Detail Information for IndEnz0002019382
IED ID IndEnz0002019382
Enzyme Type ID protease019382
Protein Name Venom prothrombin activator trocarin-D
vPA
EC 3.4.21.6
Venom coagulation factor Xa-like protease

Cleaved into: Trocarin-D light chain; Trocarin-D heavy chain
Gene Name
Organism Tropidechis carinatus (Australian rough-scaled snake)
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 Elapidae Notechinae Tropidechis Tropidechis carinatus (Australian rough-scaled snake)
Enzyme Sequence MAPQLLLCLILTFLWSLPEAESNVFLKSKVANRFLQRTKRSNSLFEEIRPGNIERECIEEKCSKEEAREVFEDNEKTETFWNVYVDGDQCSSNPCHYRGTCKDGIGSYTCTCLPNYEGKNCEKVLYQSCRVDNGNCWHFCKRVQSETQCSCAESYRLGVDGHSCVAEGDFSCGRNIKARNKREASLPDFVQSQKATLLKKSDNPSPDIRIVNGMDCKLGECPWQAVLINEKGEVFCGGTILSPIHVLTAAHCINQTKSVSVIVGEIDISRKETRRLLSVDKIYVHTKFVPPNYYYVHQNFDRVAYDYDIAIIRMKTPIQFSENVVPACLPTADFANEVLMKQDSGIVSGFGRIQFKQPTSNTLKVITVPYVDRHTCMLSSDFRITQNMFCAGYDTLPQDACQGDSGGPHITAYRDTHFITGIISWGEGCARKGKYGVYTKVSKFIPWIKKIMSLK
Enzyme Length 455
Uniprot Accession Number P81428
Absorption
Active Site ACT_SITE 251; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 308; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 405; /note=Charge relay system; /evidence=ECO:0000250
Activity Regulation ACTIVITY REGULATION: Activated by calcium and phospholipids.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.; EC=3.4.21.6;
DNA Binding
EC Number 3.4.21.6
Enzyme Function FUNCTION: Snake prothrombin activator that attacks the hemostatic system of prey. This protein is functionally similar to blood coagulation factor Xa. Induces cyanosis and death in mice at 1 mg/kg body weight during blood clotting. {ECO:0000269|PubMed:10397729}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (2); Disulfide bond (12); Domain (4); Glycosylation (2); Modified residue (11); Propeptide (2); Sequence conflict (1); Signal peptide (1); Site (1)
Keywords Blood coagulation cascade activating toxin;Calcium;Cleavage on pair of basic residues;Direct protein sequencing;Disulfide bond;EGF-like domain;Gamma-carboxyglutamic acid;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Protease;Prothrombin activator;Repeat;Secreted;Serine protease;Sialic acid;Signal;Toxin
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10397729, ECO:0000269|PubMed:12871464}.
Modified Residue MOD_RES 46; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:10397729"; MOD_RES 47; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:10397729"; MOD_RES 54; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:10397729"; MOD_RES 56; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:10397729"; MOD_RES 59; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:10397729"; MOD_RES 60; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:10397729"; MOD_RES 65; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:10397729"; MOD_RES 66; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:10397729"; MOD_RES 69; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:10397729"; MOD_RES 72; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:10397729"; MOD_RES 75; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:10397729"
Post Translational Modification PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation. These residues are essential for the binding of calcium. {ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:10397729}.; PTM: The O-linked saccharides at Ser-92 are a mixture of Xyl-Glc, and Glc along with smaller amounts of Xyl-GlcNAc, GlcNAc, Gal, GalNAc, Xyl-Gal, and Xyl-GalNAc, suggesting that the glycosyl transferases responsible for this modification are non-specific. The N-linked carbohydrate at Asn-254 (Asn-45 of the heavy chain) is a sialylated and diantennary oligosaccharide. {ECO:0000269|PubMed:10397729, ECO:0000269|PubMed:12871464}.
Signal Peptide SIGNAL 1..20; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 51,407
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.21.6;