IED Industry Enzyme Database

Detail Information for IndEnz0002006914
IED ID IndEnz0002006914
Enzyme Type ID protease006914
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 Bos taurus (Bovine)
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 Ruminantia Pecora Bovidae Bovinae Bos (oxen cattle) Bos taurus (Bovine)
Enzyme Sequence MWCLNMIMAESPGLVTICLLGYLLSAECTVFLDRENATKILHRPKRYNSGKLEEFVRGNLERECKEEKCSFEEAREVFENTEKTTEFWKQYVDGDQCESNPCLNGGMCKDDINSYECWCQAGFEGTNCELDATCSIKNGRCKQFCKRDTDNKVVCSCTDGYRLAEDQKSCEPAVPFPCGRVSVSHISKKLTRAETIFSNTNYENSSEAEIIWDNVTQSNQSFDEFSRVVGGEDAERGQFPWQVLLHGEIAAFCGGSIVNEKWVVTAAHCIKPGVKITVVAGEHNTEKPEPTEQKRNVIRAIPYHSYNASINKYSHDIALLELDEPLELNSYVTPICIADRDYTNIFLKFGYGYVSGWGKVFNRGRSASILQYLKVPLVDRATCLRSTKFSIYSHMFCAGYHEGGKDSCQGDSGGPHVTEVEGTSFLTGIISWGEECAMKGKYGIYTKVSRYVNWIKEKTKLT
Enzyme Length 462
Uniprot Accession Number P00741
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:0000269|PubMed:6782101};
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:0000269|PubMed:6782101}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Beta strand (1); Chain (3); Disulfide bond (11); Domain (4); Glycosylation (6); Helix (4); Metal binding (34); Modified residue (16); Propeptide (2); Sequence conflict (2); Signal peptide (1); Site (2)
Keywords 3D-structure;Blood coagulation;Calcium;Direct protein sequencing;Disulfide bond;EGF-like domain;Gamma-carboxyglutamic acid;Glycoprotein;Hemophilia;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:0000269|PubMed:12695512}.
Modified Residue MOD_RES 53; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:12695512, ECO:0000269|PubMed:291916, ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"; MOD_RES 54; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:12695512, ECO:0000269|PubMed:291916, ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"; MOD_RES 61; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:12695512, ECO:0000269|PubMed:291916, ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"; MOD_RES 63; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:12695512, ECO:0000269|PubMed:291916, ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"; MOD_RES 66; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:12695512, ECO:0000269|PubMed:291916, ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"; MOD_RES 67; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:12695512, ECO:0000269|PubMed:291916, ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"; MOD_RES 72; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:12695512, ECO:0000269|PubMed:291916, ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"; MOD_RES 73; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:12695512, ECO:0000269|PubMed:291916, ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"; MOD_RES 76; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:12695512, ECO:0000269|PubMed:291916, ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"; MOD_RES 79; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:12695512, ECO:0000269|PubMed:291916, ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"; MOD_RES 82; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:12695512, ECO:0000269|PubMed:291916, ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"; MOD_RES 86; /note="4-carboxyglutamate"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:12695512, ECO:0000269|PubMed:291916, ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"; MOD_RES 110; /note="(3R)-3-hydroxyaspartate"; /evidence="ECO:0000269|PubMed:6688526"; 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"
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:0000269|PubMed:6688526}.; 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 X-ray crystallography (2)
Cross Reference PDB 1J34; 1J35;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 52,046
Kinetics
Metal Binding METAL 47; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:12695512, ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"; METAL 48; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:12695512, ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"; METAL 53; /note="Calcium 1; via 4-carboxyglutamate"; /evidence="ECO:0000269|PubMed:12695512, ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"; METAL 53; /note="Calcium 2; via 4-carboxyglutamate"; /evidence="ECO:0000269|PubMed:12695512, ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"; METAL 54; /note="Calcium 2; via 4-carboxyglutamate"; /evidence="ECO:0000269|PubMed:12695512, ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"; METAL 54; /note="Calcium 3; via 4-carboxyglutamate"; /evidence="ECO:0000269|PubMed:12695512, ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"; METAL 61; /note="Calcium 4; via 4-carboxyglutamate"; /evidence="ECO:0000269|PubMed:12695512, ECO:0007744|PDB:1J35"; METAL 61; /note="Magnesium 1; via 4-carboxyglutamate"; /evidence="ECO:0000269|PubMed:12695512, ECO:0007744|PDB:1J34"; METAL 63; /note="Calcium 1; via 4-carboxyglutamate"; /evidence="ECO:0000269|PubMed:12695512, ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"; METAL 63; /note="Calcium 2; via 4-carboxyglutamate"; /evidence="ECO:0000269|PubMed:12695512, ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"; METAL 63; /note="Calcium 3; via 4-carboxyglutamate"; /evidence="ECO:0000269|PubMed:12695512, ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"; METAL 66; /note="Calcium 4; via 4-carboxyglutamate"; /evidence="ECO:0000269|PubMed:12695512, ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"; METAL 66; /note="Magnesium 1; via 4-carboxyglutamate"; /evidence="ECO:0000269|PubMed:12695512, ECO:0007744|PDB:1J34"; METAL 67; /note="Calcium 1; via 4-carboxyglutamate"; /evidence="ECO:0000269|PubMed:12695512, ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"; METAL 72; /note="Calcium 5; via 4-carboxyglutamate"; /evidence="ECO:0000269|PubMed:12695512, ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"; METAL 72; /note="Magnesium 2; via 4-carboxyglutamate"; /evidence="ECO:0000269|PubMed:12695512, ECO:0007744|PDB:1J34"; METAL 73; /note="Calcium 2; via 4-carboxyglutamate"; /evidence="ECO:0000269|PubMed:12695512, ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"; METAL 73; /note="Calcium 3; via 4-carboxyglutamate"; /evidence="ECO:0000269|PubMed:12695512, ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"; 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:0000269|PubMed:12695512, ECO:0007744|PDB:1J34"; METAL 82; /note="Calcium 6 ; via 4-carboxyglutamate"; /evidence="ECO:0000269|PubMed:12695512, ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"; METAL 82; /note="Magnesium 3; via 4-carboxyglutamate"; /evidence="ECO:0000269|PubMed:12695512, ECO:0007744|PDB:1J34"; METAL 86; /note="Calcium 6; via 4-carboxyglutamate"; /evidence="ECO:0000269|PubMed:12695512, ECO:0007744|PDB:1J34, ECO:0007744|PDB:1J35"; METAL 86; /note="Magnesium 3; via 4-carboxyglutamate"; /evidence="ECO:0000269|PubMed:12695512, ECO:0007744|PDB:1J34"; 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 282; /note="Calcium 8"; /evidence="ECO:0000250|UniProtKB:P00740"; METAL 284; /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