| IED ID | IndEnz0002011037 |
| Enzyme Type ID | protease011037 |
| Protein Name |
Snake venom metalloproteinase basparin-A SVMP EC 3.4.24.- Fragments |
| Gene Name | |
| Organism | Bothrops asper (Terciopelo) |
| 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 Viperidae Crotalinae (pit vipers) Bothrops Bothrops asper (Terciopelo) |
| Enzyme Sequence | SHDNAQLLTAIKAYIATMCDPKMAVIMAHEIGHGGYYGYCRKIPCAPEDVKDDDIGMVLPGTK |
| Enzyme Length | 63 |
| Uniprot Accession Number | P84035 |
| Absorption | |
| Active Site | ACT_SITE 30; /evidence="ECO:0000250|UniProtKB:P30431, ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Clotting activity on human plasma is not abrogated by the plasma proteinase inhibitors alpha(2) macroglobulin and murinoglobulin. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Snake venom zinc metalloproteinase that catalyzes the conversion of prothrombin (F2) to alpha-thrombin through formation of a thrombin intermediate, without requiring additional cofactors. Also inhibits collagen-dependent platelet aggregation in vitro, an effect that does not depend on proteolytic activity. In vivo, at low doses, induces defibrin(ogen)ation when injected intravenously or intramuscularly into mice. At higher doses, causes sudden death by intravenous administration due to numerous occluding thrombi in pulmonary vessels. {ECO:0000269|PubMed:13679078}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (1); Domain (1); Metal binding (2); Non-adjacent residues (5); Non-terminal residue (2) |
| Keywords | Blood coagulation cascade activating toxin;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Fibrinolytic toxin;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Prothrombin activator;Secreted;Toxin;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:13679078}. |
| Modified Residue | |
| Post Translational Modification | PTM: Glycosylated. {ECO:0000269|PubMed:13679078}.; PTM: The N-terminus is blocked. {ECO:0000269|PubMed:13679078}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 6,839 |
| Kinetics | |
| Metal Binding | METAL 29; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 33; /note=Zinc; catalytic; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |