IED ID | IndEnz0002010304 |
Enzyme Type ID | protease010304 |
Protein Name |
Zinc metalloproteinase/disintegrin Cleaved into: Snake venom metalloproteinase graminelysin SVMP EC 3.4.24.- Graminelysin I ; Disintegrin-like Fragment |
Gene Name | |
Organism | Trimeresurus gramineus (Bamboo pit viper) (Indian green tree 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 Crotalinae (pit vipers) Trimeresurus Trimeresurus gramineus (Bamboo pit viper) (Indian green tree viper) |
Enzyme Sequence | KMCGVTQNWESYESTKKASQLNLTPEQQRFPQRYIKLGIFVDHGMYTKYSGNSERITKRVHQMINNINMMCRALNIVTTLSLLEIWSEKDLITVQASAPTTLTLFGAWRETVLLNRTSHDHAQLLTATIFNGNVIGRAPVGGMCDPKRSVAIVRDHNAIVFVVAVTMTHEMGHNLGNHHDEDKCNCNTCIMSKVLSRQPSKYFSECSKDYYQTFLTNHNFQCILNAPLRTDTVSTPVSGNELLEAGEDCDCGSPANPCCDAATCKLRPGAQCGEGLCCDQCRFTSAGTECRAARSECDIAESCAGQSADCPTDDFHRNGQPCLNNHGYCYNGNCPIMFYQCIALFGSNATVGQDGCFDANDIGHKYFHCRKDNEKYIPCAPQDVKCGRLFCTYIYDIDLCRYDDSANGMVAQGTKCADGKVCNSNRQCADVNTAY |
Enzyme Length | 435 |
Uniprot Accession Number | P0C6E8 |
Absorption | |
Active Site | ACT_SITE 170; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA. {ECO:0000269|PubMed:11463342}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.24.- |
Enzyme Function | FUNCTION: [Snake venom metalloproteinase graminelysin]: Cleaves the alpha chain of fibrinogen (FGA) preferentially and cleaves the beta chain (FGB) either on longer incubation or at high concentrations. Induces apoptosis of endothelial cells (prior to cell detachment). {ECO:0000269|PubMed:11463342, ECO:0000269|PubMed:11776320, ECO:0000269|PubMed:12878166}.; FUNCTION: Disintegrin: inhibits platelet aggregation induced by ADP, thrombin, platelet-activating factor and collagen. Acts by inhibiting fibrinogen interaction with platelet receptors GPIIb/GPIIIa (ITGA2B/ITGB3) (By similarity). {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (2); Disulfide bond (9); Domain (2); Glycosylation (1); Metal binding (9); Modified residue (1); Motif (1); Non-terminal residue (1); Propeptide (2) |
Keywords | Apoptosis;Calcium;Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Platelet aggregation inhibiting toxin;Protease;Pyrrolidone carboxylic acid;Secreted;Toxin;Zinc;Zymogen |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
Modified Residue | MOD_RES 27; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000250 |
Post Translational Modification | PTM: The N-terminus of the metalloproteinase is blocked. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | MOTIF 296..298; /note=D/ECD-tripeptide |
Gene Encoded By | |
Mass | 48,204 |
Kinetics | |
Metal Binding | METAL 169; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 173; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 179; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 237; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 240; /note=Calcium; /evidence=ECO:0000250; METAL 242; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 244; /note=Calcium; /evidence=ECO:0000250; METAL 247; /note=Calcium; /evidence=ECO:0000250; METAL 250; /note=Calcium; /evidence=ECO:0000250 |
Rhea ID | |
Cross Reference Brenda |