| IED ID | IndEnz0002010625 |
| Enzyme Type ID | protease010625 |
| Protein Name |
Coagulation factor X-activating enzyme heavy chain EC 3.4.24.58 Coagulation factor X-activating enzyme chain alpha RVV-X heavy chain Russellysin Snake venom metalloproteinase SVMP |
| Gene Name | |
| Organism | Daboia siamensis (Eastern Russel's viper) (Daboia russelii siamensis) |
| 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) Daboia Daboia siamensis (Eastern Russel's viper) (Daboia russelii siamensis) |
| Enzyme Sequence | MMQVLLVTISLAVFPYQGSSIILESGNVNDYEVVYPQKVTALPKGAVQQPEQKYEDTMQYEFEVNGEPVVLHLEKNKILFSEDYSETHYYPDGREITTNPPVEDHCYYHGRIQNDAHSSASISACNGLKGHFKLRGEMYFIEPLKLSNSEAHAVYKYENIEKEDEIPKMCGVTQTNWESDKPIKKASQLVSTSAQFNKIFIELVIIVDHSMAKKCNSTATNTKIYEIVNSANEIFNPLNIHVTLIGVEFWCDRDLINVTSSADETLNSFGEWRASDLMTRKSHDNALLFTDMRFDLNTLGITFLAGMCQAYRSVEIVQEQGNRNFKTAVIMAHELSHNLGMYHDGKNCICNDSSCVMSPVLSDQPSKLFSNCSIHDYQRYLTRYKPKCIFNPPLRKDIVSPPVCGNEIWEEGEECDCGSPANCQNPCCDAATCKLKPGAECGNGLCCYQCKIKTAGTVCRRARDECDVPEHCTGQSAECPRDQLQQNGKPCQNNRGYCYNGDCPIMRNQCISLFGSRANVAKDSCFQENLKGSYYGYCRKENGRKIPCAPQDVKCGRLFCLNNSPRNKNPCNMHYSCMDQHKGMVDPGTKCEDGKVCNNKRQCVDVNTAYQSTTGFSQI |
| Enzyme Length | 619 |
| Uniprot Accession Number | Q7LZ61 |
| Absorption | |
| Active Site | ACT_SITE 334; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Specifically activates several components of the blood clotting system, including coagulation factor X, coagulation factor IX and protein C by cleavage of Arg-|-Xaa bonds. Has no action on insulin B chain.; EC=3.4.24.58; Evidence={ECO:0000269|PubMed:1629211, ECO:0000269|PubMed:8144654}; |
| DNA Binding | |
| EC Number | 3.4.24.58 |
| Enzyme Function | FUNCTION: Catalytic subunit of blood coagulation factor X-activating enzyme. Activates coagulation factor X (F10) by cleaving the Arg-Ile bond and is also able to activate coagulation factor IX (F9) and protein S (PROS1) by specific cleavage of Arg-Ile and Arg-Val bonds. {ECO:0000269|PubMed:18616470}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (12); Chain (1); Disulfide bond (19); Domain (2); Glycosylation (4); Helix (12); Metal binding (14); Motif (1); Propeptide (1); Sequence conflict (1); Signal peptide (1); Turn (5) |
| Keywords | 3D-structure;Blood coagulation cascade activating toxin;Calcium;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Toxin;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated; probably required for conformation. Removal of easily accessible sugars does not change its functional capacity, but removal of the core sugars with N-glycanase causes a virtually complete loss of enzyme activity, apparently as a result of major conformational changes in the molecule. Not O-glycosylated. {ECO:0000269|PubMed:1629211, ECO:0000269|PubMed:18060879, ECO:0000269|PubMed:18616470, ECO:0000269|PubMed:8144654}. |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 2E3X; |
| Mapped Pubmed ID | - |
| Motif | MOTIF 465..467; /note=D/ECD-tripeptide |
| Gene Encoded By | |
| Mass | 69,648 |
| Kinetics | |
| Metal Binding | METAL 333; /note=Zinc; catalytic; METAL 337; /note=Zinc; catalytic; METAL 343; /note=Zinc; catalytic; METAL 403; /note=Calcium 1; via carbonyl oxygen; METAL 406; /note=Calcium 1; METAL 408; /note=Calcium 1; via carbonyl oxygen; METAL 410; /note=Calcium 1; METAL 413; /note=Calcium 1; METAL 416; /note=Calcium 1; METAL 467; /note=Calcium 2; METAL 468; /note=Calcium 2; via carbonyl oxygen; METAL 470; /note=Calcium 2; METAL 482; /note=Calcium 2; METAL 483; /note=Calcium 2; via carbonyl oxygen |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.58; |