| IED ID | IndEnz0002011474 |
| Enzyme Type ID | protease011474 |
| Protein Name |
Zinc metalloproteinase/disintegrin Cleaved into: Snake venom metalloproteinase SVMP EC 3.4.24.- ; Disintegrin flavoridin |
| 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 | MIQVLLVTICLAVFPYQGSSIILESGNVNDYEVVYPRKVTALPKRAVQQKYEDAMQYELKVNGEPVVLHLEKNKGLFSEDYSETHYSPDGREITTYPSVEDHCYYHGRIHNDADSTASISACDGLKGYFKLQGETYLIEPLKLSDSEAHAVYKYENIEKEDEAPKMCGVTQNWESDESIKKASQLYLTPEQQRFPQRYIELAIVVDHGMYKKYNHDSDKIKVRVHQMVNHINEMYRPLNIAITLSLLQIWSNKDLITVKSASNVTLNLFGNWRETVLLKRRSHDCAHLLTDINFTGNIIGLAYKQGMCNPKLSVGLVQDYSSNVFVVAVIMTHELGHNLGMEHDEEKNGKKCNCKTCIMSPAISDPPAQLFSDCSKNDYHTFLTNRNPQCILNAPLRTDTVSTPVSGNEFLEAGEECDCGSPSNPCCDAATCKLRPGAQCADGLCCDQCRFKKKRTICRIARGDFPDDRCTGLSNDCPRWNDL |
| Enzyme Length | 483 |
| Uniprot Accession Number | P18619 |
| Absorption | |
| Active Site | ACT_SITE 334; /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: [Snake venom metalloproteinase]: Impairs hemostasis in the envenomed animal. {ECO:0000250}.; FUNCTION: [Disintegrin flavoridin]: 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); Beta strand (4); Chain (2); Disulfide bond (9); Domain (2); Glycosylation (2); Metal binding (7); Motif (1); Propeptide (2); Sequence conflict (1); Signal peptide (1); Turn (1) |
| Keywords | 3D-structure;Calcium;Cell adhesion impairing toxin;Direct protein sequencing;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. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | NMR spectroscopy (1) |
| Cross Reference PDB | 1FVL; |
| Mapped Pubmed ID | - |
| Motif | MOTIF 462..464; /note=Cell attachment site |
| Gene Encoded By | |
| Mass | 54,514 |
| Kinetics | |
| Metal Binding | METAL 200; /note=Calcium; /evidence=ECO:0000250; METAL 284; /note=Calcium; /evidence=ECO:0000250; METAL 333; /note=Zinc; catalytic; /evidence=ECO:0000305; METAL 337; /note=Zinc; catalytic; /evidence=ECO:0000305; METAL 343; /note=Zinc; catalytic; /evidence=ECO:0000305; METAL 390; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 393; /note=Calcium; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |