IED ID | IndEnz0002012165 |
Enzyme Type ID | protease012165 |
Protein Name |
Zinc metalloproteinase/disintegrin Cleaved into: Snake venom metalloproteinase HR2a SVMP EC 3.4.24.53 Snake venom metalloproteinase HR2b Trimerelysin II ; Disintegrin flavostatin Platelet aggregation activation inhibitor |
Gene Name | |
Organism | Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis) |
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) Protobothrops Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis) |
Enzyme Sequence | MIEVLLVTICLAVFPYPGSSIILESGNVDDYEVVYPQKLTALPKGAVQPKYEDAMQYEFKVNGEPVVLHLEKNKGLFSEDYSETHYSPDGREITTYPSVEDHCYYHGRIQNDADSTASISACDGLKGYFKLQGETYLIEPLELSDSEAHAVFKYENVEKEDEAPKMCGVTQNWESDESIKKASQLYLTPEQQRFPQRYIELAIVVDHGMYTKYSSNFKKIRKRVHQMVNNINEMYRPLNIAITLSLLDVWSEKDLITMQAVAPTTARLFGDWRETVLLKQKDHDHAQLLTDINFTGNTIGWAYMGGMCNAKNSVGIVKDHSSNVFMVAVTMTHEIGHNLGMEHDDKDKCKCEACIMSAVISDKPSKLFSDCSKDYYQTFLTNSKPQCIINAPLRTDTVSTPVSGNEFLEAGEECDCGSPSNPCCDAATCKLRPGAQCADGLCCDQCRFKKKRTICRRARGDNPDDRCTGQSADCPRNS |
Enzyme Length | 478 |
Uniprot Accession Number | P14530 |
Absorption | |
Active Site | ACT_SITE 334 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleavage of 3-Asn-|-Gln-4, 10-His-|-Leu-11 and 14-Ala-|-Leu-15 in the insulin B chain, and the bond Z-Gly-Pro-|-Leu-Gly-Pro in a small molecule substrate of microbial collagenase.; EC=3.4.24.53; |
DNA Binding | |
EC Number | 3.4.24.53 |
Enzyme Function | FUNCTION: [Snake venom metalloproteinase HR2a]: Zinc protease that induces hemorrhage. {ECO:0000269|PubMed:9114455}.; FUNCTION: [Disintegrin flavostatin]: Inhibits platelet aggregation induced by ADP, thrombin, and collagen. Acts by inhibiting fibrinogen interaction with platelet receptors GPIIb/GPIIIa (ITGA2B/ITGB3). {ECO:0000269|PubMed:9114455}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (2); Disulfide bond (9); Domain (2); Metal binding (7); Modified residue (1); Motif (1); Natural variant (3); Propeptide (2); Region (1); Signal peptide (1); Site (1) |
Keywords | Calcium;Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemorrhagic toxin;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 191; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000269|PubMed:2753880, ECO:0000269|PubMed:7597726" |
Post Translational Modification | PTM: Not N-glycosylated. {ECO:0000269|PubMed:2753880}. |
Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | MOTIF 459..461; /note=Cell attachment site |
Gene Encoded By | |
Mass | 53,646 |
Kinetics | |
Metal Binding | METAL 200; /note=Calcium; /evidence=ECO:0000250; METAL 284; /note=Calcium; /evidence=ECO:0000250; METAL 333; /note=Zinc; catalytic; METAL 337; /note=Zinc; catalytic; METAL 343; /note=Zinc; catalytic; METAL 387; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 390; /note=Calcium; /evidence=ECO:0000250 |
Rhea ID | |
Cross Reference Brenda |