| IED ID | IndEnz0002004994 |
| Enzyme Type ID | protease004994 |
| 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 | Canis lupus familiaris (Dog) (Canis familiaris) |
| 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 Caniformia Canidae (dog coyote wolf fox) Canis Canis lupus (Gray wolf) Canis lupus familiaris (Dog) (Canis familiaris) |
| Enzyme Sequence | MAEASGLVTVCLLGYLLSAECAVFLDRENATKILSRPKRYNSGKLEEFVRGNLERECIEEKCSFEEAREVFENTEKTTEFWKQYVDGDQCESNPCLNDGVCKDDINSYECWCRAGFEGKNCELDVTCNIKNGRCKQFCKLGPDNKVVCSCTTGYQLAEDQRSCEPAVPFPCGRVSVPHISMTRTRAETLFSNMDYENSTEVEKILDNVTQPLNDFTRVVGGKDAKPGQFPWQVLLNGKVDAFCGGSIINEKWVVTAAHCIEPDVKITIVAGEHNTEKREHTEQKRNVIRTILHHSYNATINKYNHDIALLELDEPLTLNSYVTPICIADREYSNIFLKFGSGYVSGWGRVFNKGRSASILQYLKVPLVDRATCLRSTKFTIYNNMFCAGFHEGGKDSCQGDSGGPHVTEVEGISFLTGIISWGEECAMKGKYGIYTKVSRYVNWIKEKTKLT |
| Enzyme Length | 452 |
| Uniprot Accession Number | P19540 |
| Absorption | |
| Active Site | ACT_SITE 258; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P00740; ACT_SITE 306; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P00740; ACT_SITE 402; /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, ECO:0000269|PubMed:2367529, ECO:0000269|PubMed:2481310}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (3); Disulfide bond (11); Domain (4); Glycosylation (8); Metal binding (34); Modified residue (17); Natural variant (1); Propeptide (2); Signal peptide (1); Site (2) |
| Keywords | Blood coagulation;Calcium;Cleavage on pair of basic residues;Disease variant;Disulfide bond;EGF-like domain;Gamma-carboxyglutamic acid;Glycoprotein;Hemophilia;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:0000269|PubMed:2367529}. |
| Modified Residue | MOD_RES 46; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00741, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 47; /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 56; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00741, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 59; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00741, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 60; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00741, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 65; /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 69; /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 75; /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 103; /note="(3R)-3-hydroxyaspartate"; /evidence="ECO:0000250|UniProtKB:P00740"; MOD_RES 107; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P00740"; MOD_RES 195; /note="Sulfotyrosine"; /evidence="ECO:0000250|UniProtKB:P00740"; MOD_RES 198; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P00740"; MOD_RES 199; /note="Phosphothreonine; alternate"; /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}.; PTM: Predominantly O-glucosylated at Ser-92 by POGLUT1 in vitro. {ECO:0000250|UniProtKB:P00740}. |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 18449417; 22482117; 22919027; 23043073; |
| Motif | |
| Gene Encoded By | |
| Mass | 50,828 |
| Kinetics | |
| Metal Binding | METAL 40; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00740; 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 104; /note=Calcium 7; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00740; METAL 272; /note=Calcium 8; /evidence=ECO:0000250|UniProtKB:P00740; METAL 274; /note=Calcium 8; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00740; METAL 279; /note=Calcium 8; /evidence=ECO:0000250|UniProtKB:P00740; METAL 282; /note=Calcium 8; /evidence=ECO:0000250|UniProtKB:P00740 |
| Rhea ID | |
| Cross Reference Brenda |