| IED ID | IndEnz0002011068 |
| Enzyme Type ID | protease011068 |
| Protein Name |
Zinc metalloproteinase-disintegrin-like VMP-III AplVMP-III EC 3.4.24.- Snake venom metalloproteinase SVMP |
| Gene Name | |
| Organism | Agkistrodon piscivorus leucostoma (Western cottonmouth) (Acontias leucostoma) |
| 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) Agkistrodon Agkistrodon piscivorus (cottonmouth) Agkistrodon piscivorus leucostoma (Western cottonmouth) (Acontias leucostoma) |
| Enzyme Sequence | MIQVLLVTLCLAAFPYQGSSIILDSGNVNDYEVVYPRKVTALPKGAVQPKYEDTMQYEFKVNGEPVVLHLEKNKGLFSEDYSETHYSPDGREITTYPSIEDHCYYRGRIQNDADSTASISACNGLKGHFKLQGEMYLIEPLKLPDSEAHAVYKYENIEKEDEAPKMCGVTQTNWKSDEPIKKASQLVVTPEEQRYLNTKKYIELVIVADNVMVKKYTSNSTAIRTRIYACVNTLNLIYRAFNIYIALIGLEIWSNRDLINVQSASSVTLDLFGTWRETVLLRHKRHDNAQLLTGINFDGDTVGLAYVGSMCDPKRSAGIIQDHNKLDVMVAIAMAHELGHDLGINHDGNQCNCGGNPCIMSATLNFEPVYRFSDCSRDEHWRYLIDNRPPCILNKPSITDIVSPPVCGNYFVEVGEECDCGLPAHCQNPCCDAATCKLRPETQCEDGECCEQCQFTRAGTECRAARSECDIAESCTGQSAECPTDDFQRNGQPCLNNNGYCYNGTCPILTNQCISFFGSSATVAPDVCFDFNLQGQGNFYCRRERARIFPCAPQDKKCGRLFCVKGPIGNTISCQSTSSQSDLDIGMVDLGTKCGDGRVCNSNRQCVDVNTAY |
| Enzyme Length | 613 |
| Uniprot Accession Number | C9E1S0 |
| 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: Snake venom metalloproteinase that impairs hemostasis in the envenomed animal. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (17); Domain (2); Glycosylation (2); Metal binding (13); Motif (1); Propeptide (1); Signal peptide (1) |
| Keywords | Calcium;Cell adhesion impairing toxin;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Toxin;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| 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 | 68,212 |
| 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 |
| Rhea ID | |
| Cross Reference Brenda |