Detail Information for IndEnz0002013599
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