IED ID | IndEnz0010001515 |
Enzyme Type ID | esterase001515 |
Protein Name |
Factor V activator FVA VLFVA EC 3.4.21.95 Lebetina viper venom FV activator LVV-V Snake venom serine protease SVSP |
Gene Name | |
Organism | Macrovipera lebetina (Levantine viper) (Vipera lebetina) |
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) Macrovipera Macrovipera lebetina (Levantine viper) (Vipera lebetina) |
Enzyme Sequence | MVLIRVLANLLVLQLSYAQKSSELVVGGDECDINEHPFLVALYTSSSSTVHCAGTLINQEWVLTAVHCDRKNIRIKLGMHSKNIRNEDEQIRVPRRKFFCLNTKFPNGKDKDIMLIRLRRPVKNSAHIAPISLPSSPSSPRSRCRIMGWGKISTTEETYPDVPHCAKIFIVKHAWCEALYPWVPADSRTLCAGILQGGKDTCEGDSGGPLICNGQIQGIVSGGSDPCGQRLKPAVYTKVFDYTDWIQSIIAGNTTATCP |
Enzyme Length | 259 |
Uniprot Accession Number | Q9PT41 |
Absorption | |
Active Site | ACT_SITE 67; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 112; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 206; /note=Charge relay system; /evidence=ECO:0000250 |
Activity Regulation | ACTIVITY REGULATION: Inhibited by D-Phe-Pro-Arg-chloromethyl ketone (FPRCK) (98%), PMSF (93%), benzamidine (67%), and diisopropylfluorophosphate (DFP). Is not inhibited by BPTI, antithrombin and EDTA. {ECO:0000269|PubMed:16807918, ECO:0000269|PubMed:9920400}. |
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 converts factor V (F5) to the active form Va in the presence of calcium ions and phospholipids. It cleaves the Arg(1545)-Ser(1546) linkage in the human factor V molecule. Has hydrolytic activities against BAEE (1.2 U/mg), TAME, and Pro-Phe-Arg-MCA (4.9 U/mg). Shows coagulant activity. {ECO:0000269|PubMed:11910177, ECO:0000269|PubMed:16807918, ECO:0000269|PubMed:9920400}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1); Disulfide bond (6); Domain (1); Glycosylation (1); Propeptide (1); Signal peptide (1) |
Keywords | Blood coagulation cascade activating toxin;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Protease;Secreted;Serine protease;Sialic acid;Signal;Toxin |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
Modified Residue | |
Post Translational Modification | PTM: N-glycosylated. Contains 4.4% of hexoses, 4.4% of hexosamines and 3.1% of sialic acids. {ECO:0000269|PubMed:11910177}. |
Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000250 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 28,595 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.4.21.95; |