| IED ID | IndEnz0002004622 |
| Enzyme Type ID | protease004622 |
| Protein Name |
Venom prothrombin activator omicarin-C non-catalytic subunit vPA Venom coagulation factor Va-like protein Cleaved into: Omicarin-C non-catalytic subunit heavy chain; Omicarin-C non-catalytic subunit light chain |
| Gene Name | |
| Organism | Oxyuranus microlepidotus (Inland taipan) (Diemenia microlepidota) |
| 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 microlepidotus (Inland taipan) (Diemenia microlepidota) |
| Enzyme Sequence | MGRYSVSPVPKCLLLMFLGWSGLKYYQVNAAQLREYRIAAQLEDWDYNPQPEELSRLSESELTFKKIVYREYELDFKQEKPRDELSGLLGPTLRGEVGDILIIYFKNFATQPVSIHPQSAVYNKWSEGSSYSDGTSDVERLDDAVPPGQSFKYVWNITAEIGPKKADPPCLTYAYYSHVNMVRDFNSGLIGALLICKEGSLNANGAQKFFNREYVLMFSVFDESKNWYRKPSLQYTINGFANGTLPDVQACAYDHISWHLIGMSSSPEIFSVHFNGQTLEQNHYKVSTINLVGGASVTANMSVSRTGKWLISSLVAKHLQAGMYGYLNIKDCGHPNTLTRKLSFRELRRIMNWEYFIAAEEITWDYAPEIPSSVDRRYKAQYLDNFSNFIGKKYKKAVFRQYEDGNFTKPTYAIWPKERGILGPVIKAKVRDTVTIVFKNLASRPYSIYVHGVSVSKDAEGAIYPSDPKENITHGKAVEPGQVYTYKWTVLDTDEPTVKDSECITKLYHSAVDMTRDIASGLIGPLLVCKLKALSVKGVQNKADVEQHAVFAVFDENKSWYLEDNIKKYCSNPSSVKKDDPKFYKSNVMYTLNGYASDRTEVLGFHQSEVVQWHLTSVGTVDEIVPVHLSGHTFLSKGKHQDILNLFPMSGESATVTMDNLGTWLLSSWGSCEMSNGMRLRFLDANYDDEDEGNEEEEEDDGDIFADIFSPPEVVKKKEEVPVNFVPDPESDALAKELGLLDDEDNPEQSRSEQTEDDEEQLMIASVLGLRSFKGSVAEEELKHTALALEEDAHASDPRIDSNSARNSDDIAGRYLRTINRRNKRRYYIAAEEVLWDYSPIGKSQVRSLPAKTTFKKAIFRSYLDDTFQTPSTGGEYEKHLGILGPIIRAEVDDVIEVQFRNLASRPYSLHAHGLLYEKSSEGRSYDDNSPELFKKDDAIMPNGTYTYVWQVPPRSGPTDNTEKCKSWAYYSGVNPEKDIHSGLIGPILICQKGMIDKYNRTIDIREFVLFFMVFDEEKSWYFPKSDKSTCEEKLIGVQSSHHTFPAINGIPYQLQGLMMYKDENVHWHLLNMGGPKDIHVVNFHGQTFTEEGREDNQLGVLPLLPGTFASIKMKPSKIGTWLLETEVGENQERGMQALFTVIDKDCKLPMGLASGIIQDSQISASGHVEYWEPKLARLNNTGMFNAWSIIKKEHEHPWIQIDLQRQVVITGIQTQGTVQLLKHSYTVEYFVTYSKDGQNWITFKGRHSETQMHFEGNSDGTTVKENHIDPPIIARYIRLHPTKFYNTPTFRIELLGCEVEGCSVPLGMESGAIKNSEITASSYKKTWWSSWEPFLARLNLEGGTNAWQPEVNNKDQWLQIDLQHLTKITSIITQGATSMTTAMYVKTFSIHYTDDNSTWKPYLDVRTSMEKVFTGNINSDGHVKHFFKPPILSRFIRIIPKTWNQYIALRIELFGCEVF |
| Enzyme Length | 1460 |
| Uniprot Accession Number | Q58L90 |
| 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. This non-catalytic subunit is functionally similar to blood coagulation factor V. It serves as a critical cofactor for the prothrombinase activity of the catalytic subunit, which is similar to the blood coagulation factor X. The complex converts prothrombin to thrombin by sequential cleavage at two positions, Arg-320 followed by Arg-271. Cleavage at Arg-320 produces an active intermediate known as meizothrombin. Meizothrombin is the 'second' substrate for prothrombinase, and it docks in an altered manner to present the second cleavage site (271). Cleavage at Arg-271 releases active thrombin from its pro-fragment. 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. {ECO:0000250|UniProtKB:Q7SZN0}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (2); Disulfide bond (7); Domain (11); Glycosylation (11); Metal binding (8); Propeptide (1); Region (2); Signal peptide (1); Site (2) |
| Keywords | Blood coagulation cascade activating toxin;Calcium;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Metal-binding;Prothrombin activator;Repeat;Secreted;Signal;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| 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, omicarin-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:0000250 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 166,082 |
| 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 |