{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P00740","secondaryAccessions":["A8K9N4","F2RM36","Q5FBE1","Q5JYJ8"],"uniProtkbId":"FA9_HUMAN","entryAudit":{"firstPublicDate":"1986-07-21","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2005-06-07","entryVersion":288,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"3857619"}],"value":"Coagulation factor IX"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12444082"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20121197"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20121198"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2592373"}],"value":"3.4.21.22"}]},"alternativeNames":[{"fullName":{"value":"Christmas factor"}},{"fullName":{"value":"Plasma thromboplastin component"},"shortNames":[{"value":"PTC"}]}],"contains":[{"recommendedName":{"fullName":{"value":"Coagulation factor IXa light chain"}}},{"recommendedName":{"fullName":{"value":"Coagulation factor IXa heavy chain"}}}],"flag":"Precursor"},"genes":[{"geneName":{"value":"F9"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1730085"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19846852"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20121197"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20121198"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2592373"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39880037"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8295821"}],"value":"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 (PubMed:8295821, PubMed:2592373, PubMed:20121197, PubMed:20121198, PubMed:1730085, PubMed:19846852, PubMed:39880037)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.","ecNumber":"3.4.21.22","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12444082"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20121197"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20121198"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2592373"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10692472"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20004170"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20080729"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20121197"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20121198"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22961984"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2592373"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34502392"}],"value":"Heterodimer of a light chain and a heavy chain; disulfide-linked (PubMed:20080729, PubMed:20121197, PubMed:20121198). Interacts (inactive and activated) with F11 (activated) in calcium-dependent manner (PubMed:22961984). Interacts with SERPINC1 (PubMed:20080729). Interacts (activated) with iripin-8, a serine protease inhibitor from Ixodes ricinus saliva (PubMed:34502392). Interacts (inactive and activated) with nitrophorin-2, an anticoagulant protein from Rhodnius prolixus (PubMed:10692472)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P00740","intActId":"EBI-9640450"},"interactantTwo":{"uniProtKBAccession":"P00451","geneName":"F8","chainId":"PRO_0000002968","intActId":"EBI-11621603"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P00740","intActId":"EBI-9640450"},"interactantTwo":{"uniProtKBAccession":"Q3U4G3","geneName":"Xxylt1","intActId":"EBI-16178491"},"numberOfExperiments":3,"organismDiffer":true}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19846852"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2592373"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3857619"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8295821"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9169594"}],"value":"Secreted","id":"SL-0243"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["P00740-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["P00740-2"],"sequenceIds":["VSP_047689"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19846852"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2592373"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3857619"}],"value":"Detected in blood plasma (at protein level) (PubMed:19846852, PubMed:2592373, PubMed:3857619, PubMed:8295821, PubMed:9169594). Synthesized primarily in the liver and secreted in plasma"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P00741"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14722079"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1730085"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6425296"}],"value":"Calcium binds to the gamma-carboxyglutamic acid (Gla) residues in the Gla domain. Calcium can also bind, with stronger affinity, to another site beyond the Gla domain (PubMed:6425296). Under physiological ion concentrations, Ca(2+) is displaced by Mg(2+) from some of the gammaglutamate residues in the N-terminal Gla domain. This leads to a subtle conformation change that may affect the interaction with its binding protein (By similarity)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1730085"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20004170"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20080729"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22961984"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2592373"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"271951"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8295821"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9169594"}],"value":"Activated by factor XIa, which excises the activation peptide (PubMed:1730085, PubMed:9169594, PubMed:22961984). The propeptide can also be removed by snake venom protease (PubMed:20004170, PubMed:20080729). Activated by coagulation factor VIIa-tissue factor (F7-F3) complex in calcium-dependent manner (PubMed:271951)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6688526"}],"value":"The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2129367"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2511201"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25456591"}],"value":"Predominantly O-glucosylated at Ser-99 by POGLUT1 in vitro"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39880037"}],"value":"Carboxylated by vitamin K-dependent GGCX to form gamma-carboxyglutamate; these residues are essential for the binding of calcium"}],"commentType":"PTM"},{"commentType":"DISEASE","disease":{"diseaseId":"Hemophilia B","diseaseAccession":"DI-02248","acronym":"HEMB","description":"An X-linked blood coagulation disorder characterized by a permanent tendency to hemorrhage, due to factor IX deficiency. 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Mutation in position 93 (Alabama) probably fails to bind to cell membranes (PubMed:3790720). Mutation in position 191 (Chapel-Hill) or in position 226 (Nagoya or Hilo) prevent cleavage of the activation peptide (PubMed:12588353, PubMed:2162822, PubMed:25251685, PubMed:2713493, PubMed:6603618, PubMed:8076946)"}]}},{"commentType":"DISEASE","disease":{"diseaseId":"Thrombophilia, X-linked, due to factor IX defect","diseaseAccession":"DI-02524","acronym":"THPH8","description":"A hemostatic disorder characterized by a tendency to thrombosis.","diseaseCrossReference":{"database":"MIM","id":"300807"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19846852"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"commentType":"DISEASE","disease":{"diseaseId":"Warfarin sensitivity, X-linked","diseaseAccession":"DI-05867","acronym":"WARFS","description":"A condition characterized by sensitivity to warfarin, a drugs used as anti-coagulants for the prevention of thromboembolic diseases in subjects with deep vein thrombosis, atrial fibrillation, or mechanical heart valve replacement. 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