| IED ID | IndEnz0002012117 |
| Enzyme Type ID | protease012117 |
| Protein Name |
Zinc metalloproteinase-disintegrin-like atrolysin-A EC 3.4.24.1 Alpha-proteinase Hemorrhagic toxin A HT-A Snake venom metalloproteinase SVMP Fragment |
| Gene Name | |
| Organism | Crotalus atrox (Western diamondback rattlesnake) |
| 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) Crotalus Crotalus atrox (Western diamondback rattlesnake) |
| Enzyme Sequence | ERLTKRYVELVIVADHRMFTKYNGNLKKIRKWIYQIVNTINEIYIPLNIRVALVRLEIWSNGDLIDVTSAANVTLKSFGNWRVTNLLRRKSHDNAQLLTAIDLDEETLGLAPLGTMCDPKLSIGIVQDHSPINLLVAVTMAHELGHNLGMVHDENRCHCSTPACVMCAVLRQRPSYEFSDCSLNHYRTFIINYNPQCILNEPLQTDIISPPVCGNELLEVGEECDCGSPRTCRDPCCDAATCKLHSWVECESGECCQQCKFTSAGNVCRPARSECDIAESCTGQSADCPTDDFHRNGKPCLHNFGYCYNGNCPIMYHQCYALWGSNVTVAPDACFDINQSGNNSFYCRKENGVNIPCAQEDVKCGRLFCNVNDFLCRHKYSDDGMVDHGTKCADGKVCKNRQCVDVTTAYKSTSGFSQI |
| Enzyme Length | 419 |
| Uniprot Accession Number | Q92043 |
| Absorption | |
| Active Site | ACT_SITE 143; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleavage of 3-Asn-|-Gln-4, 5-His-|-Leu-6, 10-His-|-Leu-11, 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in insulin B chain. Removes C-terminal Leu from small peptides.; EC=3.4.24.1; |
| DNA Binding | |
| EC Number | 3.4.24.1 |
| Enzyme Function | FUNCTION: Snake venom zinc metalloproteinase-disintegrin that causes hemorrhage by provoking the degradation of the sub-endothelial matrix proteins (fibronectin, laminin, type IV collagen, nidogen, and gelatins) and disturbances in platelet function. The recombinant cysteine-rich domain interacts with the alpha-2/beta-1 integrin (ITGA2/ITGB1) (collagen receptor), and inhibits the platelet aggregation induced by collagen. {ECO:0000269|PubMed:10620350, ECO:0000269|PubMed:12914938, ECO:0000269|PubMed:2817904}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (17); Domain (2); Glycosylation (4); Metal binding (13); Motif (1); Non-terminal residue (1) |
| Keywords | Calcium;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemorrhagic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Platelet aggregation inhibiting toxin;Protease;Secreted;Toxin;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 274..276; /note=D/ECD-tripeptide |
| Gene Encoded By | |
| Mass | 46,879 |
| Kinetics | |
| Metal Binding | METAL 9; /note=Calcium 1; /evidence=ECO:0000250; METAL 93; /note=Calcium 1; /evidence=ECO:0000250; METAL 142; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 146; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 152; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 197; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 200; /note=Calcium 1; /evidence=ECO:0000250; METAL 212; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 215; /note=Calcium 2; /evidence=ECO:0000250; METAL 217; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 219; /note=Calcium 2; /evidence=ECO:0000250; METAL 222; /note=Calcium 2; /evidence=ECO:0000250; METAL 225; /note=Calcium 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |