| IED ID | IndEnz0002013392 |
| Enzyme Type ID | protease013392 |
| Protein Name |
Zinc metalloproteinase-disintegrin-like VLAIP-B EC 3.4.24.- Snake venom metalloproteinase SVMP |
| Gene Name | |
| Organism | Macrovipera lebetina (Levantine viper) (Vipera lebetina) |
| 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) Macrovipera Macrovipera lebetina (Levantine viper) (Vipera lebetina) |
| Enzyme Sequence | MMQVLLVTICLAVFPYQGSSIILESGNVNDYEVVYPQKITALPKGAIQQPEQKYEDAIKYEFKVNGKPVVLHLEKNKGLFSEDYSETHYTPDGREITINPPVEDHCYYHGRIQNDADSTASISACNGLKGHFKLQGEMYLIEPLRIPDSEAHAIYKYENIEKEDEAPKMCGVTQTNWESDEPIKASQLNLTPEQRTYLKSKKYVELVIVADYIMFWKYDRSLSTIRTRIYEIVNTLNVIYRFLNIYIALVAVEIWSKGDLINVTSSAYDTLDSFGEWRERDLLNRKRHDNAQLLTGINFNGPSAGRGFVGRMCQPKYSVGIVQDHSKIYLLVASAMAHEMGHNLGMDHDRIDCTCGAKSCIMSGILRCETSYLFSDCSREEHRKYLINKMPQCILNKPLKTDIVSPAVCGNYFVEVGEECDCGSPANCQDRCCDAATCKLRPGAQCGDGVCCYQCKFRRAGTVCRPANGECDVSDLCTGQSAECPTDQFQRNGQPCQNNKGYCYNGTCPIMEKQCISLFGASATVAQDSCFQFNRRGNHYGYCRKENNTKIACAPEDVKCGRLYCLDNSSGHKNPCQIYYIPSDENKGMVDPGTKCGDGMVCSNGKCVDVTIAY |
| Enzyme Length | 614 |
| Uniprot Accession Number | Q4VM07 |
| Absorption | |
| Active Site | ACT_SITE 339; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA or 1,10-phenanthroline. Not inhibited by PMSF. {ECO:0000269|PubMed:15922394}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: This metalloproteinase hydrolyzes azocasein, and insulin B-chain (at the '38-Ala-|-Leu-39' bond). Also hydrolyzes the Aalpha-chain (FGA) and more slowly the Bbeta-chain of fibrinogen (FGB), without affecting the gamma-chain. Cleaves alpha-chain of fibrinogen at '432-Lys-|-Leu-433' and '535-Pro-|-Met-536' bonds. Does not cleave fibrin. Inhibits endothelial cell adhesion to extracellular matrix proteins such as fibrinogen, fibronectin, vitronectin, collagen I, and collagen IV. Induces apoptosis in vascular endothelial cells. {ECO:0000269|PubMed:15922394}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (18); Domain (2); Glycosylation (4); Metal binding (13); Modified residue (1); Motif (1); Propeptide (1); Signal peptide (1) |
| Keywords | Apoptosis;Calcium;Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Pyrrolidone carboxylic acid;Secreted;Signal;Toxin;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | MOD_RES 194; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000305|PubMed:15922394 |
| Post Translational Modification | PTM: The N-terminus is blocked. {ECO:0000269|PubMed:15922394}. |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 470..472; /note=D/ECD-tripeptide |
| Gene Encoded By | |
| Mass | 68,843 |
| Kinetics | |
| Metal Binding | METAL 205; /note=Calcium 1; /evidence=ECO:0000250; METAL 289; /note=Calcium 1; /evidence=ECO:0000250; METAL 338; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 342; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 348; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 393; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 396; /note=Calcium 1; /evidence=ECO:0000250; METAL 408; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 411; /note=Calcium 2; /evidence=ECO:0000250; METAL 413; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 415; /note=Calcium 2; /evidence=ECO:0000250; METAL 418; /note=Calcium 2; /evidence=ECO:0000250; METAL 421; /note=Calcium 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |