| IED ID | IndEnz0002004624 |
| Enzyme Type ID | protease004624 |
| 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 | Felis catus (Cat) (Felis silvestris catus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Laurasiatheria Carnivora Feliformia Felidae (cat family) Felinae Felis Felis catus (Cat) (Felis silvestris catus) |
| Enzyme Sequence | MRCLNMIMAEPPGLITICLLGYLLGADCTVFLDHEDATKVLSRPKRYNSGKLEEFVQGNLERECMEEKCSFEEAREVFENTEKTTEFWKQYVDGDQCESNPCLNGGICKDDINSYECWCQTGFEGKNCELDVTCNIKNGRCKQFCKLDADNKVVCSCTTGYQLAEDQKSCEPAVPFPCGRVSVPHISTTHTRAETLFLNMDYENSTTDYENSAEAEKNVDNVTQPLNDLTRIVGGKTAKPGQFPWQVLLKGKIDAFCGGSIINEKWVVTAAHCINPDVEITVVAGEHNTEETEHTEQKRNVIRTILHHSYNASVNKYSHDIALLELDEPLTLNSYVTPICVADREYTNTFLKFGYGYVSGWGKVFNKGRPATILQYLKVPLVDRATCLRSTKFTIYNNMFCAGFHEGGKDSCQGDSGGPHVTEVEGINFLTGIISWGEECAMKGKYGIYTKVSRYVNWIKEKTKLT |
| Enzyme Length | 466 |
| Uniprot Accession Number | Q6SA95 |
| Absorption | |
| Active Site | ACT_SITE 272; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P00740; ACT_SITE 320; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P00740; ACT_SITE 416; /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 (6); Metal binding (35); Modified residue (17); 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;Sulfation;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P00740}. |
| Modified Residue | MOD_RES 53; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00741, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 54; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00741, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 61; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00741, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 63; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00741, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 66; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00741, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 67; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00741, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 72; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00741, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 73; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00741, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 76; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00741, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 79; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00741, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 82; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00741, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 86; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00741, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 110; /note="(3R)-3-hydroxyaspartate"; /evidence="ECO:0000250|UniProtKB:P00740"; MOD_RES 114; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P00740"; MOD_RES 202; /note="Sulfotyrosine"; /evidence="ECO:0000250|UniProtKB:P00740"; MOD_RES 205; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P00740"; MOD_RES 206; /note="Phosphothreonine; alternate"; /evidence="ECO:0000250|UniProtKB:P00740" |
| Post Translational Modification | PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000250|UniProtKB:P00740}.; 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: Predominantly O-glucosylated at Ser-99 by POGLUT1 in vitro. {ECO:0000250|UniProtKB:P00740}. |
| Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 15822564; |
| Motif | |
| Gene Encoded By | |
| Mass | 52,320 |
| Kinetics | |
| Metal Binding | METAL 47; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00740; METAL 48; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P00740; METAL 53; /note=Calcium 1; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 53; /note=Calcium 2; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 54; /note=Calcium 2; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 54; /note=Calcium 3; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 61; /note=Calcium 4; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 61; /note=Magnesium 1; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 63; /note=Calcium 1; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 63; /note=Calcium 2; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 63; /note=Calcium 3; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 66; /note=Calcium 4; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 66; /note=Magnesium 1; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 67; /note=Calcium 1; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 72; /note=Calcium 5; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 72; /note=Magnesium 2; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 73; /note=Calcium 2; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 73; /note=Calcium 3; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 76; /note=Calcium 3; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 76; /note=Calcium 5; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 76; /note=Magnesium 2; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 82; /note=Calcium 6; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 82; /note=Magnesium 3; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 86; /note=Calcium 6; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 86; /note=Magnesium 3; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 93; /note=Calcium 7; /evidence=ECO:0000250|UniProtKB:P00740; METAL 94; /note=Calcium 7; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00740; METAL 96; /note=Calcium 7; /evidence=ECO:0000250|UniProtKB:P00740; METAL 110; /note=Calcium 7; /evidence=ECO:0000250|UniProtKB:P00740; METAL 111; /note=Calcium 7; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00740; METAL 286; /note=Calcium 8; /evidence=ECO:0000250|UniProtKB:P00740; METAL 288; /note=Calcium 8; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00740; METAL 291; /note=Calcium 8; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00740; METAL 293; /note=Calcium 8; /evidence=ECO:0000250|UniProtKB:P00740; METAL 296; /note=Calcium 8; /evidence=ECO:0000250|UniProtKB:P00740 |
| Rhea ID | |
| Cross Reference Brenda |