GET /api/protein/reviewed/Q7SZN0/?format=api
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{
"metadata": {
"accession": "Q7SZN0",
"id": "FA5V_PSETE",
"source_organism": {
"taxId": "8673",
"scientificName": "Pseudonaja textilis",
"fullName": "Pseudonaja textilis (Eastern brown snake)"
},
"name": "Venom prothrombin activator pseutarin-C non-catalytic subunit",
"description": [
"Snake prothrombin activator that attacks the hemostatic system of prey. This non-catalytic subunit is functionally similar to blood coagulation factor V (PubMed:12362232, PubMed:23869089). It serves as a critical cofactor for the prothrombinase activity of the catalytic subunit, which is similar to the blood coagulation factor X (PubMed:12362232, PubMed:23869089). The complex converts prothrombin to thrombin by sequential cleavage at two positions, Arg-320 followed by Arg-271 (PubMed:23869089). Cleavage at Arg-320 produces an active intermediate known as meizothrombin (PubMed:23869089). Meizothrombin is the 'second' substrate for prothrombinase, and it docks in an altered manner to present the second cleavage site (271) (PubMed:23869089). Cleavage at Arg-271 releases active thrombin from its pro-fragment (PubMed:23869089). This order of events is reversed if the protease component of prothrombinase is used on its own, suggesting that the 271 site is inherently more accessible to proteolysis (PubMed:23869089). The complex converts prothrombin to thrombin in presence but also in the absence of membrane (PubMed:23869089)"
],
"length": 1460,
"sequence": "MGRYSVSPVPKCLLLMFLGWSGLKYYQVNAAQLREYHIAAQLEDWDYNPQPEELSRLSESDLTFKKIVYREYELDFKQEEPRDALSGLLGPTLRGEVGDSLIIYFKNFATQPVSIHPQSAVYNKWSEGSSYSDGTSDVERLDDAVPPGQSFKYVWNITAEIGPKKADPPCLTYAYYSHVNMVRDFNSGLIGALLICKEGSLNANGSQKFFNREYVLMFSVFDESKNWYRKPSLQYTINGFANGTLPDVQACAYDHISWHLIGMSSSPEIFSVHFNGQTLEQNHYKVSTINLVGGASVTADMSVSRTGKWLISSLVAKHLQAGMYGYLNIKDCGNPDTLTRKLSFRELMKIKNWEYFIAAEEITWDYAPEIPSSVDRRYKAQYLDNFSNFIGKKYKKAVFRQYEDGNFTKPTYAIWPKERGILGPVIKAKVRDTVTIVFKNLASRPYSIYVHGVSVSKDAEGAIYPSDPKENITHGKAVEPGQVYTYKWTVLDTDEPTVKDSECITKLYHSAVDMTRDIASGLIGPLLVCKHKALSVKGVQNKADVEQHAVFAVFDENKSWYLEDNIKKYCSNPSAVKKDDPKFYKSNVMYTLNGYASDRTEVLRFHQSEVVQWHLTSVGTVDEIVPVHLSGHTFLSKGKHQDILNLFPMSGESATVTMDNLGTWLLSSWGSCEMSNGMRLRFLDANYDDEDEGNEEEEEDDGDIFADIFIPSEVVKKKEEVPVNFVPDPESDALAKELGLIDDEGNPIIQPRREQTEDDEEQLMKASMLGLRSFKGSVAEEELKHTALALEEDAHASDPRIDSNSARNPDDIAGRYLRTINRGNKRRYYIAAEEVLWDYSPIGKSQVRSRAAKTTFKKAIFRSYLDDTFQTPSTGGEYEKHLGILGPIIRAEVDDVIEIQFKNLASRPYSLHAHGLLYEKSSEGRSYDDKSPELFKKDDAIMPNGTYTYVWQVPPRSGPTDNTEKCKSWAYYSGVNPEKDIHSGLIGPILICQKGMIDKYNRTIDIREFVLFFMVFDEEKSWYFPKSDKSTCEEKLIGVQSLHTFPAINGIPYQLQGLTMYKDENVHWHLLNMGGPKDIHVVNFHGQTFTEEGREDNQLGVLPLLPGTFASIKMKPSKIGTWLLETEVGENQERGMQALFTVIDKDCKLPMGLASGIIQDSQISASGHVGYWEPKLARLNNTGKYNAWSIIKKEHEHPWIQIDLQRQVVITGIQTQGTVQLLQHSYTVEYFVTYSEDGQNWITFKGRHSETQMHFEGNSDGTTVKENHIDPPIIARYIRLHPTKFYNRPTFRIELLGCEVEGCSVPLGMESGAIKNSEITASSYKKTWWSSWEPSLARLNLEGGTNAWQPEVNNKDQWLQIDLQHLTKITSIITQGATSMTTSMYVKTFSIHYTDDNSTWKPYLDVRTSMEKVFTGNINSDGHVKHFFKPPILSRFIRIIPKTWNQYIALRIELFGCEVF",
"proteome": "UP000472273",
"gene": null,
"go_terms": [
{
"identifier": "GO:0005507",
"name": "copper ion binding",
"category": {
"code": "F",
"name": "molecular_function"
}
}
],
"protein_evidence": 1,
"source_database": "reviewed",
"is_fragment": false,
"in_alphafold": true,
"in_bfvd": false,
"ida_accession": "646f5e9a260b46ae4a010b420737a969945f9f16",
"counters": {
"domain_architectures": 120,
"entries": 26,
"isoforms": 0,
"proteomes": 1,
"sets": 4,
"structures": 1,
"taxa": 1,
"dbEntries": {
"ssf": 2,
"cathgene3d": 2,
"cdd": 6,
"pfam": 2,
"smart": 1,
"profile": 1,
"pirsf": 1,
"panther": 1,
"prosite": 3,
"interpro": 7
},
"proteome": 1,
"taxonomy": 1,
"similar_proteins": 120
}
}
}