| IED ID | IndEnz0002011112 |
| Enzyme Type ID | protease011112 |
| Protein Name |
Zinc metalloproteinase-disintegrin VMP-II CamVMP-II EC 3.4.24.- Disintegrin r-Cam-dis Snake venom metalloproteinase SVMP |
| Gene Name | |
| Organism | Crotalus adamanteus (Eastern diamondback rattlesnake) |
| 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) Crotalus Crotalus adamanteus (Eastern diamondback rattlesnake) |
| Enzyme Sequence | MIQVLLVTICLAVFPYQGSSIILESGNVNDYEVVYPRKVTALPKGAVQLKYEDAMQYEFKVNGEPVVLHLEKNKGLFSEDYSETHYSPDGREITTYPPVEDHCYYHGRIQNDADSTASISACNGLKGHFKLQGEMYLIEPLKLSDSEAHAVYKYENVEKEDEASKMCGVTETNWESYEPIKKASQSNIPPEEEAFYQRYIELVVVADHRMYTKYDGDKTEISSIIYEIVNTLTQIFRPLHIRVALIGLEIWSSGELSKVTLSADDTLEAFGEWRKTVLMNRKRHDNAQLLTGMIFNETIEGRTYKSGMCNPKHSVGIVRDYRTRRHFVANRMAHELGHNLGIDHDRDSCTCGANSCIMSATVSNEPSSQFSDCSLNKYLNYIVRYQSTTRCLHNEPSETDIVSPPFCGNYFKEVGEDCDCGPPANCQNPCCDAATCKLTTGSQCAEGLCCDQCKFTKKGTACRPARGDWNDDTCTGQSADCPRNGLYG |
| Enzyme Length | 488 |
| Uniprot Accession Number | J9Z332 |
| Absorption | |
| Active Site | ACT_SITE 335; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Zinc metalloproteinase-disintegrin VMP-II: inhibits ADP-induced platelet aggregation (probably by binding integrin alpha-IIb/beta-3 (ITGA2B/ITGB3)) and degrades fibrinogen. {ECO:0000250}.; FUNCTION: Recombinant disintegrin r-Cam-dis (413-488): this recombinant protein inhibits platelet adhesion to fibrinogen (IC(50) is 1 nM), inhibits collagen- (IC(50) is 18 nM) and ADP-induced (IC(50) is 6 nM) platelet aggregation, and also inhibits platelet function on clot retraction. May act by binding integrin alpha-IIb/beta-3 (ITGA2B/ITGB3). {ECO:0000269|PubMed:23313448}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (10); Domain (2); Glycosylation (1); Metal binding (11); Motif (1); Propeptide (1); Signal peptide (1) |
| Keywords | Calcium;Cell adhesion impairing toxin;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Platelet aggregation inhibiting toxin;Protease;Secreted;Signal;Toxin;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 466..468; /note=Cell attachment site |
| Gene Encoded By | |
| Mass | 54,823 |
| Kinetics | |
| Metal Binding | METAL 201; /note=Calcium 1; /evidence=ECO:0000250; METAL 285; /note=Calcium 1; /evidence=ECO:0000250; METAL 334; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276; METAL 338; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276; METAL 344; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276; METAL 391; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 394; /note=Calcium 1; /evidence=ECO:0000250; METAL 409; /note=Calcium 2; /evidence=ECO:0000250; METAL 413; /note=Calcium 2; /evidence=ECO:0000250; METAL 416; /note=Calcium 2; /evidence=ECO:0000250; METAL 419; /note=Calcium 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.1; |