| IED ID | IndEnz0010001899 |
| Enzyme Type ID | esterase001899 |
| Protein Name |
Factor V activator RVV-V alpha EC 3.4.21.95 Russel's viper venom FV activator alpha RVV-V alpha Snake venom serine protease SVSP |
| Gene Name | |
| Organism | Daboia siamensis (Eastern Russel's viper) (Daboia russelii siamensis) |
| 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 Viperinae (vipers) Daboia Daboia siamensis (Eastern Russel's viper) (Daboia russelii siamensis) |
| Enzyme Sequence | VVGGDECNINEHPFLVALYTSTSSTIHCGGALINREWVLTAAHCDRRNIRIKLGMHSKNIRNEDEQIRVPRGKYFCLNTKFPNGLDKDIMLIRLRRPVTYSTHIAPVSLPSRSRGVGSRCRIMGWGKISTTEDTYPDVPHCTNIFIVKHKWCEPLYPWVPADSRTLCAGILKGGRDTCHGDSGGPLICNGQIQGIVAGGSEPCGQHLKPAVYTKVFDYNNWIQNIIAGNRTVTCPP |
| Enzyme Length | 236 |
| Uniprot Accession Number | P18964 |
| Absorption | |
| Active Site | ACT_SITE 43; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 88; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 182; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by D-Phe-Pro-Arg-chloromethyl ketone (FPRCK) (97%), PMSF (76%), and benzamidine (50%). Is not inhibited by BPTI, antithrombin and EDTA. {ECO:0000269|PubMed:16807918}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Fully activates human clotting factor V by a single cleavage at the 1545-Trp-Tyr-Leu-Arg-|-Ser-Asn-Asn-Gly-1552 bond. Cattle, but not rabbit, factor V is cleaved, and no other proteins of the clotting system are attacked. Esterase activity is observed on Bz-Arg-OEt and Tos-Arg-OMe, and amidase activity on Phe-pipecolyl-Arg-NHPhNO(2).; EC=3.4.21.95; |
| DNA Binding | |
| EC Number | 3.4.21.95 |
| Enzyme Function | FUNCTION: Venom serine protease that activates factor V (F5) in a calcium-independent manner. It cleaves the Arg(1545)-Ser(1546) linkage in the human factor V molecule. Induces the coagulation of mammalian plasma. {ECO:0000269|PubMed:16807918, ECO:0000269|PubMed:3053712}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (6); Domain (1); Glycosylation (1) |
| Keywords | Blood coagulation cascade activating toxin;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Hydrolase;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 | 26,182 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.95; |