| IED ID | IndEnz0002011069 |
| Enzyme Type ID | protease011069 |
| Protein Name |
Zinc metalloproteinase-disintegrin-like VLAIP-A EC 3.4.24.- Snake venom metalloproteinase SVMP Vipera lebetina apoptosis-inducing protein |
| 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 | MMQVLLVTISLAVFPYQGSSIILESGNVNDYEVVYPQKVTAMPKGAVKQPEQKYEDAMQYEFKVKGEPVVLLLEKNKDLFSEDYSETHYSPDGREITTNPPVEDHCYYHGRIQNDADSSASISACNGLKGHFMLQGETYLIEPLKLPDSEAHAVYKYENVEKEDEAPKMCGVTQTNWESDEPIKKASQLNLTPEQRRYLNSPKYIKLVIVADYIMFLKYGRSLITIRTRIYEIVNILNVIYRVLNIYIALLGLEIWNNGDKINVLPETKVTLDLFGKWRERDLLNRRKHDNAQLLTDINFNGPTAGLGYVGSMCDPQYSAGIVQDHNKVNFLVALAMAHEMGHNLGMEHDEIHCTCGAKSCIMSGTLSCEASIRFSNCSREEHQKYLINKMPQCILNKPLKTDIVSPAVCGNYLVELGEDCDCGSPRDCQNPCCNAATCKLTPGSQCADGECCDQCKFRRAGTVCRPANGECDVSDLCTGQSAECPTDQFQRNGQPCQNNNGYCYSGTCPIMGKQCISLFGASATVAQDACFQFNSLGNEYGYCRKENGRKIPCAPQDVKCGRLYCFDNLPEHKNPCQIYYTPSDENKGMVDPGTKCGDGKACSSNRQCVDVNTAY |
| Enzyme Length | 616 |
| Uniprot Accession Number | Q4VM08 |
| Absorption | |
| Active Site | ACT_SITE 340; /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: Snake venom zinc metalloprotease that hydrolyzes the alpha-chain (FGA) and more slowly the beta-chain (FGB) of fibrinogen, without affecting the gamma-chain. Cleaves alpha-chain of fibrinogen at '432-Lys-|-Leu-433' and '535-Pro-|-Met-536' bonds. Induces apoptosis in vascular endothelial cells and inhibits endothelial cell adhesion to extracellular matrix proteins such as fibrinogen, fibronectin, vitronectin, collagen I, and collagen IV. Also hydrolyzes azocasein, and insulin B-chain (at the '38-Ala-|-Leu-39' bond). {ECO:0000269|PubMed:15922394}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (18); Domain (2); Glycosylation (1); Metal binding (9); 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 195; /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 471..473; /note=D/ECD-tripeptide |
| Gene Encoded By | |
| Mass | 68,710 |
| Kinetics | |
| Metal Binding | METAL 339; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 343; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 349; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 409; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 412; /note=Calcium; /evidence=ECO:0000250; METAL 414; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 416; /note=Calcium; /evidence=ECO:0000250; METAL 419; /note=Calcium; /evidence=ECO:0000250; METAL 422; /note=Calcium; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |