Detail Information for IndEnz0010001515
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;