| IED ID | IndEnz0002006023 |
| Enzyme Type ID | protease006023 |
| Protein Name |
Venom prothrombin activator pseutarin-C catalytic subunit PCCS vPA EC 3.4.21.6 Venom coagulation factor Xa-like protease Cleaved into: Pseutarin-C catalytic subunit light chain; Pseutarin-C catalytic subunit heavy chain |
| Gene Name | |
| Organism | Pseudonaja textilis (Eastern brown 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 Acanthophiinae Pseudonaja Pseudonaja textilis (Eastern brown snake) |
| Enzyme Sequence | MAPQLLLCLILTFLWSLPEAESNVFLKSKVANRFLQRTKRANSLVEEFKSGNIERECIEERCSKEEAREVFEDDEKTETFWNVYVDGDQCSSNPCHYRGICKDGIGSYTCTCLSGYEGKNCERVLYKSCRVDNGNCWHFCKSVQNDIQCSCAEGYLLGEDGHSCVAGGNFSCGRNIKTRNKREASLPDFVQSHNATLLKKSDNPSPDIRIVNGMDCKLGECPWQAALVDDKKGVFCGGTILSPIYVLTAAHCINETETISVVVGEIDRSRAETGPLLSVDKVYVHKKFVPPKKSQEFYEKFDLVSYDYDIAIIQMKTPIQFSENVVPACLPTADFANQVLMKQDFGIVSGFGGIFERGPNSKTLKVLKVPYVDRHTCMLSSNFPITPTMFCAGYDTLPQDACQGDSGGPHITAYRDTHFITGIVSWGEGCARKGRYGIYTKLSKFIPWIKRIMRQKLPSTESSTGRL |
| Enzyme Length | 467 |
| Uniprot Accession Number | Q56VR3 |
| Absorption | |
| Active Site | ACT_SITE 251; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 309; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 406; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Activated by calcium and negatively charged phospholipids. {ECO:0000269|PubMed:12362232, ECO:0000269|PubMed:23869089}. |
| 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; Evidence={ECO:0000269|PubMed:12362232, ECO:0000269|PubMed:23869089}; |
| DNA Binding | |
| EC Number | 3.4.21.6 |
| Enzyme Function | FUNCTION: Snake prothrombin activator that attacks the hemostatic system of prey. This non-catalytic subunit is functionally similar to blood coagulation factor V (PubMed:12362232, PubMed:23869089). It serves as a critical cofactor for the prothrombinase activity of the catalytic subunit, which is similar to the blood coagulation factor X (PubMed:12362232, PubMed:23869089). The complex converts prothrombin to thrombin by sequential cleavage at two positions, Arg-320 followed by Arg-271 (PubMed:23869089). Cleavage at Arg-320 produces an active intermediate known as meizothrombin (PubMed:23869089). Meizothrombin is the 'second' substrate for prothrombinase, and it docks in an altered manner to present the second cleavage site (271) (PubMed:23869089). Cleavage at Arg-271 releases active thrombin from its pro-fragment (PubMed:23869089). This order of events is reversed if the protease component of prothrombinase is used on its own, suggesting that the 271 site is inherently more accessible to proteolysis (PubMed:23869089). The complex converts prothrombin to thrombin in presence but also in the absence of membrane (PubMed:23869089). {ECO:0000269|PubMed:12362232, ECO:0000269|PubMed:23869089}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (21); Chain (2); Disulfide bond (12); Domain (4); Glycosylation (2); Helix (9); Modified residue (10); Propeptide (2); Sequence conflict (19); Signal peptide (1); Site (3); Turn (4) |
| Keywords | 3D-structure;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;Pharmaceutical;Protease;Prothrombin activator;Reference proteome;Repeat;Secreted;Serine protease;Signal;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12362232, ECO:0000269|PubMed:3075905}. |
| Modified Residue | MOD_RES 46; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:12362232"; MOD_RES 47; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:12362232"; MOD_RES 54; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:12362232"; MOD_RES 56; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:12362232"; MOD_RES 59; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:12362232"; MOD_RES 60; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:12362232"; MOD_RES 65; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:12362232"; MOD_RES 66; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:12362232"; MOD_RES 69; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 72; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463" |
| 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:12362232}. |
| Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 4BXS; 4BXW; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 52,215 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.60; |