IED Industry Enzyme Database

Detail Information for IndEnz0002005413
IED ID IndEnz0002005413
Enzyme Type ID protease005413
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 Cf9
Organism Rattus norvegicus (Rat)
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 Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat)
Enzyme Sequence MADAPGLIPIFLLGYLLSTECAVFLDRENATKILTRPKRYNSGKLEEFVQGNLERECIEERCSFEEAREVFENTEKTTEFWKQYVDGDQCESNPCLNGGICKDDINSYECWCQAGFEGRNCELDATCSIKNGRCKQFCKNSPDNKIICSCTEGYQLAEDQKSCEPAVPFPCGRVSVAYNSKKITRAETVFSNTDYGNSTELILDDITNSTILDNLTENSEPINDFTRVVGGENAKPGQIPWQVILNGEIEAFCGGAIINEKWIVTAAHCLKPGDKIEVVAGEHNIDEKEDTEQRRNVIRTIPHHQYNATINKYSHDIALLELDKPLILNSYVTPICVANKEYTNIFLKFGSGYVSGWGKVFNKGRQASILQYLRVPLVDRATCLRSTKFSIYNNMFCAGYREGGKDSCEGDSGGPHVTEVEGTSFLTGIISWGEECAMKGKYGIYTKVSRYVNWIKEKTKLT
Enzyme Length 462
Uniprot Accession Number P16296
Absorption
Active Site ACT_SITE 268; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P00740; ACT_SITE 316; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P00740; ACT_SITE 412; /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 (3); Glycosylation (8); Metal binding (35); Modified residue (17); Propeptide (2); Signal peptide (1); Site (2)
Keywords Blood coagulation;Calcium;Disulfide bond;EGF-like domain;Gamma-carboxyglutamic acid;Glycoprotein;Hemostasis;Hydrolase;Hydroxylation;Magnesium;Metal-binding;Phosphoprotein;Protease;Reference proteome;Secreted;Serine protease;Signal;Sulfation;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P00740}.
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 10048754; 12000738; 20838739; 25790442;
Motif
Gene Encoded By
Mass 51,808
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, ECO:0000250|UniProtKB:P00741"; METAL 54; /note="Magnesium 1; via 4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00740, ECO:0000250|UniProtKB:P00741"; 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, ECO:0000250|UniProtKB:P00741"; METAL 59; /note="Magnesium 1; via 4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00740, ECO:0000250|UniProtKB:P00741"; 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, ECO:0000250|UniProtKB:P00741"; METAL 65; /note="Magnesium 2; via 4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00740, ECO:0000250|UniProtKB:P00741"; 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:P00741"; METAL 75; /note="Magnesium 3; via 4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00741"; METAL 79; /note="Calcium 6; via 4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00741"; METAL 79; /note="Magnesium 3; via 4-carboxyglutamate"; /evidence="ECO:0000250|UniProtKB:P00741"; 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 282; /note="Calcium 8"; /evidence="ECO:0000250|UniProtKB:P00740"; METAL 284; /note="Calcium 8; via carbonyl oxygen"; /evidence="ECO:0000250|UniProtKB:P00740"; METAL 287; /note="Calcium 8; via carbonyl oxygen"; /evidence="ECO:0000250|UniProtKB:P00740"; METAL 289; /note="Calcium 8"; /evidence="ECO:0000250|UniProtKB:P00740"; METAL 292; /note="Calcium 8"; /evidence="ECO:0000250|UniProtKB:P00740"
Rhea ID
Cross Reference Brenda