| IED ID | IndEnz0010001519 |
| Enzyme Type ID | esterase001519 |
| Protein Name |
Factor V activator RVV-V gamma EC 3.4.21.95 Russel's viper venom FV activator gamma RVV-V gamma 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 | MVLIKVLANLLVLQLSYAQKSSELVVGGDECNINEHPFLVALYTSASSTIHCAGALINREWVLTAAHCDRRNIRIKLGMHSKNIRNEDEQIRVPRGKYFCLNTKFPNGLDKDIMLIRLRRPVTYSTHIAPVSLPSRSRGVGSRCRIMGWGKISTTEDTYPDVPHCTNIFIVKHKWCEPLYPWVPADSRTLCAGILKGGRDTCHGDSGGPLICNGEMHGIVAGGSEPCGQHLKPAVYTKVFDYNNWIQSIIAGNRTVTCPP |
| Enzyme Length | 260 |
| Uniprot Accession Number | P18965 |
| Absorption | |
| Active Site | ACT_SITE 67; /note=Charge relay system; /evidence=ECO:0000269|PubMed:21871889; ACT_SITE 112; /note=Charge relay system; /evidence=ECO:0000269|PubMed:21871889; ACT_SITE 206; /note=Charge relay system; /evidence=ECO:0000269|PubMed:21871889 |
| Activity Regulation | |
| 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 selectively 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:3053712}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (15); Chain (1); Disulfide bond (6); Domain (1); Glycosylation (1); Helix (5); Propeptide (1); Sequence conflict (1); Signal peptide (1); Turn (1) |
| Keywords | 3D-structure;Blood coagulation cascade activating toxin;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Protease;Secreted;Serine protease;Signal;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3053712}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 3S9A; 3S9B; 3S9C; 3SBK; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 28,823 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |