| IED ID | IndEnz0002012150 |
| Enzyme Type ID | protease012150 |
| Protein Name |
Zinc metalloproteinase-disintegrin-like alternagin EC 3.4.24.- Snake venom metalloproteinase SVMP Cleaved into: Disintegrin-like alternagin-C Alt-C Fragment |
| Gene Name | |
| Organism | Bothrops alternatus (Urutu) (Rhinocerophis alternatus) |
| 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 alternatus (Urutu) (Rhinocerophis alternatus) |
| Enzyme Sequence | IISPPVCGNELLEVGEECDCGTPENCQNXCCDAATCKLKSGSQCGHXDCCEQCKFTKSGTECRASMSECDPAEHCTGQSXXCXXDVFHKNGQPCLDNYGYCYNGNCPIMYHAQCYALFGADVYEAEDSCFKDNQKGNYYGYCRKENXXXXXCXXXDVKCGRLYCKDNSPKQNNPCKMFYSNDDEHKGNVLPGTKCE |
| Enzyme Length | 196 |
| Uniprot Accession Number | P0C6R9 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA. {ECO:0000269|PubMed:11368322}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: [Zinc metalloproteinase-disintegrin-like alternagin]: hemorrhagic protease that acts as a potent inhibitor of collagen-induced adhesion by blockage of alpha-2/beta-1 (ITGA2/ITGB1) integrin. Cleaves at Leu-|-Met bonds (PubMed:11368322). {ECO:0000269|PubMed:11368322}.; FUNCTION: Disintegrin alternagin-C: potent inhibitor of the collagen binding to alpha-2/beta-1 (ITGA2/ITGB1) integrin. Has a chemotactic activity on neutrophils and this effect involves actin cytoskeleton rearrangement, FAK, PI3-kinase and Erk-2 activities. Induces endothelial cell proliferation, and these effects are mediated at least in part by an increased expression of vascular endothelial growth factor (VEGF). In injured muscles, reduces both MMP-2 mRNA and gelatinolytic activity, suggesting that it changes the overall balance of extracellular matrix protein turnover during muscle regeneration. In low concentrations, induces formation of new vessels and up-regulates the expression of VEGF receptor 2 (KDR) without affecting VEGF receptor 1 (FLT1) expression. In high concentrations, strongly inhibits angiogenesis, and the expression of both receptors is down-regulated. Has very low plasma clotting activity. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (2); Disulfide bond (19); Domain (1); Metal binding (11); Motif (1); Non-terminal residue (2); Sequence uncertainty (3) |
| Keywords | Angiogenesis;Calcium;Cell adhesion impairing toxin;Chemotaxis;Developmental protein;Differentiation;Direct protein sequencing;Disulfide bond;Hemorrhagic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | PTM: The N-terminus of alternagin is blocked. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 68..70; /note=D/ECD-tripeptide |
| Gene Encoded By | |
| Mass | 21,731 |
| Kinetics | |
| Metal Binding | METAL 6; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 9; /note=Calcium 1; /evidence=ECO:0000250; METAL 11; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 13; /note=Calcium 1; /evidence=ECO:0000250; METAL 16; /note=Calcium 1; /evidence=ECO:0000250; METAL 19; /note=Calcium 1; /evidence=ECO:0000250; METAL 70; /note=Calcium 2; /evidence=ECO:0000250; METAL 71; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 73; /note=Calcium 2; /evidence=ECO:0000250; METAL 85; /note=Calcium 2; /evidence=ECO:0000250; METAL 86; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |