| IED ID | IndEnz0002012121 |
| Enzyme Type ID | protease012121 |
| Protein Name |
Zinc metalloproteinase-disintegrin-like batroxstatin-2 EC 3.4.24.- Snake venom metalloprotease SVMP Vascular apoptosis-inducing protein-like VAP-like Fragment |
| 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 | EQQRYLNAKKYVKLVLVADYIMYLKYGRSLTTLRTRMYDIVNIINLIFQRMNIHVALVGLEIWSNRDKIIVQSSADVTLDLFAKWRETDLLKRKSHDNAQLLTGINFNGPTAGLAYLSGICKPMYSAGIVQDHNKVHHLVAIAMAHEMGHNLGMDHDKDTCTCGARSCVMAGTLSCEPSYLFSDCSRRGHRAFLIKDMPQCILEKPLRTDVVSPPVCGNYFVEVGEECDCGSPATCRDTCCDAATCKLRQGAQCAEGLCCDQCRFKGAGTECRAAKDECDMADLCTGRSAECTDRFQRNGQPCQNNNGYCYNGTCPIMRDQCIALFGPNAAVSQDACFQFNLQGNHYGYCRKEQNTKIACEPQDVKCGRLYCFPSSPATKNPCNIHYSPNDEDKGMVLPGTKCADGKACSNGRCVDVT |
| Enzyme Length | 418 |
| Uniprot Accession Number | C5H5D3 |
| Absorption | |
| Active Site | ACT_SITE 147; /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 zinc metalloprotease that induces apoptosis in vascular endothelial cells (VEC), without degrading the extracellular matrix (it cannot cleave collagen) or inhibiting adhesion of VEC. Has also fibrinogenolytic and hemorrhagic activities (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (18); Domain (2); Glycosylation (1); Metal binding (14); Motif (1); Non-terminal residue (1) |
| Keywords | Apoptosis;Calcium;Cell adhesion impairing toxin;Disulfide bond;Fibrinogenolytic toxin;Glycoprotein;Hemorrhagic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;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 278..280; /note=D/ECD-tripeptide |
| Gene Encoded By | |
| Mass | 46,303 |
| Kinetics | |
| Metal Binding | METAL 146; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 150; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 156; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 216; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 219; /note=Calcium 1; /evidence=ECO:0000250; METAL 221; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 223; /note=Calcium 1; /evidence=ECO:0000250; METAL 226; /note=Calcium 1; /evidence=ECO:0000250; METAL 229; /note=Calcium 1; /evidence=ECO:0000250; METAL 280; /note=Calcium 2; /evidence=ECO:0000250; METAL 281; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 283; /note=Calcium 2; /evidence=ECO:0000250; METAL 294; /note=Calcium 2; /evidence=ECO:0000250; METAL 295; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |