| IED ID | IndEnz0002011818 |
| Enzyme Type ID | protease011818 |
| Protein Name |
Zinc metalloproteinase/disintegrin Metalloproteinase PII MPII Cleaved into: Snake venom metalloproteinase SVMP EC 3.4.24.- ; Disintegrin Cdc |
| Gene Name | MPII |
| Organism | Crotalus durissus collilineatus (Brazilian 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 durissus (tropical rattlesnake) Crotalus durissus collilineatus (Brazilian rattlesnake) |
| Enzyme Sequence | MIQVLLVTICLAAFPYQGSSIILESGNVNDYEVIYPRKVTALPKGAVQPKYEDTMQYELKVNGQPVVLHLEKNKGLFSKDYSETHYSPDGRKITTNPSVEDHCYYHGRIENDADSTASISACNGLKGHFKLQGEMYIIEPLELSDSEDHAVFKLENVEKEDEAPKMCGVTQNWESNEPIKKASHLNLNPEHQRYVEIVIVVDHGMFTKYNGDSDKIRQRVHQMVNIMKESYRYMYIDISLAGIEIWSNKDLINVQPAAPNTLKSFGEWRETDLPKRKSHDNAQLLTSIDFNGQTIGIANIGAICDPKPSTRVVQDHSKINLRVALTMTHELSHNLGIHHDTGSCSCSGYSCIMSPVISDEPSKYFSDCSYIQCWNFIMNQKPQCILKKPLRTDTVSTPVSGNELLEARIECDCGSIENPCCYATTCKLRPGSQCAEGMCCDQCRFMKKGTVCRVSLVNKNDDTCTGQSADCPRNVLYG |
| Enzyme Length | 478 |
| Uniprot Accession Number | C0L2T8 |
| Absorption | |
| Active Site | ACT_SITE 330; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: [Snake venom metalloproteinase]: Snake venom zinc metalloproteinase that causes hemorrhage by provoking the degradation of the sub-endothelial matrix proteins (fibronectin, laminin, type IV collagen, nidogen, and gelatins). {ECO:0000250|UniProtKB:P34182}.; FUNCTION: [Disintegrin Cdc]: Displays low cytotoxicity and inhibits cell migration. {ECO:0000269|PubMed:30377432}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (2); Disulfide bond (9); Domain (2); Metal binding (3); Propeptide (3); Signal peptide (1) |
| Keywords | Cell adhesion impairing toxin;Collagen degradation;Direct protein sequencing;Disulfide bond;Hemorrhagic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Toxin;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19230843}.; SUBCELLULAR LOCATION: [Disintegrin Cdc]: Secreted {ECO:0000269|PubMed:30377432}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 53,639 |
| Kinetics | |
| Metal Binding | METAL 329; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276; METAL 333; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276; METAL 339; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276 |
| Rhea ID | |
| Cross Reference Brenda |