| IED ID | IndEnz0002006022 |
| Enzyme Type ID | protease006022 |
| Protein Name |
Venom prothrombin activator oscutarin-C catalytic subunit vPA EC 3.4.21.6 Factor VII activator Snake venom serine protease SVSP Venom coagulation factor Xa-like protease Cleaved into: Oscutarin-C catalytic subunit light chain; Oscutarin-C catalytic subunit heavy 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 | MAPQLLLCLILTFLWSLPEAESNVFLKSKVANRFLQRTKRANSLYEEFRSGNIERECIEERCSKEEAREVFEDDEKTETFWNVYVDGDQCSSNPCHYRGTCKDGIGSYTCTCLSGYEGKNCERVLYKSCRVDNGNCWHFCKPVQNDIQCSCAEGYLLGEDGHSCVAGGNFSCGRNIKTRNKREASLPDFVQSQNAILLKKSDNPSPDIRIVNGMDCKLGECPWQAVLVDEKEDAFCGGTILSPIYVLTAAHCINQTKMISVVVGEINISRKNPGRLLSVDKIYVHQKFVPPKKGYEFYEKFDLVSYDYDIAILQMKTPIQFSENVVPACLPTADFANQVLMKQDFGIVSGFGRIFEKGPQSKTLKVLKVPYVDRHTCMLSSESPITPTMFCAGYDTLPRDACQGDSGGPHITAYRDTHFITGIVSWGEGCAQTGKYGVYTKVSKFILWIKRIMRQKLPSTESSTGRL |
| Enzyme Length | 467 |
| Uniprot Accession Number | Q58L96 |
| Absorption | |
| Active Site | ACT_SITE 251; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 309; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 406; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Activated by calcium and negatively charged phospholipids. {ECO:0000269|PubMed:3531198}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.; EC=3.4.21.6; Evidence={ECO:0000269|PubMed:3531198}; |
| DNA Binding | |
| EC Number | 3.4.21.6 |
| Enzyme Function | FUNCTION: Snake prothrombin (F2) activator that attacks the hemostatic system of prey. This catalytic subunit is functionally similar to blood coagulation factor Xa. For prothrombin activation, it requires a non-catalytic subunit present in the venom, which is similar to coagulation factor Va, to be fully active. In contrast to the 8 other snake venoms tested, this protein is the only one to also activate factor VII (F7). However, in contrast to prothrombin activation, the factor Va-like subunit is not essential for this activation. {ECO:0000269|PubMed:1604437, ECO:0000269|PubMed:3531198, ECO:0000269|PubMed:6986908}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (2); Disulfide bond (12); Domain (4); Glycosylation (2); Modified residue (11); Propeptide (2); Signal peptide (1); Site (1) |
| Keywords | Blood coagulation cascade activating toxin;Calcium;Cleavage on pair of basic residues;Disulfide bond;EGF-like domain;Gamma-carboxyglutamic acid;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Protease;Prothrombin activator;Repeat;Secreted;Serine protease;Signal;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1604437, ECO:0000269|PubMed:3531198, ECO:0000269|PubMed:6986908}. |
| Modified Residue | MOD_RES 46; /note=4-carboxyglutamate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00463; MOD_RES 47; /note=4-carboxyglutamate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00463; MOD_RES 54; /note=4-carboxyglutamate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00463; MOD_RES 56; /note=4-carboxyglutamate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00463; MOD_RES 59; /note=4-carboxyglutamate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00463; MOD_RES 60; /note=4-carboxyglutamate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00463; MOD_RES 65; /note=4-carboxyglutamate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00463; MOD_RES 66; /note=4-carboxyglutamate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00463; MOD_RES 69; /note=4-carboxyglutamate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00463; MOD_RES 72; /note=4-carboxyglutamate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00463; MOD_RES 75; /note=4-carboxyglutamate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00463 |
| Post Translational Modification | PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation. These residues are essential for the binding of calcium. {ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:3531198}. |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 52,454 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |