IED ID | IndEnz0002011453 |
Enzyme Type ID | protease011453 |
Protein Name |
Snake venom serine protease SVSP EC 3.4.21.- Fragment |
Gene Name | |
Organism | Crotalus viridis viridis (Prairie 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 viridis (Western rattlesnake) Crotalus viridis viridis (Prairie rattlesnake) |
Enzyme Sequence | VIGGDECNINEHRFLVALYDPDGFLSGGIL |
Enzyme Length | 30 |
Uniprot Accession Number | P0DJG6 |
Absorption | |
Active Site | |
Activity Regulation | ACTIVITY REGULATION: Inhibited by diisopropylfluorophosphate (DFP). {ECO:0000269|PubMed:3167099}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.21.- |
Enzyme Function | FUNCTION: Snake venom serine protease that catalyzes the hydrolysis of arginine esters, kallikrein substrates Pro-Phe-Arg-MCA and Z-Phe-Arg-MCA. Cleaves kininogen analogs to release bradykinin. Induces contraction of the isolated rat uterus directly at high concentrations, but provokes more forceful contractions when injected in presence of bovine plasma. Shows capillary permeability-increasing activity and hypotensive activity on the anesthetized rat. {ECO:0000269|PubMed:3167099}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Disulfide bond (1); Domain (1); Non-terminal residue (1) |
Keywords | Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Hypotensive agent;Protease;Secreted;Serine protease;Toxin |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
Modified Residue | |
Post Translational Modification | PTM: N-Glycosylated. {ECO:0000250}. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 3,235 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |