| IED ID | IndEnz0002012154 |
| Enzyme Type ID | protease012154 |
| Protein Name |
Zinc metalloproteinase-disintegrin stejnitin EC 3.4.24.- Snake venom metalloproteinase SVMP |
| Gene Name | |
| Organism | Trimeresurus stejnegeri (Chinese green tree viper) (Viridovipera stejnegeri) |
| 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) Trimeresurus Trimeresurus stejnegeri (Chinese green tree viper) (Viridovipera stejnegeri) |
| Enzyme Sequence | MIQVLLVTICLAVFPYQGNSIILESGNVNDYEVVYPRKVTALPKGAVQPKYEDAMQYEFKVNGEPVVLHLEKNKGLFSEDYSETHYSPDGREITTYPSVEDHCYYHGRIQNDADLTASISACNGLKGYFKLQGETYLIEPLKLPDSEAHAVFKYENVEKEDEAPKMCGVTETNWESDEPIKKASQLNLTPDEQRFIELVIVADHRMYTKYDGDETEISSKIYEIANDLNVIFRALYIHVALIGLEIWPSGELCNVTLSADDTLDSFAEWTKRDLQKRKRHDNAQLLTGMIFNEKIEGRAYKKTMCHWKRSVGIVRDHRTRPHFVANRMAHGLGHNLGINHDGDSCTCGANSCIMSATVSNDPSSRFSDCSLNQYSSDIIHNPYTSRCLYNGPWKTDIVSPPVCGNYYVEVGEDCDCGPPANCQNRCCDAATCRLTPGSQCAEGLCCEQCRFSTEGKLCREAKGDWNNDYCSGQSGDCPRNPFRA |
| Enzyme Length | 484 |
| Uniprot Accession Number | P0DM87 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Snake venom zinc metalloproteinase that inhibits ADP-induced platelet aggregation in human platelet-rich plasma (IC(50) is 175 nM) and cleaves alpha-(FGA) and subsequently the beta-chain (FGG) of bovine fibrinogen, leaving the gamma-chain unaffected. It is also able to inhibit proliferatin of ECV304 cells by inducing apoptosis of these cells. {ECO:0000269|PubMed:17403531}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Disulfide bond (10); Domain (2); Glycosylation (1); Metal binding (12); Modified residue (1); 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;Pyrrolidone carboxylic acid;Secreted;Signal;Toxin;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | MOD_RES 193; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000305|PubMed:17403531 |
| Post Translational Modification | PTM: The N-terminus is blocked. {ECO:0000269|PubMed:17403531}. |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 462..464; /note=Cell attachment site; /evidence=ECO:0000255|PROSITE-ProRule:PRU00068 |
| Gene Encoded By | |
| Mass | 54,436 |
| Kinetics | |
| Metal Binding | METAL 197; /note=Calcium 1; /evidence=ECO:0000250; METAL 281; /note=Calcium 1; /evidence=ECO:0000250; METAL 330; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276; METAL 334; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276; METAL 340; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276; METAL 387; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 390; /note=Calcium 1; /evidence=ECO:0000250; METAL 402; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 405; /note=Calcium 2; /evidence=ECO:0000250; METAL 409; /note=Calcium 2; /evidence=ECO:0000250; METAL 412; /note=Calcium 2; /evidence=ECO:0000250; METAL 415; /note=Calcium 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |