IED ID | IndEnz0002005429 |
Enzyme Type ID | protease005429 |
Protein Name |
Venom prothrombin activator nigrarin-D vPA EC 3.4.21.6 Venom coagulation factor Xa-like protease Cleaved into: Nigrarin-D light chain; Nigrarin-D heavy chain |
Gene Name | |
Organism | Cryptophis nigrescens (Eastern small-eyed snake) (Rhinoplocephalus nigrescens) |
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 Cryptophis Cryptophis nigrescens (Eastern small-eyed snake) (Rhinoplocephalus nigrescens) |
Enzyme Sequence | MAPPLLLCLILTFLWNLPEAESNVFLKSKVANRFLQRTKRSNSIFEEFKAGNIERECIEEKCSKEEAREVFEDNEKTETFWNVYVDGDQCSSNPCHYRGTCKDGIGSYTCTCLPNYEGKNCEKVLFESCRVFNGNCWHFCKSVQNEIQCSCAESYRLGDDGHSCVAEGDFSCGRNIKARNKREASLPDFVQSQKAILLKKSDNPSPDIRIINGMDCKLGECPWQAVLLDEDDDVFCGGTILSSIHVLTAAHCINQTKNISVIVGEIDISRKETIRLLPVDKVYVHTKFVPPSYLYGHQNVDRKTYDYDIAIIRMKTPIQFSENVVPACLPTADFVKQVLMKQDFGIVSGFGRTQYRGQTSNTLKVITVPYVDRRTCMLSSDFPITPNMFCAGYDTLPQDACQGDSGGPHITAYGDTHFITGINSWGEGCAKKGKYGVYTKVSNFIPWIKAIMSLK |
Enzyme Length | 455 |
Uniprot Accession Number | B5G6G5 |
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 | |
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 (By similarity). {ECO:0000250}. |
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); Signal peptide (1) |
Keywords | Blood coagulation cascade activating toxin;Calcium;Cleavage on pair of basic residues;Disulfide bond;EGF-like domain;Gamma-carboxyglutamic acid;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Protease;Prothrombin activator;Repeat;Secreted;Serine protease;Signal;Toxin |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
Modified Residue | MOD_RES 46; /note=4-carboxyglutamate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00463; MOD_RES 47; /note=4-carboxyglutamate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00463; MOD_RES 54; /note=4-carboxyglutamate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00463; MOD_RES 56; /note=4-carboxyglutamate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00463; MOD_RES 59; /note=4-carboxyglutamate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00463; MOD_RES 60; /note=4-carboxyglutamate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00463; MOD_RES 65; /note=4-carboxyglutamate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00463; MOD_RES 66; /note=4-carboxyglutamate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00463; MOD_RES 69; /note=4-carboxyglutamate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00463; MOD_RES 72; /note=4-carboxyglutamate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00463; MOD_RES 75; /note=4-carboxyglutamate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00463 |
Post Translational Modification | PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium. {ECO:0000250}. |
Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 51,144 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |