| IED ID | IndEnz0002006046 |
| Enzyme Type ID | protease006046 |
| Protein Name |
Venom prothrombin activator pseutarin-C non-catalytic subunit PCNS vPA Venom coagulation factor Va-like protein Cleaved into: Pseutarin-C non-catalytic subunit heavy chain; Pseutarin-C non-catalytic subunit light 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 | MGRYSVSPVPKCLLLMFLGWSGLKYYQVNAAQLREYHIAAQLEDWDYNPQPEELSRLSESDLTFKKIVYREYELDFKQEEPRDALSGLLGPTLRGEVGDSLIIYFKNFATQPVSIHPQSAVYNKWSEGSSYSDGTSDVERLDDAVPPGQSFKYVWNITAEIGPKKADPPCLTYAYYSHVNMVRDFNSGLIGALLICKEGSLNANGSQKFFNREYVLMFSVFDESKNWYRKPSLQYTINGFANGTLPDVQACAYDHISWHLIGMSSSPEIFSVHFNGQTLEQNHYKVSTINLVGGASVTADMSVSRTGKWLISSLVAKHLQAGMYGYLNIKDCGNPDTLTRKLSFRELMKIKNWEYFIAAEEITWDYAPEIPSSVDRRYKAQYLDNFSNFIGKKYKKAVFRQYEDGNFTKPTYAIWPKERGILGPVIKAKVRDTVTIVFKNLASRPYSIYVHGVSVSKDAEGAIYPSDPKENITHGKAVEPGQVYTYKWTVLDTDEPTVKDSECITKLYHSAVDMTRDIASGLIGPLLVCKHKALSVKGVQNKADVEQHAVFAVFDENKSWYLEDNIKKYCSNPSAVKKDDPKFYKSNVMYTLNGYASDRTEVLRFHQSEVVQWHLTSVGTVDEIVPVHLSGHTFLSKGKHQDILNLFPMSGESATVTMDNLGTWLLSSWGSCEMSNGMRLRFLDANYDDEDEGNEEEEEDDGDIFADIFIPSEVVKKKEEVPVNFVPDPESDALAKELGLIDDEGNPIIQPRREQTEDDEEQLMKASMLGLRSFKGSVAEEELKHTALALEEDAHASDPRIDSNSARNPDDIAGRYLRTINRGNKRRYYIAAEEVLWDYSPIGKSQVRSRAAKTTFKKAIFRSYLDDTFQTPSTGGEYEKHLGILGPIIRAEVDDVIEIQFKNLASRPYSLHAHGLLYEKSSEGRSYDDKSPELFKKDDAIMPNGTYTYVWQVPPRSGPTDNTEKCKSWAYYSGVNPEKDIHSGLIGPILICQKGMIDKYNRTIDIREFVLFFMVFDEEKSWYFPKSDKSTCEEKLIGVQSLHTFPAINGIPYQLQGLTMYKDENVHWHLLNMGGPKDIHVVNFHGQTFTEEGREDNQLGVLPLLPGTFASIKMKPSKIGTWLLETEVGENQERGMQALFTVIDKDCKLPMGLASGIIQDSQISASGHVGYWEPKLARLNNTGKYNAWSIIKKEHEHPWIQIDLQRQVVITGIQTQGTVQLLQHSYTVEYFVTYSEDGQNWITFKGRHSETQMHFEGNSDGTTVKENHIDPPIIARYIRLHPTKFYNRPTFRIELLGCEVEGCSVPLGMESGAIKNSEITASSYKKTWWSSWEPSLARLNLEGGTNAWQPEVNNKDQWLQIDLQHLTKITSIITQGATSMTTSMYVKTFSIHYTDDNSTWKPYLDVRTSMEKVFTGNINSDGHVKHFFKPPILSRFIRIIPKTWNQYIALRIELFGCEVF |
| Enzyme Length | 1460 |
| Uniprot Accession Number | Q7SZN0 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| 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 | Beta strand (95); Chain (2); Disulfide bond (7); Domain (11); Glycosylation (9); Helix (16); Metal binding (8); Propeptide (1); Region (1); Sequence conflict (21); Signal peptide (1); Site (4); Turn (14) |
| Keywords | 3D-structure;Blood coagulation cascade activating toxin;Calcium;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Metal-binding;Pharmaceutical;Prothrombin activator;Reference proteome;Repeat;Secreted;Signal;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12362232, ECO:0000269|PubMed:12730119}. |
| Modified Residue | |
| Post Translational Modification | PTM: In physiological conditions, blood coagulation factor V and factor Va are inactivated by activated protein C (APC) through proteolytic degradation of the heavy chain. However, pseutarin-C non-catalytic subunit (factor V-like protein) retains its full activity even at high concentration of APC. This has two explanations: this protein has only one of the three cleavage sites present in factor V that are targeted by the APC for inactivation, and the binding with the catalytic subunit protect the cleavage site from inactivation. |
| Signal Peptide | SIGNAL 1..30; /evidence=ECO:0000269|PubMed:12730119 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 4BXS; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 165,932 |
| Kinetics | |
| Metal Binding | METAL 124; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000312|PDB:4BXS; METAL 139; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000312|PDB:4BXS; METAL 142; /note=Calcium 1; /evidence=ECO:0000312|PDB:4BXS; METAL 143; /note=Calcium 1; /evidence=ECO:0000312|PDB:4BXS; METAL 920; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000312|PDB:4BXS; METAL 935; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000312|PDB:4BXS; METAL 938; /note=Calcium 2; /evidence=ECO:0000312|PDB:4BXS; METAL 939; /note=Calcium 2; /evidence=ECO:0000312|PDB:4BXS |
| Rhea ID | |
| Cross Reference Brenda |