| IED ID | IndEnz0002012653 |
| Enzyme Type ID | protease012653 |
| Protein Name |
Zinc metalloproteinase-disintegrin-like ammodytagin EC 3.4.24.- Snake venom metalloproteinase SVMP Fragments |
| Gene Name | |
| Organism | Vipera ammodytes ammodytes (Western sand viper) |
| 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 Viperinae (vipers) Vipera Vipera ammodytes (Nose-horned viper) Vipera ammodytes ammodytes (Western sand viper) |
| Enzyme Sequence | KSAAXVTLDLFGDWRAKRHDNAQLLTGINLNGQTLGIAFMSKXSVGLIQDYXKSYLLVASVMAHELGHNLGMEHDDGNCICPAKCIDNKPLRTDIVSPAVCGNYFVELTPGSQCADGVCCDQCRKAGVTVAPDLCFDYNQLGTEDKFTHSPDDPDYGMVDLGTKCADGKVCNSNRQCVDVNTAY |
| Enzyme Length | 184 |
| Uniprot Accession Number | P0DJE2 |
| Absorption | |
| Active Site | ACT_SITE 65; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA, DTT and zinc ions. Partially inhibited by L-cysteine. Not inhibited by 2-propanol or PMSF. Activity is enhanced by calcium or magnesium ions. {ECO:0000269|PubMed:21933678}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Snake venom zinc metalloprotease that has fibrinogenolytic and hemorrhagic activities in mouse and rats. Hydrolyzes the Aalpha-chain (FGA) and more slowly the Bbeta-chain of fibrinogen (FGB), without affecting the gamma-chain. Its hemorrhagic activity results of its involvement in cleavage of basal membrane components (nidogen and fibronectin but not laminin) and depletion of fibrinogen, prothrombin (F2) and factor X (F10) in blood circulation. Also possess potent azocaseinolytic activity and cleaves insulin B-chain, hydrolyzing it at positions Gln(4)-His(5), His(10)-Leu(11) and Tyr(16)-Leu(17). {ECO:0000269|PubMed:21933678}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (2); Domain (2); Metal binding (9); Non-adjacent residues (6); Non-terminal residue (1); Sequence uncertainty (7) |
| Keywords | Calcium;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Glycoprotein;Hemorrhagic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Toxin;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | PTM: The N-terminus is blocked.; PTM: N-glycosylated. {ECO:0000269|PubMed:21933678}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 19,879 |
| Kinetics | |
| Metal Binding | METAL 20; /note=Calcium 1; /evidence=ECO:0000250; METAL 64; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 68; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 74; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 88; /note=Calcium 1; /evidence=ECO:0000250; METAL 100; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 103; /note=Calcium 2; /evidence=ECO:0000250; METAL 105; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 107; /note=Calcium 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.B38; |