{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P04798","secondaryAccessions":["A4F3V9","A4F3W0","Q53G18"],"uniProtkbId":"CP1A1_HUMAN","entryAudit":{"firstPublicDate":"1987-08-13","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1988-04-01","entryVersion":248,"sequenceVersion":1},"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":"11555828"}],"value":"Cytochrome P450 1A1"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10681376"}],"value":"CYPIA1"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12865317"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15041462"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15805301"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18577768"}],"value":"1.14.14.1"}]},"alternativeNames":[{"fullName":{"value":"Cytochrome P450 form 6"}},{"fullName":{"value":"Cytochrome P450-C"}},{"fullName":{"value":"Cytochrome P450-P1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21068195"}],"value":"Hydroperoxy icosatetraenoate dehydratase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21068195"}],"value":"4.2.1.152"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10681376"},{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:2595"}],"value":"CYP1A1"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10681376"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11555828"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12865317"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14559847"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15041462"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15805301"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18577768"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19965576"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20972997"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21068195"}],"value":"A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins (PubMed:10681376, PubMed:11555828, PubMed:12865317, PubMed:14559847, PubMed:15041462, PubMed:15805301, PubMed:18577768, PubMed:19965576, PubMed:20972997). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase) (PubMed:10681376, PubMed:11555828, PubMed:12865317, PubMed:14559847, PubMed:15041462, PubMed:15805301, PubMed:18577768, PubMed:19965576, PubMed:20972997). Catalyzes the hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2, as well as D-ring hydroxylated E1 and E2 at the C15-alpha and C16-alpha positions (PubMed:11555828, PubMed:12865317, PubMed:14559847, PubMed:15805301). Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation (PubMed:15041462, PubMed:18577768). Catalyzes the epoxidation of double bonds of certain PUFA (PubMed:15041462, PubMed:19965576, PubMed:20972997). Converts arachidonic acid toward epoxyeicosatrienoic acid (EET) regioisomers, 8,9-, 11,12-, and 14,15-EET, that function as lipid mediators in the vascular system (PubMed:20972997). Displays an absolute stereoselectivity in the epoxidation of eicosapentaenoic acid (EPA) producing the 17(R),18(S) enantiomer (PubMed:15041462). May play an important role in all-trans retinoic acid biosynthesis in extrahepatic tissues. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid (PubMed:10681376). May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase-like reaction, NADPH-independent) (PubMed:21068195)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"an organic molecule + reduced [NADPH--hemoprotein reductase] + O2 = an alcohol + oxidized [NADPH--hemoprotein reductase] + H2O + 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