| IED ID | IndEnz0002010746 |
| Enzyme Type ID | protease010746 |
| Protein Name |
Zinc metalloproteinase/disintegrin-like HR1a EC 3.4.24.- Snake venom metalloproteinase SVMP Cleaved into: Disintegrin-like 1a |
| 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 | MIQVLLVTICLAVFPYQGSSIILGSGNVNDYEVVYPRKVTAVPKGAVQPKYEDTMQYEFKVNGEPVVLHLEKNKGLFSKDYSETHYSPDGREITTYPSVEDHCYYHGRIQNDADSTASISACNGLKGHFKLQGEMYLIEPLRFSDSEAHAVFKYENVEKEDEAPKMCGVTQTNWESDEPIKKASKLVVTAEQQRYLNNFRFIELVIVADYRMFTKFNSNLNEVKTWVYEIVNTLNEIYRYLYVRVALVALEVWSNGDLSSVTLSAYDTLDSFGEWRKRDLLKRKSHDNAQLLTAIDFNGTIIGLAHVASMCDPKCSTGIVQDYSSRNLVVAVIMAHEMGHNLGIRHDRENCTCHANSCIMSAVISDQPSKYFSNCSHVQYWNYINDDEPQCILNEPLRTDIVSPPVCGNELLEVGEECDCGSPATCRYPCCDAATCKLHSWVECESGECCEQCRFRTAGTECRARRSECDIAESCTGHSADCPTDRFHRNGQPCLHNFGYCYNGNCPIMYHQCYALWGANATVAKDSCFEDNQKGNDYGYCRKENGRKIPCEPQDVKCGRLYCSLGNQLPCRFFYTPTDENIGMVDTGTKCGDKKVCSNRQCVDVNTAY |
| Enzyme Length | 609 |
| Uniprot Accession Number | Q8JIR2 |
| Absorption | |
| Active Site | ACT_SITE 337; /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: [Zinc metalloproteinase/disintegrin-like HR1a]: Zinc protease that induces hemorrhage and has proteolytic activity (PubMed:18061641). Has preference for Ala, His, Pro, Met, and Tyr at the P1 position, in descending order (in vitro). Predominantly prefers Val and Asp at the P3 and P2 positions, respectively (PubMed:18256489). {ECO:0000269|PubMed:18061641, ECO:0000269|PubMed:18256489}.; FUNCTION: [Disintegrin-like 1a]: Inhibits platelet aggregation induced by ADP, thrombin, platelet-activating factor and collagen. Acts by inhibiting fibrinogen interaction with platelet receptors alpha-IIb/beta-3 (ITGA2B/ITGB3) (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (2); Disulfide bond (25); Domain (2); Glycosylation (4); Metal binding (16); Motif (1); Propeptide (2); Signal peptide (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;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 | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 468..470; /note=D/ECD-tripeptide |
| Gene Encoded By | |
| Mass | 68,765 |
| Kinetics | |
| Metal Binding | METAL 203; /note=Calcium 1; /evidence=ECO:0000250; METAL 287; /note=Calcium 1; /evidence=ECO:0000250; METAL 336; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 340; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 346; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 391; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 394; /note=Calcium 1; /evidence=ECO:0000250; METAL 406; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 409; /note=Calcium 2; /evidence=ECO:0000250; METAL 411; /note=Calcium 2; via carbonyl oxygen; /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; METAL 470; /note=Calcium 3; /evidence=ECO:0000250; METAL 473; /note=Calcium 3; /evidence=ECO:0000250; METAL 485; /note=Calcium 3; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |