| IED ID | IndEnz0002004623 |
| Enzyme Type ID | protease004623 |
| Protein Name |
Coagulation factor IX EC 3.4.21.22 Christmas factor Cleaved into: Coagulation factor IXa light chain; Coagulation factor IXa heavy chain |
| Gene Name | F9 |
| Organism | Gallus gallus (Chicken) |
| 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) Archelosauria Archosauria Dinosauria Saurischia Theropoda Coelurosauria Aves Neognathae Galloanserae Galliformes Phasianidae (turkeys) Phasianinae Gallus Gallus gallus (Chicken) |
| Enzyme Sequence | MAKIPLILSFCLLEAFLGAESTVFIENKEASTVLSRTRRGNSNRLEELIPGNLERECIEEKCSFEEAREVFENTEKTMEFWKIYIDGDQCNSNPCKNGAVCKDGVSSYECMCPPGYGGRNCEIDSTCATKNGGCEHFCRHDTPQKAVCSCASGYKLHEDGKSCKPAVPYPCGRITAPEMRGKVTRTENTIERWNITAHDEGDAHDEALDITEPPPPPTTSAAPAKIVPITKNDTRVVGGYDSVKGQLPWQVHLVDSRGLGFCGGSIINEKWVVTAAHCLEPGDNVTAVAGEYNTKEDDHTEQRRQVVKILPYPTYNRTRNKHHNDIALLELDQPLTFNSYVTPICIGSRDFTNNLLSNGPGTVSGWGSMLYRGRSAIVLQVLTVPFVDRVTCLKSTSTTILHSMFCAGYTAGGKDTCGGDSGGPYTNSIGETWFLTGVTSWGEECAKPGKYGIYTKVAKYVKWIRETTRLT |
| Enzyme Length | 471 |
| Uniprot Accession Number | Q804X6 |
| Absorption | |
| Active Site | ACT_SITE 277; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P00740; ACT_SITE 325; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P00740; ACT_SITE 421; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P00740 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.; EC=3.4.21.22; Evidence={ECO:0000250|UniProtKB:P00740}; |
| DNA Binding | |
| EC Number | 3.4.21.22 |
| Enzyme Function | FUNCTION: Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa. {ECO:0000250|UniProtKB:P00740}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (3); Disulfide bond (11); Domain (4); Glycosylation (1); Metal binding (32); Modified residue (14); Propeptide (2); Signal peptide (1); Site (2) |
| Keywords | Blood coagulation;Calcium;Cleavage on pair of basic residues;Disulfide bond;EGF-like domain;Gamma-carboxyglutamic acid;Glycoprotein;Hemostasis;Hydrolase;Hydroxylation;Magnesium;Metal-binding;Phosphoprotein;Protease;Reference proteome;Repeat;Secreted;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P00740}. |
| 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; MOD_RES 79; /note=4-carboxyglutamate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00463; MOD_RES 103; /note=(3R)-3-hydroxyaspartate; /evidence=ECO:0000250|UniProtKB:P00740; MOD_RES 107; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P00740 |
| Post Translational Modification | PTM: Activated by factor XIa, which excises the activation peptide. The propeptide can also be removed by snake venom protease. {ECO:0000250|UniProtKB:P00740}.; PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000250|UniProtKB:P00740}. |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 51,804 |
| Kinetics | |
| Metal Binding | METAL 41; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P00740; METAL 46; /note=Calcium 1; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 46; /note=Calcium 2; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 47; /note=Calcium 2; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 47; /note=Calcium 3; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 54; /note=Calcium 4; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 54; /note=Magnesium 1; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 56; /note=Calcium 1; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 56; /note=Calcium 2; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 56; /note=Calcium 3; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 59; /note=Calcium 4; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 59; /note=Magnesium 1; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 60; /note=Calcium 1; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 65; /note=Calcium 5; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 65; /note=Magnesium 2; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 66; /note=Calcium 2; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 66; /note=Calcium 3; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 69; /note=Calcium 3; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 69; /note=Calcium 5; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 69; /note=Magnesium 2; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 75; /note=Calcium 6; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 75; /note=Magnesium 3; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 79; /note=Calcium 6; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 79; /note=Magnesium 3; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 86; /note=Calcium 7; /evidence=ECO:0000250|UniProtKB:P00740; METAL 87; /note=Calcium 7; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00740; METAL 89; /note=Calcium 7; /evidence=ECO:0000250|UniProtKB:P00740; METAL 103; /note=Calcium 7; /evidence=ECO:0000250|UniProtKB:P00740; METAL 291; /note=Calcium 8; /evidence=ECO:0000250|UniProtKB:P00740; METAL 293; /note=Calcium 8; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00740; METAL 296; /note=Calcium 8; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00740; METAL 301; /note=Calcium 8; /evidence=ECO:0000250|UniProtKB:P00740 |
| Rhea ID | |
| Cross Reference Brenda |