IED ID | IndEnz0002011181 |
Enzyme Type ID | protease011181 |
Protein Name |
Platelet-aggregating proteinase PA-BJ EC 3.4.21.- Snake venom serine protease SVSP Fragment |
Gene Name | |
Organism | Bothrops jararaca (Jararaca) (Bothrops jajaraca) |
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 jararaca (Jararaca) (Bothrops jajaraca) |
Enzyme Sequence | NSLVIVVGGRPCKINVHRSLVLLYNSSSLLCSGTLINQEWVLTAAHCDSKNFKMKLGVHSIKIRNKNERTRHPKEKFICPNRKKDDVLDKDIMLIRLNRPVSNSEHIAPLSLPSSPPSVGSVCYVMGWGKISSTKETYPDVPHCAKINILDHAVCRAAYTWWPATSTTLCAGILQGGKDTCEGDSGGPLICNGLQGIVSGGGNPCGQPRKPALYTKVFDYLPWIESIIAGTTTATCP |
Enzyme Length | 237 |
Uniprot Accession Number | P81824 |
Absorption | |
Active Site | ACT_SITE 46; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 91; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 185; /note=Charge relay system; /evidence=ECO:0000250 |
Activity Regulation | ACTIVITY REGULATION: Inhibited by PMSF. The amidolytic activity is also inhibited by benzamidine derivatives. |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.21.- |
Enzyme Function | FUNCTION: Snake venom serine protease that induces platelet aggregation through activation of protease-activated platelet receptors (PAR1/F2R and PAR4/F2RL3). On F2R, the cleavage occurs at Arg41-Ser42 (like thrombin cleavage), and Arg46-Asn47. In normal condition of hemostasis, the cleavage of the Arg41-Ser42 bond liberates a new N-terminus that functions as an agonist. However after envenomation, the cleavage of Arg46-Asn47 bond degrades this potential agonist. This may explain why the snake protease is less potent than thrombin in causing platelet aggregation and release reaction. On F2RL3, a thrombin-like activity has also been proven by calcium release from lung fibroblasts transfected with this receptor. Possesses amidolytic activities. {ECO:0000269|PubMed:10908720, ECO:0000269|PubMed:7766629}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1); Disulfide bond (6); Domain (1); Glycosylation (2); Non-terminal residue (1); Propeptide (1); Sequence conflict (7) |
Keywords | Direct protein sequencing;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Platelet aggregation activating toxin;Protease;Secreted;Serine protease;Toxin |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 25,742 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |