| IED ID | IndEnz0002013488 |
| Enzyme Type ID | protease013488 |
| Protein Name |
Snake venom metalloproteinase atroxlysin-1 SVMP EC 3.4.24.- Atroxlysin-I |
| Gene Name | |
| Organism | Bothrops atrox (Barba amarilla) (Fer-de-lance) |
| 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) Bothrops Bothrops atrox (Barba amarilla) (Fer-de-lance) |
| Enzyme Sequence | TPEQQRYVDLFIVVDHGMFMKYNGNSDKIRRRIHQMVNIMKEAYSTMYIDILLTGVEIWSNKDLINVQPAAPQTLDSFGEWRKTDLLNRKSHDNAQLLTSTDFNGPTIGLAYVGSMCDPKRSTGVIQDHSEQDLMVAITMAHELGHNLGISHDTGSCSCGGYSCIMSPVLSHEPSKYFSDCSYIQCWDFIMKENPQCILNKR |
| Enzyme Length | 202 |
| Uniprot Accession Number | P85420 |
| Absorption | |
| Active Site | ACT_SITE 143; /evidence="ECO:0000250|UniProtKB:P83512, ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA, DTT and high concentrations of zinc ions (>2 mM). Weakly inhibited by TLCK. Not inhibited by PMSF. Activated by calcium ions. {ECO:0000269|PubMed:20102699}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Snake venom zinc metalloproteinase that acts on fibrinogen, fibrin, fibronectin (FN1), type I collagen, type IV collagen, integrin alpha-7/beta-1 (ITGA7/ITGB1) and integrin alpha-1/beta-1 (ITGA1/ITGB1). Binds to fibronectin (FN1), fibrinogen and, weakly, to type I collagen and laminin. Cleaves Xaa-Leu bonds. Inhibits ADP- and collagen-induced platelet aggregation both in the presence (IC(50)=1.4 uM for collagen) and in the absence (IC(50)=2.2 uM for collagen) of cofactors. Has hemorrhagic activity. {ECO:0000269|PubMed:20102699}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|Ref.2}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|Ref.2}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (3); Domain (1); Metal binding (7); Sequence conflict (4) |
| Keywords | Calcium;Direct protein sequencing;Disulfide bond;Fibrinolytic toxin;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:0000269|PubMed:20102699}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 22,918 |
| 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 |
| Rhea ID | |
| Cross Reference Brenda |