| IED ID | IndEnz0002004990 |
| Enzyme Type ID | protease004990 |
| Protein Name |
Venom prothrombin activator oscutarin-C non-catalytic subunit vPA Venom coagulation factor Va-like protein Cleaved into: Oscutarin-C non-catalytic subunit heavy chain; Oscutarin-C non-catalytic subunit light chain |
| Gene Name | |
| Organism | Oxyuranus scutellatus (Coastal taipan) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Lepidosauria (lepidosaurs) Squamata (squamates) Bifurcata (split-tongued squamates) Unidentata Episquamata Toxicofera Serpentes (snakes) Colubroidea Elapidae Acanthophiinae Oxyuranus Oxyuranus scutellatus (Coastal taipan) |
| Enzyme Sequence | MGRYSVSPVPKCLLLMFLGWSGLKYYQVNAAQLREYRLAAQLEDWDYNPQPEELSRLSESDLTFKKIVYREYELDFKQEKPRDELSGLLGPTLRGEVGDSLIIYFKNFATQPVSIHPQSAVYNKWSEGSSYSDGTSDVERLDDAVPPGQSFKYVWNITAEIGPKKADPPCLTYAYYSHVNMVRDFNSGLIGALLICKEGSLNADGAQKFFNREYVLMFSVFDESKNWYRKPSLQYTINGFANGTLPDVQACAYDHISWHLIGMSSSPEIFSVHFNGQTLEQNHYKVSTINLVGGASVTANMSVSRTGKWLISSLVAKHLQAGMYGYLNIKDCGNPDTLTRKLSFRERRRIMKWEYFIAAEEITWDYAPEIPSSVDRRYKAQYLDNFSNFIGKKYKKAVFRQYEDSNFTKPTYAIWPKERGILGPVIKAKVRDTVTIVFKNLASRPYSIYVHGVSVSKDAEGAVYPSDPKENITHGKAVEPGQVYTYKWTVLDTDEPTVKDSECITKLYHSAVDMTRDIASGLIGPPLVCKRKALSIRGVQNKADVEQHAVFAVFDENKSWYLEDNIKKYCSNPSSVKKDDPKFYKSNVMYTLNGYASDRTEVWGFHQSEVVEWHLTSVGTVDEIVPVHLSGHTFLSKGKHQDILNLFPMSGESATVTMDNLGTWLLSSWGSCEMSNGMRLRFLDANYDDEDEGNEEEEEDDGDIFADIFNPPEVVIKKEEVPVNFVPDPESDALAKELGLFDDEDNPKQSRSEQTEDDEEQLMIASMLGLRSFKGSVAEEELKHTALALEEDAHASDPRIDSNSAHNSDDIAGRYLRTINRRNKRRYYIAAEEVLWDYSPIGKSQVRSLPAKTTFKKAIFRSYLDDTFQTPSTGGEYEKHLGILGPIIRAEVDDVIEVQFRNLASRPYSLHAHGLLYEKSSEGRSYDDNSPELFKKDDAIMPNGTYTYVWQVPPRSGPTDNTEKCKSWAYYSGVNPEKDIHSGLIGPILICQKGMIDKYNRTIDIREFVLFFMVFDEEKSWYFPKSDKSTCEEKLIGVQSRHTFPAINGIPYQLQGLMMYKDENVHWHLLNMGGPKDVHVVNFHGQTFTEEGREDNQLGVLPLLPGTFASIKMKPSKIGTWLLETEVGENQERGMQALFTVIDKDCKLPMGLASGIIQDSQISASGHVGYWEPKLARLNNTGMFNAWSIIKKEHEHPWIQIDLQRQVVITGIQTQGTVQLLKHSYTVEYFVTYSKDGQNWITFKGRHSKTQMHFEGNSDGTTVKENHIDPPIIARYIRLHPTKFYNTPTFRIELLGCEVEGCSVPLGMESGAIKDSEITASSYKKTWWSSWEPFLARLNLKGRTNAWQPKVNNKDQWLQIDLQHLTKITSIITQGATSMTTSMYVKTFSIHYTDDNSTWKPYLDVRTSMEKVFTGNINSDGHVKHFFNPPILSRFIRIIPKTWNQYIALRIELFGCEVF |
| Enzyme Length | 1459 |
| Uniprot Accession Number | Q58L91 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Snake prothrombin activator that attacks the hemostatic system of prey (PubMed:6986908, PubMed:3531198). This non-catalytic subunit is functionally similar to blood coagulation factor V (PubMed:6986908, PubMed:3531198). It serves as a critical cofactor for the prothrombinase activity of the catalytic subunit, which is similar to the blood coagulation factor X (PubMed:6986908, PubMed:3531198). The complex converts prothrombin to thrombin by sequential cleavage at two positions, Arg-320 followed by Arg-271 (PubMed:6986908, PubMed:3531198). Cleavage at Arg-320 produces an active intermediate known as meizothrombin (PubMed:6986908, PubMed:3531198). Meizothrombin is the 'second' substrate for prothrombinase, and it docks in an altered manner to present the second cleavage site (271) (PubMed:6986908, PubMed:3531198). Cleavage at Arg-271 releases active thrombin from its pro-fragment (PubMed:6986908, PubMed:3531198). 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:6986908, PubMed:3531198). {ECO:0000269|PubMed:3531198, ECO:0000269|PubMed:6986908}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (2); Compositional bias (1); Disulfide bond (7); Domain (11); Glycosylation (11); Metal binding (8); Propeptide (1); Region (2); Sequence conflict (6); Signal peptide (1); Site (2) |
| Keywords | Blood coagulation cascade activating toxin;Calcium;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Metal-binding;Prothrombin activator;Repeat;Secreted;Signal;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15993914, ECO:0000269|PubMed:3531198, ECO:0000269|PubMed:6986908}. |
| Modified Residue | |
| Post Translational Modification | PTM: In physiological conditions, blood coagulation factor V and factor Va are inactivated by activated protein C (APC) through proteolytic degradation of the heavy chain. However, oscutarin-C non-catalytic subunit (factor V-like protein) retains its full activity even at high concentration of APC. This has two explanations: this protein has only one of the three cleavage sites present in factor V that are targeted by the APC for inactivation, and the binding with the catalytic subunit protect the cleavage site from inactivation (By similarity). {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..30; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 166,240 |
| Kinetics | |
| Metal Binding | METAL 124; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q7SZN0; METAL 139; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q7SZN0; METAL 142; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q7SZN0; METAL 143; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q7SZN0; METAL 919; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q7SZN0; METAL 934; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q7SZN0; METAL 937; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q7SZN0; METAL 938; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q7SZN0 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.6; |