| IED ID | IndEnz0002006994 |
| Enzyme Type ID | protease006994 |
| Protein Name |
Venom prothrombin activator notanarin-D vPA EC 3.4.21.6 Venom coagulation factor Xa-like protease Cleaved into: Notanarin-D light chain; Notanarin-D heavy chain Fragments |
| Gene Name | |
| Organism | Notechis scutatus niger (Peninsula tiger snake) (Notechis ater niger) |
| 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 Notechis Notechis scutatus (mainland tiger snake) Notechis scutatus niger (Peninsula tiger snake) (Notechis ater niger) |
| Enzyme Sequence | SNSLFEEVRPIVNGMDCKLG |
| Enzyme Length | 20 |
| Uniprot Accession Number | P0CY52 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| 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; |
| DNA Binding | |
| EC Number | 3.4.21.6 |
| Enzyme Function | FUNCTION: Snake prothrombin activator that attacks the hemostatic system of prey. This protein is functionally similar to blood coagulation factor Xa. {ECO:0000269|PubMed:12403650}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (2); Domain (2); Modified residue (2); Non-adjacent residues (1); Non-terminal residue (1); Sequence uncertainty (1) |
| Keywords | Blood coagulation cascade activating toxin;Calcium;Direct protein sequencing;Disulfide bond;EGF-like domain;Gamma-carboxyglutamic acid;Hemostasis impairing toxin;Hydrolase;Protease;Prothrombin activator;Secreted;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12403650}. |
| Modified Residue | MOD_RES 6; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:12403650"; MOD_RES 7; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:12403650" |
| 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:12403650}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 2,209 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |