{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P05177","secondaryAccessions":["Q16754","Q6NWU3","Q6NWU5","Q9BXX7","Q9UK49"],"uniProtkbId":"CP1A2_HUMAN","entryAudit":{"firstPublicDate":"1987-08-13","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2018-09-12","entryVersion":238,"sequenceVersion":4},"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":"14725854"}],"value":"Cytochrome P450 1A2"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11555828"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12865317"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9435160"}],"value":"1.14.14.1"}]},"alternativeNames":[{"fullName":{"value":"CYPIA2"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21576599"}],"value":"Cholesterol 25-hydroxylase"}},{"fullName":{"value":"Cytochrome P(3)450"}},{"fullName":{"value":"Cytochrome P450 4"}},{"fullName":{"value":"Cytochrome P450-P3"}},{"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":"2575218"},{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:2596"}],"value":"CYP1A2"}}],"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":"14725854"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19965576"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21068195"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21576599"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9435160"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"16522833"}],"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:19965576, PubMed:9435160). 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:19965576, PubMed:9435160). Catalyzes the hydroxylation of carbon-hydrogen bonds (PubMed:11555828, PubMed:12865317). Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2 (PubMed:11555828, PubMed:12865317). Metabolizes cholesterol toward 25-hydroxycholesterol, a physiological regulator of cellular cholesterol homeostasis (PubMed:21576599). May act as a major enzyme for all-trans retinoic acid biosynthesis in the liver. 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). Primarily catalyzes stereoselective epoxidation of the last double bond of polyunsaturated fatty acids (PUFA), displaying a strong preference for the (R,S) stereoisomer (PubMed:19965576). Catalyzes bisallylic hydroxylation and omega-1 hydroxylation of PUFA (PubMed:9435160). May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase-like reaction, NADPH-independent) (PubMed:21068195). Plays a role in the oxidative metabolism of xenobiotics. Catalyzes the N-hydroxylation of heterocyclic amines and the O-deethylation of phenacetin (PubMed:14725854). Metabolizes caffeine via N3-demethylation (Probable)"}],"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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