| IED ID | IndEnz0002005411 |
| Enzyme Type ID | protease005411 |
| Protein Name |
Coagulation factor IX EC 3.4.21.22 Christmas factor Cleaved into: Coagulation factor IXa light chain; Coagulation factor IXa heavy chain Fragment |
| Gene Name | F9 |
| Organism | Sus scrofa (Pig) |
| 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 Artiodactyla Suina Suidae (pigs) Sus Sus scrofa (Pig) |
| Enzyme Sequence | YNSGKLEESFVRGNLERECIEEKCSFEEAREVFENTEKTNEFWKQYVDGDQCEPNPCLNGGLCKDDINSYECWCQVGFEGKNCELDATCNIKNGRCKQFCKTGADSKVLCSCTTGYRLAPDQKSCKPAVPFPCGRVSVSHSPTTLTRAEIIFSNMDYENSTEVEPILDSLTESNQSSDDFIRIVGGENAKPGQFPWQVLLNGKIDAFCGGSIINEKWVVTAAHCIEPGVKITVVAGEYNTEETEPTEQRRNVIRAIPHHSYNATVNKYSHDIALLELDEPLTLNSYVTPICIADKEYTNIFLKFGSGYVSGWGRVFNRGRSATILQYLKVPLVDRATCLRSTKVTIYSNMFCAGFHEGGKDSCLGDSGGPHVTEVEGTSFLTGIISWGEECAVKGKYGIYTKVSRYVNW |
| Enzyme Length | 409 |
| Uniprot Accession Number | P16293 |
| Absorption | |
| Active Site | ACT_SITE 223; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P00740; ACT_SITE 271; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P00740; ACT_SITE 367; /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); Beta strand (26); Chain (3); Disulfide bond (11); Domain (4); Glycosylation (4); Helix (8); Metal binding (35); Modified residue (17); Non-terminal residue (1); Propeptide (1); Site (2); Turn (5) |
| Keywords | 3D-structure;Blood coagulation;Calcium;Direct protein sequencing;Disulfide bond;EGF-like domain;Gamma-carboxyglutamic acid;Glycoprotein;Hemostasis;Hydrolase;Hydroxylation;Magnesium;Metal-binding;Phosphoprotein;Protease;Reference proteome;Repeat;Secreted;Serine protease;Sulfation;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P00740}. |
| Modified Residue | MOD_RES 7; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00741, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 8; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00741, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 16; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00741, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 18; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00741, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 21; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00741, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 22; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00741, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 27; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00741, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 28; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00741, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 31; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00741, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 34; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00741, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 37; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00741, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 41; /note="4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00741, ECO:0000255|PROSITE-ProRule:PRU00463"; MOD_RES 65; /note="(3R)-3-hydroxyaspartate"; /evidence="ECO:0000250|UniProtKB:P00740"; MOD_RES 69; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P00740"; MOD_RES 157; /note="Sulfotyrosine"; /evidence="ECO:0000250|UniProtKB:P00740"; MOD_RES 160; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P00740"; MOD_RES 161; /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}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 1PFX; 1X7A; |
| Mapped Pubmed ID | 15454208; |
| Motif | |
| Gene Encoded By | |
| Mass | 45,516 |
| Kinetics | |
| Metal Binding | METAL 1; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00740; METAL 2; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P00740; METAL 7; /note=Calcium 1; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 7; /note=Calcium 2; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 8; /note=Calcium 2; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 8; /note=Calcium 3; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 16; /note=Calcium 4; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 16; /note=Magnesium 1; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 18; /note=Calcium 1; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 18; /note=Calcium 2; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 18; /note=Calcium 3; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 21; /note=Calcium 4; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 21; /note=Magnesium 1; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 22; /note=Calcium 1; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 27; /note=Calcium 5; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 27; /note=Magnesium 2; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 28; /note=Calcium 2; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 28; /note=Calcium 3; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 31; /note=Calcium 3; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 31; /note=Calcium 5; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 31; /note=Magnesium 2; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 37; /note=Calcium 6; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 37; /note=Magnesium 3; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 41; /note=Calcium 6; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 41; /note=Magnesium 3; via 4-carboxyglutamate; /evidence=ECO:0000250|UniProtKB:P00740; METAL 48; /note=Calcium 7; /evidence=ECO:0000250|UniProtKB:P00740; METAL 49; /note=Calcium 7; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00740; METAL 51; /note=Calcium 7; /evidence=ECO:0000250|UniProtKB:P00740; METAL 65; /note=Calcium 7; /evidence=ECO:0000250|UniProtKB:P00740; METAL 66; /note=Calcium 7; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00740; METAL 237; /note=Calcium 8; /evidence=ECO:0000250|UniProtKB:P00740; METAL 239; /note=Calcium 8; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00740; METAL 242; /note=Calcium 8; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00740; METAL 244; /note=Calcium 8; /evidence=ECO:0000250|UniProtKB:P00740; METAL 247; /note=Calcium 8; /evidence=ECO:0000250|UniProtKB:P00740 |
| Rhea ID | |
| Cross Reference Brenda |