| IED ID | IndEnz0002012072 |
| Enzyme Type ID | protease012072 |
| Protein Name |
Zinc metalloproteinase-disintegrin-like Eoc1 EC 3.4.24.- Snake venom metalloproteinase SVMP |
| Gene Name | Svmp3-Eoc1 EOC00001-SVMP |
| Organism | Echis ocellatus (Ocellated saw-scaled 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) Echis Echis ocellatus (Ocellated saw-scaled viper) |
| Enzyme Sequence | MQVLLITISLAVLPYLGSSIILESGIVNDYEVVNPQKVTAMLKGAVKQPEQKYEDTMQYEFKVKGEPVVLHLEKNKGLFSEDYSETHYSPDGREITTNPPVEDHCYYHGRIQNDADSSASISACNGLKGHFKLRGEMYFIEPLKIPDSEAHAVYKYENIEEEDEAPKMCGVKHTNRESDKSIKKASQLNLTPEQQRYLNTPKHIKVAIVADYLIFRKYGRNLFTIRAKIYEILNILNEIYKAFNIHVALVFLEIWSNGDKINLFPAANVTLDLFGKWRERDLMNRKNHDNTQLLTGMNFDGPTAGLGYVGTMCHPQFSAAVVQDHNKINFLVALAMAHELGHNLGMTHDEQFCTCGAKSCIMSATLSCEGSYRFSNCSREENRRYLINKMPQCILIKPSRTDIVSPPVCGNSLVEVGEDCDCGSPGYCRNPCCNAATCKLTPGSQCADGECCDQCRFTRAGTECRPARDECDKADLCTGQSAECPADQFQRNGQPCQNNSGYCYNGICPVMRNQCISLFGSRAIVAEDACFQFNSLGIDYGYCRKENGRKIPCAPEDVKCGRLYCFDNLPEHKNPCQIFYTPRDEDKGMVDPGTKCENGKVCINGKCVDVNTAY |
| Enzyme Length | 614 |
| Uniprot Accession Number | Q2UXR0 |
| Absorption | |
| Active Site | ACT_SITE 339; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: This metalloproteinase hydrolyzes azocasein, and oxidized insulin B-chain. Also hydrolyzes the alpha-chain (FGA) and more slowly the beta-chain of fibrinogen (FGB), without affecting the gamma-chain. 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 (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (18); Domain (2); Glycosylation (3); Metal binding (9); Modified residue (1); Motif (1); Propeptide (1); Signal peptide (1) |
| Keywords | Apoptosis;Calcium;Cell adhesion impairing toxin;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:0000250 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 470..472; /note=D/ECD-tripeptide |
| Gene Encoded By | |
| Mass | 68,751 |
| Kinetics | |
| Metal Binding | 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 408; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 411; /note=Calcium; /evidence=ECO:0000250; METAL 413; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 415; /note=Calcium; /evidence=ECO:0000250; METAL 418; /note=Calcium; /evidence=ECO:0000250; METAL 421; /note=Calcium; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |