| IED ID | IndEnz0002009961 |
| Enzyme Type ID | protease009961 |
| Protein Name |
Coagulation factor X-activating enzyme heavy chain EC 3.4.24.58 Coagulation factor X-activating enzyme chain alpha Snake venom metalloproteinase SVMP VL factor X activator VLFXA heavy chain Cleaved into: Coagulation factor X-activating enzyme heavy chain alternate form |
| Gene Name | |
| Organism | Macrovipera lebetina (Levantine viper) (Vipera lebetina) |
| 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) Macrovipera Macrovipera lebetina (Levantine viper) (Vipera lebetina) |
| Enzyme Sequence | MMQVLLVTISLAVFPYQGSSIILESGNVNDYEVVYPQKITALPEEAVQQPEQKYEDTMQYEFEVNGEPVVLHLEKNKDLFSEDYSETRYSPDGRETTTKPPVQDHCYYHGRIQNDAYSSASISACNGLKGHFKLQGETYLIEPLKIPDSEAHAVYKYENIEKEDEAPKMCGVTQTNWESDEPIKKASQLVATSAKRKFHKTFIELVIVVDHRVVKKYDSAATNTKIYEIVNTVNEIFIPLNIRLTLIGVEFWCNRDLINVTSSADDTLDSFGEWRGSDLLNRKRHDNAQLFTDMKFDLSTLGITFLDGMCQAYRSVGIVQEHGNKNFKTAVIMAHELGHNLGMYHDRKNCICNDSSCIMSAVLSSQPSKLFSNCSNHDYRRYLTTYKPKCILNPPLRKDIASPPICGNEIWEEGEECDCGSPKDCQNPCCDAATCKLTPGAECGNGLCCEKCKIKTAGTVCRRARDECDVPEHCTGQSAECPADGFHANGQPCQNNNGYCYNGDCPIMTKQCISLFGSRATVAEDSCFQENQKGSYYGYCRKENGRKIPCAPQDIKCGRLYCLDNSPGNKNPCKMHYRCRDQHKGMVEPGTKCEDGKVCNNKRQCVDVNTAY |
| Enzyme Length | 612 |
| Uniprot Accession Number | Q7T046 |
| Absorption | |
| Active Site | ACT_SITE 336; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Calcium is required for the activity of the heterotrimer. {ECO:0000269|PubMed:11910177}. |
| 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; |
| 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(234)-Ile(235) bond, activates coagulation factor IX (F9) by cleaving the Arg(226)-Val(227) bond and is also able to activate protein C (PROC). {ECO:0000269|PubMed:11731090, ECO:0000269|PubMed:11910177}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:11910177}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (2); Disulfide bond (5); Domain (2); Glycosylation (3); Metal binding (12); Motif (1); Propeptide (1); Signal peptide (1) |
| Keywords | Blood coagulation cascade activating toxin;Calcium;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Toxin;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. Contains 8.0% of hexoses, 2.5% of hexosamines and 2.5% of sialic acids. {ECO:0000269|PubMed:11731090, ECO:0000269|PubMed:11910177, ECO:0000269|PubMed:15450849}. |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 467..469; /note=D/ECD-tripeptide |
| Gene Encoded By | |
| Mass | 68,775 |
| Kinetics | |
| Metal Binding | METAL 204; /note=Calcium 1; /evidence=ECO:0000250; METAL 286; /note=Calcium 1; /evidence=ECO:0000250; METAL 335; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 339; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 345; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 390; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 393; /note=Calcium 1; /evidence=ECO:0000250; METAL 405; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 408; /note=Calcium 2; /evidence=ECO:0000250; METAL 412; /note=Calcium 2; /evidence=ECO:0000250; METAL 415; /note=Calcium 2; /evidence=ECO:0000250; METAL 418; /note=Calcium 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |