [Segment 9 of 9] HIBERNATION SPECIFIC PLASMA PROTEIN HP-55 (HIBERNATOR-SPECIFIC BLOOD COMPLEX, 55 KD SUBUNIT). SWISS-PROT Name: HP55_TAMAS_9 NCBI Seq ID: 1170350 Sequence 6 aa 1 vnptqq
1168462 --------------------------------------------------- Definition ANTITHROMBIN-III (ATIII). Protein Name: ANTITHROMBIN-III 1168462: 1..433 SWISS-PROT Name: ANT3_BOVIN, Accession: P41361 NCBI Seq ID: 1168462 Comment [FUNCTION] MOST IMPORTANT SERINE PROTEASE INHIBITOR IN PLASMA THAT REGULATES THE BLOOD COAGULATION CASCADE. AT-III INHIBITS THROMBIN AS WELL AS FACTORS IXA, XA AND XIA. ITS INHIBITORY ACTIVITY IS GREATLY ENHANCED IN THE PRESENCE OF HEPARIN. Comment [SUBCELLULAR LOCATION] EXTRACELLULAR. Comment [TISSUE SPECIFICITY] PLASMA. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Cross-ref PDB Molecule: 1ATT, Chain: (space) Cross-ref PROSITE PS00284 Created Nov 1, 1995 Updated Nov 1, 1995 Citation REF [1] H. Mejdoub, M. Le Ret, Y. Boulanger, M. Maman, J. Choay & J. Reinbolt (1991). The complete amino acid sequence of bovine antithrombin (ATIII). J. Protein Chem. 10, 205-212. MEDLINE identifier: 92029517 Citation REF [2] L. Mourey, J.P. Samama, M. Delarue, M. Petitou, J. Choay & D. Moras (1993). Crystal structure of cleaved bovine antithrombin III at 3.2 A resolution. J. Mol. Biol. 232, 223- 241. MEDLINE identifier: 93323115 binding site HEPARIN. 1168462: 50 binding site HEPARIN. 1168462: 130 binding site HEPARIN. 1168462: 146 active site REACTIVE BOND. 1168462: 394..395 (experimentally determined) disulfide bond (experimentally determined) 1168462: 9 bond 129 disulfide bond (experimentally determined) 1168462: 22 bond 96 disulfide bond (experimentally determined) 1168462: 248 bond 431 glycosylation (experimentally determined) 1168462: 97 site glycosylation (experimentally determined) 1168462: 136 site glycosylation (experimentally determined) 1168462: 156 site glycosylation (experimentally determined) 1168462: 193 site Gene Locus: AT3 1168462: 1..433 Sequence 433 aa 1 hrspvedvct akprdipvnp mciyrssekk ategqgseqk ipgatnrrvw 51 elskanshfa tafyqhlads knnndnifls plsistafam tklgacnntl 101 tqlmevfkfd tisektsdqi hfffaklncr lyrkanksse lvsanrlfgd 151 ksitfnetyq disevvygak lqpldfkgna eqsrltinqw isnktegrit 201 dvippqaine ftvlvlvnti yfkglwkskf spentrkelf ykadgescsv 251 lmmyqeskfr yrrvaestqv lelpfkgddi tmvlilpkle ktlakveqel 301 tpdmlqewld eltetllvvh mprfriedsf svkeqlqdmg ledlfspeks 351 rlpgivaegr sdlyvsdafh kaflevneeg seaaastvis iagrslnsdr 401 vtfkanrpfl vlirevalnt iifmgrvanp cvd
1168249 --------------------------------------------------- Definition ALPHA-2-ANTIPLASMIN PRECURSOR (ALPHA-2-PLASMIN INHIBITOR) (ALPHA-2-PI) (ALPHA-2-AP). Protein Name: ALPHA-2-ANTIPLASMIN 1168249: 1..492 PRECURSOR SWISS-PROT Name: A2AP_BOVIN, Accession: P28800 NCBI Seq ID: 1168249 Comment [FUNCTION] THE MAJOR TARGET OF THIS INHIBITOR ARE PLASMIN AND TRYPSIN, BUT IT ALSO INACTIVATES CHYMOTRYPSIN. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 498822 Cross-ref EMBL Accession: X78436 Cross-ref HSSP P01008 Cross-ref PROSITE PS00284 Created Dec 1, 1992 Updated Nov 1, 1995 Citation REF [1] S. Christensen, L. Berglund & L. Sottrup-Jensen (1994). Primary structure of bovine alpha 2-antiplasmin. FEBS Lett. 343, 223-228. MEDLINE identifier: 94229242 Citation REF [2] S. Christensen & L. Sottrup-Jensen (1992). Bovine alpha 2- antiplasmin. N-terminal and reactive site sequence. FEBS Lett. 312, 100-104. MEDLINE identifier: 93050153 Signal (experimentally determined) 1168249: 1..22 Mature chain ALPHA-2-ANTIPLASMIN. 1168249: 23..492 (experimentally determined) active site REACTIVE BOND (FOR PLASMIN). 1168249: 404..405 (experimentally determined) active site REACTIVE BOND (FOR CHYMOTRYPSIN). 1168249: 405..406 (experimentally determined) glycosylation 1168249: 127 site glycosylation 1168249: 249 site glycosylation 1168249: 296 site glycosylation 1168249: 310 site glycosylation 1168249: 317 site Conflict T -> Q (IN REF. 2). 1168249: 28 (experimentally determined) Conflict Q -> P (IN REF. 2). 1168249: 40 (experimentally determined) Conflict Q -> E (IN REF. 2). 1168249: 43 (experimentally determined) Sequence 492 aa 1 mallwgllal ilsclsslcs aqfspvstme pldlqlmdgq aqqklpplsl 51 lkldnqepgg qiapkkaped cklsptpeqt rrlarammtf ttdlfslvaq 101 sstrpnlils plsvalalsh lalgaqnqtl qrlkevlhad sgpclphlls 151 rlcqdlgpga frlaarmylq kgfpikedfl eqseqlfgak pmsltgmkge 201 dlaninrwvk eategkiedf lsdlpddtvl lllnaihfqg fwrskfdpnl 251 tqrgafhlde qftvpvdmmq altyplhwfl leqpeiqvah fpfknnmsfv 301 vlmptrfewn asqvlanltw dilhqpslse rptkvqlpkl hlkyqldlva 351 tlsqlglqel fqapdlrgis derlvvssvq hqsalelsea gvqaaaatst 401 amsrmslssf ivnrpflffi ledstslplf vgsvrnpnpg aqperkeqqd 451 spdgkdsfqd hkglprgdkp fdpdlklgpp seedyaqpss pk
464799 --------------------------------------------------- Definition SERINE PROTEINASE INHIBITOR 3. Protein Name: SERINE PROTEINASE INHIBITOR 464799: 1..373 3 SWISS-PROT Name: SPI3_VARV, Accession: P33831 NCBI Seq ID: 464799 Comment [FUNCTION] MAY PLAY A ROLE IN CONTROLLING CELL-CELL FUSION. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 297203 Cross-ref EMBL Accession: X69198 Cross-ref HSSP P01009 Cross-ref PROSITE PS00284 Created Feb 1, 1994 Updated Nov 1, 1995 Citation REF [1] S.N. Shchelkunov, V.M. Blinov & L.S. Sandakhchiev (1993). Genes of variola and vaccinia viruses necessary to overcome the host protective mechanisms. FEBS Lett. 319, 80-83. MEDLINE identifier: 93202281 Gene Locus: SPI-3 464799: 1..373 Sequence 373 aa 1 mivllilsla ctaftyrlqg ftnagivayk niqdgneddn ivfspfgysf 51 smfmsllpas gntkvellkt mdlrkidlgp aftelisgla kpktskytyt 101 dltyqsfvdn tvcikpsyyq qyhrfglyrl nfrrdavnki nsiverrsgm 151 snvvdstmld nntlwaiint iyfkgtwqyp fditkthnts ftnkygtktv 201 pmmsvvtklq gntitiddee ydmvrlqykd anismylaig dnmthftdsi 251 maakldywss qlgnkvynlk lprfsienkr diksiaemma psmfnpdnas 301 fkhmtrdply iykmfqnaki dvneqgtvae astimvatvr sspeelefnt 351 pfvfiirhdi tgfilfmgkv esp
416622 --------------------------------------------------- Definition ANTITHROMBIN-III PRECURSOR (ATIII). Protein Name: ANTITHROMBIN-III PRECURSOR 416622: 1..465 SWISS-PROT Name: ANT3_SHEEP, Accession: P32262 NCBI Seq ID: 416622 Comment [FUNCTION] MOST IMPORTANT SERINE PROTEASE INHIBITOR IN PLASMA THAT REGULATES THE BLOOD COAGULATION CASCADE. AT-III INHIBITS THROMBIN AS WELL AS FACTORS IXA, XA AND XIA. ITS INHIBITORY ACTIVITY IS GREATLY ENHANCED IN THE PRESENCE OF HEPARIN. Comment [SUBCELLULAR LOCATION] EXTRACELLULAR. Comment [TISSUE SPECIFICITY] PLASMA. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 1195 Cross-ref EMBL Accession: X68287 Cross-ref HSSP P01008 Cross-ref PROSITE PS00284 Created Oct 1, 1993 Updated Nov 1, 1995 Citation REF [1] R.W. Niessen, A. Sturk, P.L. Hordijk, F. Michiels & M. Peters (1992). Sequence characterization of a sheep cDNA for antithrombin III. Biochim. Biophys. Acta 1171, 207-210. MEDLINE identifier: 93129622 Signal 416622: 1..32 Mature chain ANTITHROMBIN-III. 416622: 33..465 (experimentally determined) binding site HEPARIN. 416622: 82 binding site HEPARIN. 416622: 162 binding site HEPARIN. 416622: 178 active site REACTIVE BOND. 416622: 426..427 (experimentally determined) disulfide bond 416622: 41 bond 161 disulfide bond 416622: 54 bond 128 disulfide bond 416622: 280 bond 463 glycosylation 416622: 129 site glycosylation 416622: 168 site glycosylation 416622: 188 site glycosylation 416622: 225 site Gene Locus: AT3 416622: 1..465 Sequence 465 aa 1 misngigtvt tgkrsmclfp llliglwgcv tchrspvedi ctakprdipv 51 npmciyrspe kkategegse qkipgatnrr vwelskansh fatafyqhla 101 dsknnndnif lsplsistaf amtklgacnn tlkqlmevfk fdtisektsd 151 qihfffakln crlyrkanks selvsanrlf gdksitfnet yqdisevvyg 201 aklqpldfkg naeqsrltin qwisnktegr itdvippqai deftvlvlvn 251 tiyfkglwks kfspentkke lfykadgesc svpmmyqegk fryrrvaegt 301 qvlelpfkgd ditmvlilpk lekplakver eltpdmlqew ldeltetllv 351 vhmphfried sfsvkeqlqd mgledlfspe ksrlpgivae grndlyvsda 401 fhkaflevne egseaaastv isiagrslnl nrvtfqanrp flvlireval 451 ntiifmgrva npcvn
416621 --------------------------------------------------- Definition ANTITHROMBIN-III PRECURSOR (ATIII). Protein Name: ANTITHROMBIN-III PRECURSOR 416621: 1..465 SWISS-PROT Name: ANT3_MOUSE, Accession: P32261 NCBI Seq ID: 416621 Comment [FUNCTION] MOST IMPORTANT SERINE PROTEASE INHIBITOR IN PLASMA THAT REGULATES THE BLOOD COAGULATION CASCADE. AT-III INHIBITS THROMBIN AS WELL AS FACTORS IXA, XA AND XIA. ITS INHIBITORY ACTIVITY IS GREATLY ENHANCED IN THE PRESENCE OF HEPARIN. Comment [SUBCELLULAR LOCATION] EXTRACELLULAR. Comment [TISSUE SPECIFICITY] PLASMA. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 258959 Cross-ref GenBank Accession: S47225 Cross-ref HSSP P01008 Cross-ref PROSITE PS00284 Created Oct 1, 1993 Updated Nov 1, 1995 Citation REF [1] J.K. Wu, W.P. Sheffield & M.A. Blajchman (1992). Molecular cloning and cell-free expression of mouse antithrombin III. Thromb. Haemost. 68, 291-296. MEDLINE identifier: 93069082 Signal 416621: 1..32 Mature chain ANTITHROMBIN-III. 416621: 33..465 (experimentally determined) binding site HEPARIN. 416621: 82 binding site HEPARIN. 416621: 162 binding site HEPARIN. 416621: 178 active site REACTIVE BOND. 416621: 426..427 (experimentally determined) disulfide bond 416621: 41 bond 161 disulfide bond 416621: 54 bond 128 disulfide bond 416621: 280 bond 463 glycosylation 416621: 129 site glycosylation 416621: 168 site glycosylation 416621: 188 site glycosylation 416621: 225 site Gene Locus: AT3 416621: 1..465 Sequence 465 aa 1 myspgagsga agerklclls llligalgca ichgnpvddi ciakprdipv 51 nplciyrspg kkateedgse qkvpeatnrr vwelskansr fatnfyqhla 101 dskndndnif lsplsistaf amtklgacnd tlkqlmevfk fdtisektsd 151 qihfffakln crlyrkanks sdlvsanrlf gdksltfnes yqdvsevvyg 201 aklqpldfke npeqsrvtin nwvanktegr ikdvipqgai neltalvlvn 251 tiyfkglwks kfspentrke pfykvdgqsc pvpmmyqegk fkyrrvaegt 301 qvlelpfkgd ditmvlilpk pekslakveq eltpellqew ldelsetmlv 351 vhmprfrted gfslkeqlqd mglidlfspe ksqlpgivag grddlyvsda 401 fhkaflevne egseaaasts vvitgrslnp nrvtfkanrp flvlireval 451 ntiifmgrva npcvn
136742 --------------------------------------------------- Definition UTEROFERRIN-ASSOCIATED PROTEIN PRECURSOR (UFAP). Protein Name: UTEROFERRIN-ASSOCIATED 136742: 1..417 PROTEIN PRECURSOR SWISS-PROT Name: UFBP_PIG, Accession: P16708 NCBI Seq ID: 136742 Comment THE UFAP ARE A GROUP OF THREE (MW 42 KD, 48 KD, AND 50 KD) ANTIGENICALLY RELATED, BASIC GLYCOPROTEINS SECRETED BY THE PORCINE UTERUS. Comment [SUBUNIT] HETERODIMER WITH THE IRON-BINDING ACID PHOSPHATASE, UF. Comment [INDUCTION] BY PROGESTERONE. Comment [SUBCELLULAR LOCATION] EXTRACELLULAR. Comment [PTM] A SERIES OF AT LEAST FOUR POSTTRANSLATIONAL PROTEOLYTIC PROCESSING STEPS AND DIFFERENTIAL N-LINKED GLYCOSYLATION GENERATE THE VARIOUS MOLECULAR FORMS OF THE UFAP. Comment [PTM] CARRIES THE SO-CALLED MANNOSE 6-PHOSPHATE LYSOSOMAL RECOGNITION MARKER ON ITS CARBOHYDRATE CHAINS. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. BELONGS TO THE UTMP SUBFAMILY. Cross-ref NCBI Seq ID: 164716 Cross-ref GenBank Accession: M30315 Cross-ref HSSP P01011 Cross-ref PROSITE PS00284 Created Aug 1, 1990 Updated Nov 1, 1995 Citation REF [1] P.V. Malathy, K. Imakawa, R.C. Simmen & R.M. Roberts (1990). Molecular cloning of the uteroferrin-associated protein, a major progesterone-induced serpin secreted by the porcine uterus, and the expression of its mRNA during pregnancy. Mol. Endocrinol. 4, 428-440. MEDLINE identifier: 90258936 Signal 136742: 1..25 Propeptide OR 44, OR 99. 136742: 26..40 (experimentally determined) Mature chain UTEROFERRIN-ASSOCIATED PROTEIN, 136742: 41..417 LONG FORM. (experimentally determined) Mature chain UTEROFERRIN-ASSOCIATED PROTEIN, 136742: 100..417 SHORT. FORM. (experimentally determined) Variant MISSING (IN AN ISOFORM). 136742: 41..44 (experimentally determined) Variant MISSING (IN AN ISOFORM). 136742: 41..99 (experimentally determined) active site REACTIVE BOND. 136742: 378..379 glycosylation 136742: 132 site glycosylation 136742: 222 site glycosylation 136742: 268 site glycosylation 136742: 340 site Sequence 417 aa 1 mshgkmplvl slvlilcglf nsiscekqqt spktitpvsf kriaalsqkm 51 eanykafaqe lfktlliedp rknmifspvs isislatlsl glrsatrtna 101 idvldvalkn lavmlmaqap talleivhel vnrtakhqdi lidrtemnqm 151 flkeidryik mdiqmidfkd kektkkainq fvadkidkka knlithldpq 201 tllclvnyif fkgilerafq tnltkkedff vnektivqvd mmrktermiy 251 srseellatm vkipckenas iilvlpdtgk fnfalkemaa krarlqktnd 301 frlvhlvvpk ikdnlqdrfk hllpkigind ifttkavtwn ttgtstilea 351 vhhavievke dgltknaakd kdfwkvpvdk kevpvvvkfd rpfflfvede 401 itrrdlfvak vfnpkte
134829 --------------------------------------------------- Definition SERINE PROTEINASE INHIBITOR 3. Protein Name: SERINE PROTEINASE INHIBITOR 134829: 1..369 3 SWISS-PROT Name: SPI3_VACCV, Accession: P18384 NCBI Seq ID: 134829 Comment [FUNCTION] MAY PLAY A ROLE IN CONTROLLING CELL-CELL FUSION. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 222706 Cross-ref DDBJ Accession: D00382 Cross-ref HSSP P01009 Cross-ref PROSITE PS00284 Created Nov 1, 1990 Updated Nov 1, 1995 Citation REF [1] M.E. Boursnell, I.J. Foulds, J.I. Campbell & M.M. Binns (1988). Non-essential genes in the vaccinia virus HindIII K fragment: a gene related to serine protease inhibitors and a gene related to the 37K vaccinia virus major envelope antigen. J. Gen. Virol. 69, 2995-3003. MEDLINE identifier: 89067908 Gene Locus: SPI-3 134829: 1..369 Sequence 369 aa 1 miallilslt csvstyrlqg ftnagivayk niqddnivfs pfgysfsmfm 51 sllpasgntr iellktmdlr krdlgpafte lisglaklkt skytytdlty 101 qsfvdntvci kpsyyqqyhr fglyrlnfrr davnkinsiv errsgmsnvv 151 dsnmldnntl waiintiyfk giwqypfdit ktrnasftnk ygtktvpmmn 201 vvtklqgnti tiddeeydmv rlpykdanis mylaigdnmt hftdsitaak 251 ldywsfqlgn kvynlklpkf sienkrdiks iaemmapsmf npdnasfkhm 301 trdplyiykm fqnakidvde qgtvaeasti mvatarsspe klefntpfvf 351 iirhditgfi lfmgkvesp
134828 --------------------------------------------------- Definition SERINE PROTEINASE INHIBITOR 3. Protein Name: SERINE PROTEINASE INHIBITOR 134828: 1..369 3 SWISS-PROT Name: SPI3_VACCC, Accession: P20532 NCBI Seq ID: 134828 Comment [FUNCTION] MAY PLAY A ROLE IN CONTROLLING CELL-CELL FUSION. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 335354 Cross-ref GenBank Accession: M35027 Cross-ref HSSP P01009 Cross-ref PROSITE PS00284 Created Feb 1, 1991 Updated Nov 1, 1995 Citation REF [1] S.J. Goebel, G.P. Johnson, M.E. Perkus, S.W. Davis, J.P. Winslow & E. Paoletti (1990). The complete DNA sequence of vaccinia virus. Virology 179, 247-266. MEDLINE identifier: 91021027 Citation REF [2] S.J. GOEBEL, G.P. JOHNSON, M.E. PERKUS, S.W. DAVIS, J.P. WINSLOW & E. PAOLETTI (1990)VIROLOGY 179, 517-563. Gene Locus: SPI-3 134828: 1..369 Sequence 369 aa 1 miallilslt csvstyrlqg ftnagivayk niqddnivfs pfgysfsmfm 51 sllpasgntr iellktmdlr krdlgpafte lisglaklkt skytytdlty 101 qsfvdntvci kplyyqqyhr fglyrlnfrr davnkinsiv errsgmsnvv 151 dsnmldnntl waiintiyfk gtwqypfdit ktrnasftnk ygtktvpmmn 201 vvtklqgnti tiddeeydmv rlpykdanis mylaigdnmt hftdsitaak 251 ldywsfqlgn kvynlklpkf sienkrdiks iaemmapsmf npdnasfkhm 301 trdplyiykm fqnakidvde qgtvaeasti mvatarsspe klefntpfvf 351 iirhditgfi lfmgkvesp
134826 --------------------------------------------------- Definition SERINE PROTEINASE INHIBITOR 2. Protein Name: SERINE PROTEINASE INHIBITOR 134826: 1..345 2 SWISS-PROT Name: SPI2_VACCV, Accession: P15059 NCBI Seq ID: 134826 Comment [FUNCTION] MAY BE INVOLVED IN THE REGULATION OF THE COMPLEMENT CASCADE. Comment [SUBCELLULAR LOCATION] CYTOPLASMIC (POTENTIAL). Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Comment [SIMILARITY] HIGHEST WITH COWPOX VIRUS CRMA. Comment [CAUTION] REF.2 SEQUENCE WAS INCORRECT. Cross-ref NCBI Seq ID: 335821 Cross-ref NCBI Seq ID: 222758 Cross-ref NCBI Seq ID: 222695 Cross-ref GenBank Accession: M24218 Cross-ref DDBJ Accession: D11079 Cross-ref DDBJ Accession: D00581 Cross-ref HSSP P05619 Cross-ref PROSITE PS00284 Created Apr 1, 1990 Updated Nov 1, 1995 Citation REF [1] G.L. Smith, Y.S. Chan & S.T. Howard (1991). Nucleotide sequence of 42 kbp of vaccinia virus strain WR from near the right inverted terminal repeat. J. Gen. Virol. 72, 1349-1376. MEDLINE identifier: 91259063 Citation REF [2] G.J. Kotwal & B. Moss (1989). Vaccinia virus encodes two proteins that are structurally related to members of the plasma serine protease inhibitor superfamily. J. Virol. 63, 600-606. MEDLINE identifier: 89094985 Citation REF [3] G.L. Smith, S.T. Howard & Y.S. Chan (1989). Vaccinia virus encodes a family of genes with homology to serine proteinase inhibitors. J. Gen. Virol. 70, 2333-2343. MEDLINE identifier: 89381686 active site REACTIVE BOND. 134826: 306..307 Gene Locus: B13R 134826: 1..345 Sequence 345 aa 1 mdifreiass mkgenvfisp asissvltil yygangstae qlskyvekee 51 nmdkvsaqni sfksinkvyg rysavfkdsf lrkigdkfqt vdftdcrtid 101 ainkcvdift egkinpllde plspdtclla isavyfkakw ltpfekefts 151 dypfyvspte mvdvsmmsmy gkafnhasvk esfgnfsiie lpyvgdtsmm 201 vilpdkidgl esieqnltdt nfkkwcnsle atfidvhipk fkvtgsynlv 251 dtlvksglte vfgstgdysn mcnsdvsvda mihktyidvn eeyteaaaat 301 calvsdcast itnefcvdhp fiyvirhvdg kilfvgrycs pttnc
134824 --------------------------------------------------- Definition SERINE PROTEINASE INHIBITOR 1. Protein Name: SERINE PROTEINASE INHIBITOR 134824: 1..353 1 SWISS-PROT Name: SPI1_VACCV, Accession: P15058 NCBI Seq ID: 134824 Comment [FUNCTION] THIS VIRAL PROTEIN MAY BE INVOLVED IN THE REGULATION OF THE COMPLEMENT CASCADE. Comment [SUBCELLULAR LOCATION] CYTOPLASMIC (POTENTIAL). Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 222767 Cross-ref NCBI Seq ID: 335818 Cross-ref NCBI Seq ID: 222703 Cross-ref DDBJ Accession: D11079 Cross-ref GenBank Accession: M24217 Cross-ref DDBJ Accession: D00582 Cross-ref HSSP P01012 Cross-ref PROSITE PS00284 Created Apr 1, 1990 Updated Nov 1, 1995 Citation REF [1] G.L. Smith, Y.S. Chan & S.T. Howard (1991). Nucleotide sequence of 42 kbp of vaccinia virus strain WR from near the right inverted terminal repeat. J. Gen. Virol. 72, 1349-1376. MEDLINE identifier: 91259063 Citation REF [2] G.J. Kotwal & B. Moss (1989). Vaccinia virus encodes two proteins that are structurally related to members of the plasma serine protease inhibitor superfamily. J. Virol. 63, 600-606. MEDLINE identifier: 89094985 Citation REF [3] G.L. Smith, S.T. Howard & Y.S. Chan (1989). Vaccinia virus encodes a family of genes with homology to serine proteinase inhibitors. J. Gen. Virol. 70, 2333-2343. MEDLINE identifier: 89381686 active site REACTIVE BOND. 134824: 318..319 Gene Locus: SPI-1 134824: 1..353 Sequence 353 aa 1 mdifkelilk htdenvlisp vsilstlsil nhgaagstae qlskyienmn 51 entpddnndm dvdipycatl atankiygsd siefhasflq kikddfqtvn 101 fnnanqtkel inewvktmtn gkinslltsp lsintrmtvv savhfkamwk 151 ypfskhltyt dkfyiskniv tsvdmmvste nnlqyvhine lfggfsiidi 201 pyegnssmvi ilpddiegiy nieknitdek fkkwcgmlst ksidlympkf 251 kvemtepynl vpilenlglt nifgyyadfs kmcnetitve kflhttfidv 301 neeyteasav tgvfmtnfsm vyrtkvyinh pfmymikdnt grilfigkyc 351 ypq
134823 --------------------------------------------------- Definition SERINE PROTEINASE INHIBITOR 1. Protein Name: SERINE PROTEINASE INHIBITOR 134823: 1..353 1 SWISS-PROT Name: SPI1_VACCC, Accession: P20531 NCBI Seq ID: 134823 Comment [FUNCTION] THIS VIRAL PROTEIN MAY BE INVOLVED IN THE REGULATION OF THE COMPLEMENT CASCADE. Comment [SUBCELLULAR LOCATION] CYTOPLASMIC (POTENTIAL). Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 335332 Cross-ref GenBank Accession: M35027 Cross-ref HSSP P01012 Cross-ref PROSITE PS00284 Created Feb 1, 1991 Updated Nov 1, 1995 Citation REF [1] S.J. Goebel, G.P. Johnson, M.E. Perkus, S.W. Davis, J.P. Winslow & E. Paoletti (1990). The complete DNA sequence of vaccinia virus. Virology 179, 247-266. MEDLINE identifier: 91021027 Citation REF [2] S.J. GOEBEL, G.P. JOHNSON, M.E. PERKUS, S.W. DAVIS, J.P. WINSLOW & E. PAOLETTI (1990)VIROLOGY 179, 517-563. active site REACTIVE BOND. 134823: 318..319 Gene Locus: SPI-1 134823: 1..353 Sequence 353 aa 1 mdifkelivk hpdenvlisp vsilstlsil nhgaagstae qlskyienmn 51 entpddnndm dvdipycatl atankiygsd siefhasflq kikddfqtvn 101 fnnanqtkel inewvktmtn gkinslltsp lsintrmtvv savhfkamwk 151 ypfskhltyt dkfyiskniv tsvdmmvgte nnlqyvhine lfggfsiidi 201 pyegnssmvi ilpddiegiy nieknitdek fkkwcgmlst ksidlympkf 251 kvemtepynl vpilenlglt nifgyyadfs kmcnetitve kflhttfidv 301 neeyteasav tgvftinfsm vyrtkvyinh pfmymikdtt grilfigkyc 351 ypq
129575 --------------------------------------------------- Definition PLASMINOGEN ACTIVATOR INHIBITOR-1 PRECURSOR, ENDOTHELIAL (PAI- 1). Protein Name: PLASMINOGEN ACTIVATOR 129575: 1..402 INHIBITOR-1 PRECURSOR, ENDOTHELIAL SWISS-PROT Name: PAI1_BOVIN, Accession: P13909 NCBI Seq ID: 129575 Comment [FUNCTION] THIS INHIBITOR ACTS AS "BAIT" FOR TISSUE PLASMINOGEN ACTIVATOR, UROKINASE, AND PROTEIN C. ITS RAPID INTERACTION WITH TPA MAY FUNCTION AS A MAJOR CONTROL POINT IN THE REGULATION OF FIBRINOLYSIS. Comment PAI1 IS INACTIVATED BY PROTEOLYTIC ATTACK OF THE UROKINASE- TYPE (U-PA) AND THE TISSUE-TYPE (TPA), CLEAVING THE 369(R)- 370(M) BOND. Comment VASCULAR ENDOTHELIAL CELLS MAY BE THE PRIMARY SITE OF SYNTHESIS OF PLASMA PAI. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 601 Cross-ref NCBI Seq ID: 930005 Cross-ref EMBL Accession: X16383 Cross-ref EMBL Accession: X52906 Cross-ref HSSP P01008 Cross-ref PROSITE PS00284 Created Jan 1, 1990 Updated Nov 1, 1995 Citation REF [1] J. Mimuro, M. Sawdey, M. Hattori & D.J. Luskutoff (1989). cDNA for bovine type 1 plasminogen activator inhibitor (PAI- 1). Nucleic Acids Res. 17, 8872. MEDLINE identifier: 90067867 Citation REF [2] K. Katagiri, K. Okada, H. Hattori & M. Yano (1988). Bovine endothelial cell plasminogen activator inhibitor. Purification and heat activation. Eur. J. Biochem. 176, 81-87. MEDLINE identifier: 88329072 Citation REF [3] M.S. Pepper, D. Belin, R. Montesano, L. Orci & J.D. Vassalli (1990). Transforming growth factor-beta 1 modulates basic fibroblast growth factor-induced proteolytic and angiogenic properties of endothelial cells in vitro. J. Cell Biol. 111, 743-755. MEDLINE identifier: 90338128 Signal (experimentally determined) 129575: 1..23 Mature chain PLASMINOGEN ACTIVATOR INHIBITOR I. 129575: 24..402 (experimentally determined) active site REACTIVE BOND. 129575: 369..370 (experimentally determined) glycosylation 129575: 232 site glycosylation 129575: 288 site glycosylation 129575: 352 site Conflict S -> L (IN REF. 2). 129575: 50 (experimentally determined) Gene Locus: PAI1 129575: 1..402 Sequence 402 aa 1 mrmspvfacl alglalifge gsasyqpqsa aaslatdfgv kvfqqvvras 51 kdrnvvfspy gvasvlamlq lttggetrqq iqeamqfkie ekgmapafhr 101 lykelmgpwn kdeistadai fvqrdlelvh gfmpnffrlf rttvkqvdfs 151 everarfivn dwvkrhtkgm isdllgegav dqltrlvlvn alyfngqwkm 201 pfpesnthhr lfhksdgsti svpmmaqtnk fnytefttpd gryydilelp 251 yhgntlsmli aapyekevpl saltsildae lisqwkgnmt rltrllvlpk 301 fsleteidlr rplenlgmtd mfrpsqadfs sfsdqeflyv sqalqkvkie 351 vnesgtlass stalvvsarm apeeiimdrp flfvvrhnpt gtvlfmgqvm 401 ep
123123 --------------------------------------------------- Definition ICE INHIBITOR (HEMORRHAGE-INDUCING 38 KD PROTEIN) (CYTOKINE RESPONSE MODIFIER PROTEIN) (SERINE PROTEINASE INHIBITOR 2). Protein Name: ICE INHIBITOR 123123: 1..341 SWISS-PROT Name: CRMA_COWPX, Accession: P07385 NCBI Seq ID: 123123 Comment [FUNCTION] SPECIFIC AND POTENT INHIBITOR OF THE INTERLEUKIN-1B CONVERTING ENZYME (ICE) THEREBY SUPPRESSING AN INTERLEUKIN-1 BETA RESPONSE TO INFECTION. THE INHIBITION OF ICE BY CRMA IS AN EXAMPLE OF A "CROSS-CLASS" INTERACTION, IN WHICH A SERPIN INHIBITS A NON-SERINE PROTEINASE. Comment [SUBCELLULAR LOCATION] CYTOPLASMIC (POTENTIAL). Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Comment [SIMILARITY] HIGHEST WITH VACCINIA VIRIUS SPI-2. Cross-ref NCBI Seq ID: 323402 Cross-ref GenBank Accession: M14217 Cross-ref HSSP P05619 Cross-ref PROSITE PS00284 Created Apr 1, 1988 Updated Nov 1, 1995 Citation REF [1] D.J. Pickup, B.S. Ink, W. Hu, C.A. Ray & W.K. Joklik (1986). Hemorrhage in lesions caused by cowpox virus is induced by a viral protein that is related to plasma protein inhibitors of serine proteases. Proc. Natl. Acad. Sci. U.S.A. 83, 7698- 7702. MEDLINE identifier: 87017016 Citation REF [2] G.J. Palumbo, D.J. Pickup, T.N. Fredrickson, L.J. McIntyre & R.M. Buller (1989). Inhibition of an inflammatory response is mediated by a 38-kDa protein of cowpox virus. Virology 172, 262-273. MEDLINE identifier: 89370309 Citation REF [3] C.A. Ray, R.A. Black, S.R. Kronheim, T.A. Greenstreet, P.R. Sleath, G.S. Salvesen & D.J. Pickup (1992). Viral inhibition of inflammation: cowpox virus encodes an inhibitor of the interleukin-1 beta converting enzyme. Cell 69, 597-604. MEDLINE identifier: 92266391 Citation REF [4] T. Komiyama, C.A. Ray, D.J. Pickup, A.D. Howard, N.A. Thornberry, E.P. Peterson & G. Salvesen (1994). Inhibition of interleukin-1 beta converting enzyme by the cowpox virus serpin CrmA. An example of cross-class inhibition. J. Biol. Chem. 269, 19331-19337. MEDLINE identifier: 94308211 active site REACTIVE BOND. 123123: 303..304 Gene Locus: CRMA 123123: 1..341 Sequence 341 aa 1 mdifreiass mkgenvfisp psissvltil yygangstae qlskyvekea 51 dknkddisfk smnkvygrys avfkdsflrk igdnfqtvdf tdcrtvdain 101 kcvdiftegk inplldepls pdtcllaisa vyfkakwlmp fekeftsdyp 151 fyvsptemvd vsmmsmygea fnhasvkesf gnfsiielpy vgdtsmvvil 201 pdnidglesi eqnltdtnfk kwcdsmdamf idvhipkfkv tgsynlvdal 251 vklgltevfg stgdysnmcn sdvsvdamih ktyidvneey teaaaatcal 301 vadcastvtn efcadhpfiy virhvdgkil fvgrycsptt n
116961 --------------------------------------------------- Definition CONTRAPSIN PRECURSOR. Protein Name: CONTRAPSIN PRECURSOR 116961: 1..418 SWISS-PROT Name: COTR_MOUSE, Accession: P07759 NCBI Seq ID: 116961 Comment [FUNCTION] CONTRAPSIN INHIBITS TRYPSIN-LIKE PROTEASES. Comment [SUBCELLULAR LOCATION] EXTRACELLULAR. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 220388 Cross-ref NCBI Seq ID: 50442 Cross-ref NCBI Seq ID: 50517 Cross-ref DDBJ Accession: D00725 Cross-ref EMBL Accession: X55147 Cross-ref EMBL Accession: X00946 Cross-ref HSSP P01008 Cross-ref PROSITE PS00284 Created Aug 1, 1988 Updated Nov 1, 1995 Citation REF [1] Y. Suzuki, K. Yamamoto & H. Sinohara (1990). Molecular cloning and sequence analysis of full-length cDNA coding for mouse contrapsin. J. Biochem. 108, 344-346. MEDLINE identifier: 91115777 Citation REF [2] K. Ohkubo, S. Ogata, Y. Misumi, N. Takami, H. Sinohara & Y. Ikehara (1991). Cloning, structure and expression of cDNA for mouse contrapsin and a related protein. Biochem. J. 276, 337- 342. MEDLINE identifier: 91264784 Citation REF [3] R.E. Hill, P.H. Shaw, P.A. Boyd, H. Baumann & N.D. Hastie (1984). Plasma protease inhibitors in mouse and man: divergence within the reactive centre regions. Nature 311, 175-177. MEDLINE identifier: 84295637 Signal * Partial 116961: 1..418 (experimentally determined) Mature chain CONTRAPSIN. 116961: 1..418 * Partial (experimentally determined) active site REACTIVE BOND. 116961: 384..385 (experimentally determined) glycosylation 116961: 39 site glycosylation 116961: 105 site glycosylation 116961: 185 site glycosylation 116961: 270 site Conflict A -> R (IN REF. 2). 116961: 84 (experimentally determined) Conflict M -> V (IN REF. 3). 116961: 204 (experimentally determined) Conflict T -> I (IN REF. 3). 116961: 347 (experimentally determined) Gene Locus: MCM2 116961: 1..418 Sequence 418 aa 1 mafivamgmi lmagicpavl cfpdgtkemd ivfhehqdng tqddsltlas 51 vntdfafsly kklalknpdt nivfsplsis aalalvslga kgktmeeile 101 glkfnltetp eadihqgfgn llqslsqped qdqinignam fiekdlqila 151 efhektraly qteaftadfq qpteaknlin dyvsnqtqgm ikeliselde 201 rtlmvlvnyi yfkgkwkisf dpqdtfesef yldekrsvkv pmmkmklltt 251 rhfrdeelsc svlelkytgn asallilpdq grmqqveasl qpetlrkwrk 301 tlfpsqieel nlpkfsiasn yrleedvlpe mgikevfteq adlsgitetk 351 klsvsqvvhk avldvaetgt eaaaatgvig girkailpav hfnrpflfvi 401 yhtsaqsilf makvnnpk
113882 --------------------------------------------------- Definition ANGIOTENSINOGEN PRECURSOR. Protein Name: ANGIOTENSINOGEN PRECURSOR 113882: 1..477 SWISS-PROT Name: ANGT_RAT, Accession: P01015 NCBI Seq ID: 113882 Comment [FUNCTION] IN RESPONSE TO LOWERED BLOOD PRESSURE, THE ENZYME RENIN CLEAVES ANGIOTENSIN I, FROM ANGIOTENSINOGEN. ACE (ANGIOTENSIN CONVERTING ENZYME) THEN REMOVES A DIPEPTIDE TO YIELD THE PHYSIOLOGICALLY ACTIVE PEPTIDE ANGIOTENSIN II, THE MOST POTENT PRESSOR SUBSTANCE KNOWN, WHICH HELPS REGULATE VOLUME AND MINERAL BALANCE OF BODY FLUIDS. Comment [TISSUE SPECIFICITY] MADE IN THE LIVER & SECRETED IN THE PLASMA. Comment [SIMILARITY] WITH SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 202914 Cross-ref GenBank Accession: L00094 Cross-ref PROSITE PS00284 Created Jul 21, 1986 Updated Nov 1, 1995 Citation REF [1] H. Ohkubo, R. Kageyama, M. Ujihara, T. Hirose, S. Inayama & S. Nakanishi (1983). Cloning and sequence analysis of cDNA for rat angiotensinogen. Proc. Natl. Acad. Sci. U.S.A. 80, 2196- 2200. MEDLINE identifier: 83169849 Citation REF [2] T. Nakayama, T. Nakajima & H. Sokabe (1972). Comparative studies on angiotensins. II. Structure of rat angiotensin and its identification by DNS-method. Chem. Pharm. Bull. 20, 1579- 1581. MEDLINE identifier: 73060322 Signal (experimentally determined) 113882: 1..24 Mature chain ANGIOTENSINOGEN. 113882: 25..477 (experimentally determined) Processed ANGIOTENSIN I. 113882: 25..34 active peptide (experimentally determined) Processed ANGIOTENSIN II. 113882: 25..32 active peptide (experimentally determined) glycosylation 113882: 295 site glycosylation 113882: 319 site Gene Locus: AGT 113882: 1..477 Sequence 477 aa 1 mtptgaglka tifciltwvs ltagdrvyih pfhllyysks tcaqlenpsv 51 etlpeptfep vpiqaktspv dektlrdklv latekleaed rqraaqvami 101 anfmgfrmyk mlseargvas gavlsppalf gtlvsfylgs ldptasqlqv 151 llgvpvkegd ctsrldghkv ltalqavqgl lvtqggsssq tpllqstvvg 201 lftapglrlk qpfveslgpf tpaifprsld lstdpvlaaq kinrfvqavt 251 gwkmnlpleg vstdstlffn tyvhfqgkmr gfsqltglhe fwvdnstsvs 301 vpmlsgtgnf qhwsdaqnnf svtrvplges vtllliqpqc asdldrvevl 351 vfqhdfltwi knppprairl tlpqleirgs ynlqdllaqa klstllgaea 401 nlgkmgdtnp rvgevlnsil lelqageeeq ptesaqqpgs pevldvtlss 451 pflfaiyerd sgalhflgrv dnpqnvv
113881 --------------------------------------------------- Definition ANGIOTENSINOGEN PRECURSOR. Protein Name: ANGIOTENSINOGEN PRECURSOR 113881: 1..477 SWISS-PROT Name: ANGT_MOUSE, Accession: P11859 NCBI Seq ID: 113881 Comment [FUNCTION] IN RESPONSE TO LOWERED BLOOD PRESSURE, THE ENZYME RENIN CLEAVES ANGIOTENSIN I, FROM ANGIOTENSINOGEN. ACE (ANGIOTENSIN CONVERTING ENZYME) THEN REMOVES A DIPEPTIDE TO YIELD THE PHYSIOLOGICALLY ACTIVE PEPTIDE ANGIOTENSIN II, THE MOST POTENT PRESSOR SUBSTANCE KNOWN, WHICH HELPS REGULATE VOLUME AND MINERAL BALANCE OF BODY FLUIDS. Comment [TISSUE SPECIFICITY] MADE IN THE LIVER & SECRETED IN THE PLASMA. Comment [SIMILARITY] WITH SERPIN SERINE PROTEASE INHIBITORS. Cross-ref PROSITE PS00284 Created Oct 1, 1989 Updated Nov 1, 1995 Citation REF [1] W.M. Clouston, B.A. Evans, J. Haralambidis & R.I. Richards (1988). Molecular cloning of the mouse angiotensinogen gene. Genomics 2, 240-248. MEDLINE identifier: 88284703 Signal (experimentally determined) 113881: 1..24 Mature chain ANGIOTENSINOGEN. 113881: 25..477 (experimentally determined) Processed ANGIOTENSIN I. 113881: 25..34 active peptide (experimentally determined) Processed ANGIOTENSIN II. 113881: 25..32 active peptide (experimentally determined) glycosylation 113881: 38 site glycosylation 113881: 319 site glycosylation 113881: 401 site Gene Locus: AGT 113881: 1..477 Sequence 477 aa 1 mtptgaglka tifciltwvs ltagdrvyih pfhllyhnks tcaqlenpsv 51 etlpestfep vpiqaktspv nektlhdqlv laaekleded rkraaqvami 101 anfvgfrmyk mlneagsgas gailsppalf gtlvsfylgs ldptasqlqt 151 lldvpvkegd ctsrldghkv laalravqgl lvtqggsssq tpllqsimvg 201 lftapgfrlk hsfvqslalf tpalfprsld lstdpvlate kinrfikavt 251 gwkmnlpleg vstdstllfn tyvhfqgtmr gfsqlpgvhe fwvdnsisvs 301 vpmisgtgnf qhwsdaqnnf svtcvplger atllliqphc tsdldrveal 351 ifrndlltwi enppprairl tlpqleirgs ynlqdllaed klptllgaea 401 nlsnigdtnp rvgevlnsil lelkageeeq pttsvqqpgs pealdvtlss 451 pflfaiyeqd sgtlhflgrv nnpqsvv
113876 --------------------------------------------------- Definition ANGIOTENSINOGEN. Protein Name: ANGIOTENSINOGEN 113876: 1..10 *: Partial SWISS-PROT Name: ANGT_BOVIN, Accession: P01017 NCBI Seq ID: 113876 Comment [FUNCTION] IN RESPONSE TO LOWERED BLOOD PRESSURE, THE ENZYME RENIN CLEAVES ANGIOTENSIN I, FROM ANGIOTENSINOGEN. ACE (ANGIOTENSIN CONVERTING ENZYME) THEN REMOVES A DIPEPTIDE TO YIELD THE PHYSIOLOGICALLY ACTIVE PEPTIDE ANGIOTENSIN II, THE MOST POTENT PRESSOR SUBSTANCE KNOWN, WHICH HELPS REGULATE VOLUME AND MINERAL BALANCE OF BODY FLUIDS. Comment [TISSUE SPECIFICITY] MADE IN THE LIVER & SECRETED IN THE PLASMA. Comment [SIMILARITY] WITH SERPIN SERINE PROTEASE INHIBITORS. Cross-ref PROSITE PS00284 Created Jul 21, 1986 Updated Nov 1, 1995 Citation REF [1] D.F. ELLIOTT & W.S. PEART (1957)BIOCHEM. J. 65, 246-254. Processed ANGIOTENSIN I. 113876: 1..10 active peptide (experimentally determined) Processed ANGIOTENSIN II. 113876: 1..8 active peptide (experimentally determined) Gene Locus: AGT 113876: 1..10 Sequence 10 aa 1 drvyvhpfhl
112907 --------------------------------------------------- Definition ALPHA-2-ANTIPLASMIN PRECURSOR (ALPHA-2-PLASMIN INHIBITOR) (ALPHA-2-PI) (ALPHA-2-AP). Protein Name: ALPHA-2-ANTIPLASMIN 112907: 1..491 PRECURSOR SWISS-PROT Name: A2AP_HUMAN, Accession: P08697 NCBI Seq ID: 112907 Comment [FUNCTION] THE MAJOR TARGET OF THIS INHIBITOR ARE PLASMIN AND TRYPSIN, BUT IT ALSO INACTIVATES CHYMOTRYPSIN. Comment [SIMILARITY] WITH OTHER SERPIN SERINE PROTEASE INHIBITORS. Cross-ref NCBI Seq ID: 219408 Cross-ref NCBI Seq ID: 219410 Cross-ref NCBI Seq ID: 177886 Cross-ref NCBI Seq ID: 178751 Cross-ref DDBJ Accession: D00116 Cross-ref DDBJ Accession: D00174 Cross-ref GenBank Accession: M20786 Cross-ref GenBank Accession: J02654 Cross-ref HSSP P01008 Cross-ref SWISS-2DPAGE P08697 Cross-ref MIM 262850 Cross-ref PROSITE PS00284 Created Jan 1, 1988 Updated Nov 1, 1995 Citation REF [1] M. Tone, R. Kikuno, A. Kume-Iwaki & T. Hashimoto-Gotoh (1987). Structure of human alpha 2-plasmin inhibitor deduced from the cDNA sequence. J. Biochem. 102, 1033-1041. MEDLINE identifier: 88139254 Citation REF [2] S. Hirosawa, Y. Nakamura, O. Miura, Y. Sumi & N. Aoki (1988). Organization of the human alpha 2-plasmin inhibitor gene. Proc. Natl. Acad. Sci. U.S.A. 85, 6836-6840. MEDLINE identifier: 88320531 Citation REF [3] S. HIROSAWA, Y. NAKAMURA, O. MIURA, Y. SUMI & N. AOKI (1989)PROC. NATL. ACAD. SCI. U.S.A. 86, 1612-1613. Citation REF [4] W.E. Holmes, L. Nelles, H.R. Lijnen & D. Collen (1987). Primary structure of human alpha 2-antiplasmin, a serine protease inhibitor (serpin). J. Biol. Chem. 262, 1659-1664. MEDLINE identifier: 87109313 Citation REF [5] Y. Sumi, Y. Nakamura, N. Aoki, M. Sakai & M. Muramatsu (1986). Structure of the carboxyl-terminal half of human alpha 2- plasmin inhibitor deduced from that of cDNA. J. Biochem. 100, 1399-1402. MEDLINE identifier: 87137400 Citation REF [6] H.R. Lijnen, W.E. Holmes, B. van Hoef, B. Wiman, H. Rodriguez & D. Collen (1987). Amino-acid sequence of human alpha 2- antiplasmin. Eur. J. Biochem. 166, 565-574. MEDLINE identifier: 87275946 Citation REF [7] B. Wiman & D. Collen (1977). Purification and characterization of human antiplasmin, the fast-acting plasmin inhibitor in plasma. Eur. J. Biochem. 78, 19-26. MEDLINE identifier: 78023887 Citation REF [8] S. Christensen & L. Sottrup-Jensen (1992). Bovine alpha 2- antiplasmin. N-terminal and reactive site sequence. FEBS Lett. 312, 100-104. MEDLINE identifier: 93050153 Citation REF [9] J. Potempa, B.H. Shieh & J. Travis (1988). Alpha-2- antiplasmin: a serpin with two separate but overlapping reactive sites. Science 241, 699-700. MEDLINE identifier: 88290696 Signal (experimentally determined) 112907: 1..27 Propeptide (experimentally determined) 112907: 28..39 Mature chain ALPHA-2-ANTIPLASMIN. 112907: 40..491 (experimentally determined) active site REACTIVE BOND (FOR PLASMIN). 112907: 403..404 (experimentally determined) active site REACTIVE BOND (FOR CHYMOTRYPSIN). 112907: 404..405 (experimentally determined) glycosylation 112907: 126 site glycosylation 112907: 295 site glycosylation 112907: 309 site glycosylation 112907: 316 site Conflict R -> W (IN REF. 1). 112907: 33 (experimentally determined) Conflict L -> G (IN REF. 6). 112907: 49 (experimentally determined) Conflict N -> D (IN REF. 6). 112907: 105 (experimentally determined) Conflict H -> D (IN REF. 4). 112907: 289 (experimentally determined) Conflict S -> G (IN REF. 6). 112907: 408 (experimentally determined) Conflict D -> N (IN REF. 6). 112907: 455 (experimentally determined) Gene Locus: PLI 112907: 1..491 Sequence 491 aa 1 mallwgllvl swsclqgpcs vfspvsamep lgrqltsgpn qeqvspltll 51 klgnqepggq talksppgvc srdptpeqth rlarammaft adlfslvaqt 101 stcpnlilsp lsvalalshl algaqnhtlq rlqqvlhags gpclphllsr 151 lcqdlgpgaf rlaarmylqk gfpikedfle qseqlfgakp vsltgkqedd 201 laninqwvke ategkiqefl sglpedtvll llnaihfqgf wrnkfdpslt 251 qrdsfhldeq ftvpvemmqa rtyplrwfll eqpeiqvahf pfknnmsfvv 301 lvpthfewnv sqvlanlswd tlhpplvwer ptkvrlpkly lkhqmdlvat 351 lsqlglqelf qapdlrgise qslvvsgvqh qstlelsevg veaaaatsia 401 msrmslssfs vnrpflffif edttglplfv gsvrnpnpsa prelkeqqds 451 pgnkdflqsl kgfprgdklf gpdlklvppm eedypqfgsp k
2144993 --------------------------------------------------- Definition M9-R protein - myxoma virus (strain Lausanne) Protein Name: M9-R protein 2144993: [ Whole ] PIR Name: WMVZMX NCBI Seq ID: 2144993 Created Jun 30, 1989 Updated Oct 19, 1995 Citation C. Upton, J.L. Macen, D.S. Wishart & G. McFadden (1990). Myxoma virus and malignant rabbit fibroma virus encode a serpin-like protein important for virus virulence. Virology 179, 618-631. MEDLINE identifier: 91049428 Citation C. Upton, J.L. Macen & G. McFadden (1987). Mapping and sequencing of a gene from myxoma virus that is related to those encoding epidermal growth factor and transforming growth factor alpha. J. Virol. 61, 1271-1275. MEDLINE identifier: 87141350 domain POZ domain homology #label POZ 2144993: 1..104 Sequence 509 aa 1 msrtllrfle dgamsdvtvv agdstflghk vilslhsdyf yrlfngdfts 51 pdtvtldatd davrtvftym yagcdglndr tiddlqsiiv ladylgitkl 101 vdecvrrivs kvdvlncvgv ytfaetyhit dlqraaktfl tellgskeaf 151 eelsqddavi alretrnivd rrsilraill wvrkcpdrie qlkvlvaavd 201 dvddddnvyt iyeryaeelk dmiacplsyn cvvvvdrdry vrlinpdtlw 251 skrvtyirkr aigdrftvvc mnnvlyclgg tldgaptcdv laydlltney 301 slmpemghyr rnasacivng yiyvvggvde enrligsvey wqpgmeewhd 351 apylqanvet atvcyrnelw ivggtvdlyh ptfisavkkl tdnrwmsmep 401 lpeprsgatt vvynnrlyci ggrihggayt nhvynyldes rtwervgdma 451 nvrrnpsccv ynkaiyvlgg ntnavekyng wkwqevgnis typacnntay 501 pffytndei
818903 --------------------------------------------------- Definition serine proteinase inhibitor Protein Name: serine proteinase inhibitor 818903: [ Whole ] NCBI Seq ID: 818903 Updated Oct 19, 1995 Citation REF [1] J Sun, J Rose & P Bird (1995). Gene structure, chromosomal localization, and expression of the murine homologue of human proteinase inhibitor 6 (PI-6) suggests divergence of PI-6 from the ovalbumin serpins. J. Biol. Chem. 270, 16089-16096. MEDLINE identifier: 95332310 Citation REF [2] Data Submission: P.I. Bird (1995). Coding region function: 818902: 68..1204 plasmin/trypsin/thrombin inhibitor. evidence: EXPERIMENTAL. Comments: serpin; similar to human proteinase inhibitor 6 (placental thrombin inhibitor), Swiss-Prot Accession Number P35237. Sequence 378 aa 1 mdplqeangt falnllkilg edssknvfls pmsissalam vfmgakgtta 51 sqmaqalald kcsgngggdv hqgfqsllte vnktgtqyll rtanrlfgdk 101 tcdllasfkd sclkfyeael eeldfqgate esrqhintwv akktedkike 151 vlspgtvnsd tslvlvnaiy fkgnwekqfn kehtrempfk vskneekpvq 201 mmfkkstfkm tyigeiftki lllpyvssel nmiimlpdeh velstvekev 251 tyekfiewtr ldkmdeeeve vflpkfklee nynmndalyk lgmtdafggr 301 adfsgmsskq glflskvvhk afvevneegt eaaaatagmm tvrcmrftpr 351 fcadhpflff ihhvktngil fcgrfssp
1008928 --------------------------------------------------- Protein 1008928: 24..413 Protein 1008928: 1..23 Protein Name: alpha-1-antiproteinase E 1008928: [ Whole ] NCBI Seq ID: 1008928 Updated Oct 5, 1995 Citation Data Submission: A. Saito (1993). Citation A. Saito & H. Sinohara (1995). Rabbit alpha-1-antiproteinase E: a novel recombinant serpin which does not inhibit proteinases. Biochem. J. 307, 369-375. MEDLINE identifier: 95251597 Coding region 1008927: 51..1292 Sequence 413 aa 1 mppsvsrall llaglgcllp gfladeaqet avssheqdhp achriapsla 51 efalslyrev ahesnttnif fspvsialaf amlslgakgd thtqvleglk 101 fnltetaeaq ihdgfrhllh tvnrpdselq laagnalvvh enlklqhkfl 151 edaknlyqse aflvdfrdpe qaktkinshv ekgtrgkivd lvqeldartl 201 lalvnyvffk gkwekpfepe ntkeedfhvd atttvrvpmm srlgmyvmfh 251 cstlastvlr mdykgnatal fllpdegklq hledtlttel iakflakssl 301 rsvtvrfpkl sisgtydlkp llgklgitqv fsnnadlsgi teqeplkvsq 351 alhkavltid ergteaagas fvelipesvp dsitldrpfl fviysheiks 401 plfvgkvvdp tqh
166062 --------------------------------------------------- Definition uterine milk protein Protein Name: uterine milk protein 166062: [ Whole ] NCBI Seq ID: 166062 Updated Sep 29, 1995 Citation REF [1] N.H. Ing & R.M. Roberts (1989). The major progesterone- modulated proteins secreted into the sheep uterus are members of the serpin superfamily of serine protease inhibitors. J. Biol. Chem. 264, 3372-3379. MEDLINE identifier: 89123464 Coding region Comments: precursor (49 could be 166061: 49..1338 64). Sequence 429 aa 1 mshrrmqlal slvfilcglf nsifcekqqh sqqhanlvll kkisafsqkm 51 eahpkafaqe lfkaliaenp kkniifspaa mtitlatlsl gikstmstnh 101 pedlelelkl ldahkclhhl vhlgrelvkq kqlrhqdilf lnskmmanqm 151 llhqirklqk mdiqmidfsd tekakkaish hvaekthtki rdlitdlnpe 201 tilclvnhif fkgilkrafq pnltqkedff lndktkvqvd mmrkteqmly 251 srseelfatm vkmpfkgnvs lilmlpdagh fdnalkklta kraklqkisn 301 frlvhltlpk fkitfdinfk hllpkinlkh llpkidpkht ltttassqhv 351 tlkaplpnle alhqveiels ehalttdtai htdnllkvpa ntkevpvvvk 401 fnrpfllfve deitqtdlfv gqvlnpqve
1083082 --------------------------------------------------- Definition serpin TI - bovine Protein Name: serpin TI 1083082: [ Whole ] PIR Name: S50034 NCBI Seq ID: 1083082 Created Aug 1, 1995 Updated Sep 1, 1995 Citation S. Christensen & L. Sottrup-Jensen (1994). Characterization of two serpins from bovine plasma and milk. Biochem. J. 303, 383-390. MEDLINE identifier: 95071234 Sequence 41 aa 1 lpenvvvkdq mrrvdghtla serertilri ivrvnrpfli a
1144299 --------------------------------------------------- Definition pigment epithelium-derived factor Protein Name: pigment epithelium-derived 1144299: [ Whole ] factor NCBI Seq ID: 1144299 Updated Aug 4, 1995 Citation REF [1] J Tombran-Tink, K Mazuruk, I. Rodriguez, R.E. Kouri, D. Chung, T. Linker & G.J. Chader. Cloning and molecular characterization of the human gene for the neurotrophic serpin PEDF: conservation, polymorphism and hereditary studies. Unpublished Citation REF [2] Data Submission: I. Rodriguez, K. Mazuruk, J. Tombran-Tink & G.J. Chader (1995). Coding region Comments: PEDF. 1144298: 11581..11664 1144298: 14528..14726 1144298: 15707..15862 1144298: 16551..16754 1144298: 19737..19879 1144298: 21219..21429 1144298: 21874..21965 Sequence 362 aa 1 mqalvlllci gallghsscq npasppeegs pdpdstgalv eeedpffkvp 51 vnklaaavsn fgydlyrvrs smspttnvll splsvatals alslgaeqrt 101 esiihralyy dlisspdihg tykelldtvt apqknlksas rivfekklri 151 kssfvaplek sygtrprvlt gnprldlqei nnwvqaqmkg klarstkeip 201 deisilllgv ahfkgqwvtk fdsrktsled fyldeertvr vpmmsdpkav 251 lrygldsdls ckiaqlpltg smsiifflpl kvtqnltlie esltsefihd 301 idrelktvqa vltvpklkls yegevtkslq emklqslfds pdfskitgkp 351 ikltqggtpg wl
439153 --------------------------------------------------- Definition serine protease inhibitor Protein Name: serine protease inhibitor 439153: [ Whole ] NCBI Seq ID: 439153 Updated Aug 3, 1995 Citation REF [1] C Huang, M Lee, F Huang & G Chang (1995). A protease inhibitor of the serpin family is a major protein in carp perimeningeal fluid: II. cDNA cloning, sequence analysis, and Escherichia coli expression. J. Neurochem. 64, 1721-1727. MEDLINE identifier: 95198028 Coding region function: protease inhibitor. 439152: 34..1266 evidence: experimental. Comments: p62. Sequence 410 aa 1 mawaaphegh dhdghpadhy hhlhhgkdea hpshsgedac hllsphnadf 51 afslykklal hpdaqgknif fspvgismal smlavgakgs tlsqiysslg 101 ysglkaqqvn egyehlihml ghsqdtmqle agagvaireg fkvvdqflkd 151 vqhyynseaf svdfskpeia aeeinqfiak ktndkitdmv kdldsdmvmm 201 linymyfrgk wdkpfeaqlt hkaefkvdkd ttvqvdmmkr tgrydiyqdp 251 vnqttvmmvp ykgntsmmiv lpdegkmkdv eesicrhhlk nwhdklfrss 301 vdlfmpkfsi satsklndil temgvtdafs dtadfsgmte elkvkvsqvv 351 hkavlsvdek gteaaaatti eimpmslpgt vmlnrpflvl ivedttksil 401 fmgkitnptv
213046 --------------------------------------------------- Definition alpha-1 antitrypsin Protein Name: alpha-1 antitrypsin 213046: [ Whole ] NCBI Seq ID: 213046 Updated Aug 3, 1995 Citation REF [1] C Huang, M Lee, F Huang & G Chang (1995). A protease inhibitor of the serpin family is a major protein in carp perimeningeal fluid: II. cDNA cloning, sequence analysis, and Escherichia coli expression. J. Neurochem. 64, 1721-1727. MEDLINE identifier: 95198028 Coding region function: protease inhibitor. 213045: 137..1255 evidence: experimental. Sequence 372 aa 1 mpatcllhtm ltlpspstrn lrsiqmprar tfsspsryrn gfehagcrcq 51 gstlsqiyss lgysglqasq vnegyehlih mlghsreamq leagagvair 101 egfkvvdqfl kdvqhyynse afsvdfskpe iaaeeinqfi akktndkitn 151 mvkdldsdtv mmlinymyfr gkwdkpfdaq lthkadfkvd edttvqvdmm 201 krtgrydiyq dpvnqttvmm vpykgntsmm iifpddgkmk eleesisrhh 251 lknwhdklfr ssvdlfmpkf sitatsklkg iledmgvtda fgdtadlsgl 301 teevkvkvsq vvhkavlsvd ekgteaaaat tieimpmslp dtvilnrpfl 351 vlivedttks ilfmgkitnp te
87514 --------------------------------------------------- Definition glia-derived nexin I alpha precursor - human Protein Name: glia-derived nexin I alpha 87514: [ Whole ] precursor PIR Name: A27496 NCBI Seq ID: 87514 Comment Two forms, alpha and beta, have been identified. Created Jun 30, 1988 Updated Jul 28, 1995 Citation J. Sommer, S.M. Gloor, G.F. Rovelli, J. Hofsteenge, H. Nick, R. Meier & D. Monard (1987). cDNA sequence coding for a rat glia-derived nexin and its homology to members of the serpin superfamily. Biochemistry 26, 6407-6410. MEDLINE identifier: 88107544 Citation M. McGrogan, J. Kennedy, M.P. Li, C. Hsu, R.W. Scott, C.C. Simonsen & J.B. Baker (1988). Molecular cloning and expression of two forms of human protease nexin I. Bio/Technology 6, 172-177. domain signal sequence 87514: 1..19 product glia-derived nexin I alpha 87514: 20..397 binding site carbohydrate (Asn) (covalent) 87514: 118 binding site carbohydrate (Asn) (covalent) 87514: 159 inhibit site Arg (thrombin, urokinase) 87514: 364 Sequence 397 aa 1 mnwhlplfll asvtlpsics hfnplsleel gsntgiqvfn qivksrphdn 51 ivisphgias vlgmlqlgad grtkkqlamv mrygvngvgk ilkkinkaiv 101 skknkdivtv anavfvknas eievpfvtrn kdvfqcevrn vnfedpasac 151 dsinawvkne trdmidnlls pdlidgvltr lvlvnavyfk glwksrfqpe 201 ntkkrtfvaa dgksyqvpml aqlsvfrcgs tsapndlwyn fielpyhges 251 ismlialpte sstplsaiip histktidsw msimvpkrvq vilpkftava 301 qtdlkeplkv lgitdmfdss kanfakitrs enlhvshilq kakievsedg 351 tkasaattai liarssppwf ivdrpflffi rhnptgavlf mgqinkp
1078955 --------------------------------------------------- Definition intracellular coagulation inhibitor LICI precursor - horseshoe crab (Tachypleus tridentatus) Protein Name: intracellular coagulation 1078955: [ Whole ] inhibitor LICI precursor PIR Name: A53120 NCBI Seq ID: 1078955 Created Jul 7, 1995 Updated Jul 7, 1995 Citation Y. Miura, S. Kawabata & S. Iwanaga (1994). A Limulus intracellular coagulation inhibitor with characteristics of the serpin superfamily. Purification, characterization, and cDNA cloning. J. Biol. Chem. 269, 542-547. MEDLINE identifier: 94103268 domain signal sequence 1078955: 1..24 product intracellular coagulation 1078955: 25..418 inhibitor LICI (experimentally determined) Sequence 418 aa 1 mklgdwkfcl llfqlmfltn vclsdlsfnp ykwpvnqlrr vigavkvtnt 51 snyfgfslye nlnsngnvfi spyslasvma mlylgargvt knemdltlgy 101 nsvnlnsedl vlgfqqslll lnaeskeyql etanslmiqn tfnildnykr 151 mledkfganv qdvdfinkae lvqryinawv afktknkipi llneplkpet 201 rlaffnavyf kgvwetkfds altrratfyn ngyvptqvpm mmlrgifpfa 251 yvsslrsyvl elpykghevs mllllpkdrn gisdlerdls sssldsvtsn 301 lreigvlvti pkfkleetye ddlkqslesm gmtslfsean anlegitghr 351 dlfvtkithr tlievneegt easgissvva gvrsgwkrpt ftadhpfvff 401 irhnrsgiil fmgrvsql
1683364 ---------------------------------------------------
Definition trypsin inhibitor, TI=serpin {N-terminal, reactive-site loop}
[cattle, plasma, milk, Peptide Partial, 41 aa 2 segments]
Segments 861517 trypsin inhibitor, TI=serpin {N-terminal,
reactive-site loop} [cattle, plasma, milk,
Peptide Partial, 20 aa, segment 1 of 2]
861518 trypsin inhibitor, TI=serpin {N-terminal,
reactive-site loop} [cattle, plasma, milk,
Peptide Partial, 21 aa, segment 2 of 2]
NCBI Journal Scan Mol ID: 361654
NCBI Seq ID: 1683364
Updated Jun 14, 1995
Citation Christensen,S. & Sottrup-Jensen,L. (1994). Characterization
of two serpins from bovine plasma and milk. Biochem. J. 303 (
Pt 2), 383-90. MEDLINE identifier: 95071234
Protein Names: trypsin inhibitor; TI 861517: 1..20
Description: serpin. [ Gap ]
*: Partial 861518: 1..21
861517 ---------------------------------------------------
Definition trypsin inhibitor, TI=serpin {N-terminal, reactive-site loop}
[cattle, plasma, milk, Peptide Partial, 20 aa, segment 1 of 2]
NCBI Journal Scan Seq ID: 161332
NCBI Seq ID: 861517
Created Jun 14, 1995
Citation MEDLINE identifier: 95071234
Figure Fig. 3a, "Bovine TI (N-terminal)"
Numbered from 1
Shown in alignment group 1
Sequence 20 aa
1 lpenvvvkdq mrrvdghtla
861518 ---------------------------------------------------
Definition trypsin inhibitor, TI=serpin {N-terminal, reactive-site loop}
[cattle, plasma, milk, Peptide Partial, 21 aa, segment 2 of 2]
NCBI Journal Scan Seq ID: 161337
NCBI Seq ID: 861518
Created Jun 14, 1995
Citation MEDLINE identifier: 95071234
Figure Fig. 3b, "Bovine TI (RSL)"
Numbered from 1
Shown in alignment group 2
Sequence 21 aa
1 serertilri ivrvnrpfli a