IED ID | IndEnz0002013599 |
Enzyme Type ID | protease013599 |
Protein Name |
Snake venom metalloproteinase crotalin SVMP EC 3.4.24.- Fragments |
Gene Name | |
Organism | Crotalus atrox (Western diamondback 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 atrox (Western diamondback rattlesnake) |
Enzyme Sequence | LLRRKSHDHAQNHDGDKCLRGASLGYYQSFLNQYKPQCILNKP |
Enzyme Length | 43 |
Uniprot Accession Number | P0DJ42 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.24.- |
Enzyme Function | FUNCTION: Snake venom zinc metalloproteinase that inhibits ristocin-induced platelet aggregation by abolishing the binding of von Willebrand factor (vWF) to platelet glycoprotein Ib alpha (GPIBA) through the cleavage of both GP1BA and vWF. Also has fibrinogenolytic activities by degrading the alpha- (FGA) and beta-chain (FGB) of fibrinogen. In vivo, induces a slight hemorrhage when applied to chick chorioallantoic membrane and has potent antithrombic effect. {ECO:0000269|PubMed:11776320, ECO:0000269|PubMed:9473223}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Disulfide bond (2); Domain (1); Metal binding (1); Non-adjacent residues (2); Non-terminal residue (1) |
Keywords | Direct protein sequencing;Disulfide bond;Fibrinogenolytic 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. |
Modified Residue | |
Post Translational Modification | PTM: This protein autoproteolytically degrades to 10 kDa and 14 kDa fragments in the presence of SDS. Interestingly, the two fragments, as well as reduced crotalin are able to bind vWF, indicating that the binding activity does not require a specific protein conformation. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 5,015 |
Kinetics | |
Metal Binding | METAL 13; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
Rhea ID | |
Cross Reference Brenda |