CP1A2_RAT
ID CP1A2_RAT Reviewed; 513 AA.
AC P04799; A1L120; Q64588;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Cytochrome P450 1A2;
DE EC=1.14.14.1 {ECO:0000250|UniProtKB:P05177};
DE AltName: Full=CYPIA2;
DE AltName: Full=Cholesterol 25-hydroxylase {ECO:0000250|UniProtKB:P05177};
DE AltName: Full=Cytochrome P-448;
DE AltName: Full=Cytochrome P-450d;
DE AltName: Full=Cytochrome P450-D;
DE AltName: Full=Hydroperoxy icosatetraenoate dehydratase;
DE EC=4.2.1.152 {ECO:0000250|UniProtKB:P05177};
GN Name=Cyp1a2; Synonyms=Cyp1a-2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6584898; DOI=10.1073/pnas.81.6.1649;
RA Kawajiri K., Gotoh O., Sogawa K., Tagashira Y., Muramatsu M.,
RA Fujii-Kuriyama Y.;
RT "Coding nucleotide sequence of 3-methylcholanthrene-inducible cytochrome P-
RT 450d cDNA from rat liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:1649-1653(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2985574; DOI=10.1016/s0021-9258(18)89174-8;
RA Sogawa K., Gotoh O., Kawajiri K., Harada T., Fujii-Kuriyama Y.;
RT "Complete nucleotide sequence of a methylcholanthrene-inducible cytochrome
RT P-450 (P-450d) gene in the rat.";
RL J. Biol. Chem. 260:5026-5032(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1793487; DOI=10.1002/mc.2940040613;
RA Wolfel C., Platt K.L., Dogra S., Glatt H., Wachter F., Doehmer J.;
RT "Stable expression of rat cytochrome P450IA2 cDNA and hydroxylation of 17
RT beta-estradiol and 2-aminofluorene in V79 Chinese hamster cells.";
RL Mol. Carcinog. 4:489-498(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=3947063; DOI=10.1016/0003-9861(86)90121-9;
RA Haniu M., Ryan D.E., Levin W., Shively J.E.;
RT "The primary structure of cytochrome P-450d purified from rat liver
RT microsomes: prediction of helical regions and domain analysis.";
RL Arch. Biochem. Biophys. 244:323-337(1986).
RN [6]
RP PROTEIN SEQUENCE OF 2-26.
RX PubMed=3718958; DOI=10.1021/bi00357a015;
RA Cheng K.C., Park S.S., Krutzsch H.C., Grantham P.H., Gelboin H.V.,
RA Friedman F.K.;
RT "Amino-terminal sequence and structure of monoclonal antibody
RT immunopurified cytochromes P-450.";
RL Biochemistry 25:2397-2402(1986).
RN [7]
RP PROTEIN SEQUENCE OF 2-20.
RX PubMed=7074072; DOI=10.1021/bi00535a007;
RA Botelho L.H., Ryan D.E., Yuan P.M., Kutny R., Shively J.E., Levin W.;
RT "Amino-terminal and carboxy-terminal sequence of hepatic microsomal
RT cytochrome P-450d, a unique hemoprotein from rats treated with
RT isosafrole.";
RL Biochemistry 21:1152-1155(1982).
RN [8]
RP PROTEIN SEQUENCE OF 67-78.
RX PubMed=1420171; DOI=10.1021/bi00158a019;
RA Yun C.H., Hammons G.J., Jones G., Martin M.V., Hopkins N.E., Alworth W.L.,
RA Guengerich F.P.;
RT "Modification of cytochrome P450 1A2 enzymes by the mechanism-based
RT inactivator 2-ethynylnaphthalene and the photoaffinity label 4-
RT azidobiphenyl.";
RL Biochemistry 31:10556-10563(1992).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 147-513.
RX PubMed=6548743; DOI=10.1093/oxfordjournals.jbchem.a134897;
RA Yabusaki Y., Murakami H., Nakamura K., Nomura N., Shimizu M., Oeda K.,
RA Ohkawa H.;
RT "Characterization of complementary DNA clones coding for two forms of 3-
RT methylcholanthrene-inducible rat liver cytochrome P-450.";
RL J. Biochem. 96:793-804(1984).
RN [10]
RP GLYCOSYLATION AT SER-68.
RX PubMed=24098488; DOI=10.1371/journal.pone.0076399;
RA Cao W., Cao J., Huang J., Yao J., Yan G., Xu H., Yang P.;
RT "Discovery and confirmation of O-GlcNAcylated proteins in rat liver
RT mitochondria by combination of mass spectrometry and immunological
RT methods.";
RL PLoS ONE 8:E76399-E76399(2013).
CC -!- FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of
CC various endogenous substrates, including fatty acids, steroid hormones
CC and vitamins. Mechanistically, uses molecular oxygen inserting one
CC oxygen atom into a substrate, and reducing the second into a water
CC molecule, with two electrons provided by NADPH via cytochrome P450
CC reductase (NADPH--hemoprotein reductase). Catalyzes the hydroxylation
CC of carbon-hydrogen bonds. Exhibits high catalytic activity for the
CC formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol
CC (E2), namely 2-hydroxy E1 and E2. Metabolizes cholesterol toward 25-
CC hydroxycholesterol, a physiological regulator of cellular cholesterol
CC homeostasis. May act as a major enzyme for all-trans retinoic acid
CC biosynthesis in the liver. Catalyzes two successive oxidative
CC transformation of all-trans retinol to all-trans retinal and then to
CC the active form all-trans retinoic acid. Primarily catalyzes
CC stereoselective epoxidation of the last double bond of polyunsaturated
CC fatty acids (PUFA), displaying a strong preference for the (R,S)
CC stereoisomer. Catalyzes bisallylic hydroxylation and omega-1
CC hydroxylation of PUFA. May also participate in eicosanoids metabolism
CC by converting hydroperoxide species into oxo metabolites (lipoxygenase-
CC like reaction, NADPH-independent). Plays a role in the oxidative
CC metabolism of xenobiotics. Catalyzes the N-hydroxylation of
CC heterocyclic amines and the O-deethylation of phenacetin. Metabolizes
CC caffeine via N3-demethylation. {ECO:0000250|UniProtKB:P05177}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein
CC reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:142491; EC=1.14.14.1;
CC Evidence={ECO:0000250|UniProtKB:P05177};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17150;
CC Evidence={ECO:0000250|UniProtKB:P05177};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase]
CC = 2-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:47212, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16469, ChEBI:CHEBI:28744,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:P05177};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47213;
CC Evidence={ECO:0000250|UniProtKB:P05177};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase]
CC = 4-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:47280, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16469, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:62845;
CC Evidence={ECO:0000250|UniProtKB:P05177};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47281;
CC Evidence={ECO:0000250|UniProtKB:P05177};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=estrone + O2 + reduced [NADPH--hemoprotein reductase] = 2-
CC hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:47208, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:1156, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17263, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:P05177};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47209;
CC Evidence={ECO:0000250|UniProtKB:P05177};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=estrone + O2 + reduced [NADPH--hemoprotein reductase] = 4-
CC hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:47292, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17263, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:87602; Evidence={ECO:0000250|UniProtKB:P05177};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47293;
CC Evidence={ECO:0000250|UniProtKB:P05177};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesterol + O2 + reduced [NADPH--hemoprotein reductase] =
CC 25-hydroxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:50256, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16113, ChEBI:CHEBI:42977, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:P05177};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50257;
CC Evidence={ECO:0000250|UniProtKB:P05177};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinol + O2 + reduced [NADPH--hemoprotein
CC reductase] = all-trans-retinal + H(+) + 2 H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:42092, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17336, ChEBI:CHEBI:17898,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:P05177};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42093;
CC Evidence={ECO:0000250|UniProtKB:P05177};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinal + O2 + reduced [NADPH--hemoprotein
CC reductase] = all-trans-retinoate + 2 H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:42088, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17898, ChEBI:CHEBI:35291,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:P05177};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42089;
CC Evidence={ECO:0000250|UniProtKB:P05177};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = (14R,15S)-epoxy-(5Z,8Z,11Z)-eicosatrienoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:49860, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:131965; Evidence={ECO:0000250|UniProtKB:P05177};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49861;
CC Evidence={ECO:0000250|UniProtKB:P05177};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = (14S,15R)-epoxy-(5Z,8Z,11Z)-eicosatrienoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:49856, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:131964; Evidence={ECO:0000250|UniProtKB:P05177};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49857;
CC Evidence={ECO:0000250|UniProtKB:P05177};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = (17R,18S)-epoxy-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:39779, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:58562,
CC ChEBI:CHEBI:76634; Evidence={ECO:0000250|UniProtKB:P05177};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39780;
CC Evidence={ECO:0000250|UniProtKB:P05177};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced
CC [NADPH--hemoprotein reductase] = (19R,20S)-epoxy-(4Z,7Z,10Z,13Z,16Z)-
CC docosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:52120, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:77016,
CC ChEBI:CHEBI:136410; Evidence={ECO:0000250|UniProtKB:P05177};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52121;
CC Evidence={ECO:0000250|UniProtKB:P05177};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate = 5-oxo-
CC (6E,8Z,11Z,14Z)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:48632,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57450, ChEBI:CHEBI:65342;
CC Evidence={ECO:0000250|UniProtKB:P05177};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48633;
CC Evidence={ECO:0000250|UniProtKB:P05177};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = 12-oxo-
CC (5Z,8Z,10E,14Z)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:37947,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57444, ChEBI:CHEBI:75231;
CC EC=4.2.1.152; Evidence={ECO:0000250|UniProtKB:P05177};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37948;
CC Evidence={ECO:0000250|UniProtKB:P05177};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate = 15-oxo-
CC (5Z,8Z,11Z,13E)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:48636,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57410, ChEBI:CHEBI:57446;
CC Evidence={ECO:0000250|UniProtKB:P05177};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48637;
CC Evidence={ECO:0000250|UniProtKB:P05177};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(13S)-hydroperoxy-(9Z,11E)-octadecadienoate = 13-oxo-(9Z,11E)-
CC octadecadienoate + H2O; Xref=Rhea:RHEA:48716, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57466, ChEBI:CHEBI:90781;
CC Evidence={ECO:0000250|UniProtKB:P05177};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48717;
CC Evidence={ECO:0000250|UniProtKB:P05177};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 13-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:52292, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:136524; Evidence={ECO:0000250|UniProtKB:P05177};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52293;
CC Evidence={ECO:0000250|UniProtKB:P05177};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:39759, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:76627; Evidence={ECO:0000250|UniProtKB:P05177};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39760;
CC Evidence={ECO:0000250|UniProtKB:P05177};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = 11-hydroxy-(9Z,12Z)-octadecadienoate + H(+) + H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:52284,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:136522;
CC Evidence={ECO:0000250|UniProtKB:P05177};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52285;
CC Evidence={ECO:0000250|UniProtKB:P05177};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC {ECO:0000250|UniProtKB:P05177}.
CC -!- PATHWAY: Steroid metabolism; cholesterol metabolism.
CC {ECO:0000250|UniProtKB:P05177}.
CC -!- PATHWAY: Lipid metabolism; arachidonate metabolism.
CC {ECO:0000250|UniProtKB:P05177}.
CC -!- SUBUNIT: Interacts with PGRMC1; the interaction requires PGRMC1
CC homodimerization. {ECO:0000250|UniProtKB:P05177}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P05177}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P05177}. Microsome membrane
CC {ECO:0000250|UniProtKB:P05177}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P05177}.
CC -!- INDUCTION: By 3-methylcholanthrene (3MC).
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; K02422; AAA41028.1; -; mRNA.
DR EMBL; K03241; AAA41053.1; -; Genomic_DNA.
DR EMBL; BC127476; AAI27477.1; -; mRNA.
DR EMBL; X01031; CAA25516.1; -; mRNA.
DR PIR; A61400; A61400.
DR RefSeq; NP_036673.3; NM_012541.3.
DR AlphaFoldDB; P04799; -.
DR SMR; P04799; -.
DR BioGRID; 246478; 1.
DR IntAct; P04799; 1.
DR STRING; 10116.ENSRNOP00000021653; -.
DR BindingDB; P04799; -.
DR ChEMBL; CHEMBL1075125; -.
DR GlyGen; P04799; 1 site.
DR iPTMnet; P04799; -.
DR PhosphoSitePlus; P04799; -.
DR PaxDb; P04799; -.
DR PRIDE; P04799; -.
DR Ensembl; ENSRNOT00000021653; ENSRNOP00000021653; ENSRNOG00000016173.
DR GeneID; 24297; -.
DR KEGG; rno:24297; -.
DR UCSC; RGD:2459; rat.
DR CTD; 1544; -.
DR RGD; 2459; Cyp1a2.
DR eggNOG; KOG0156; Eukaryota.
DR GeneTree; ENSGT00950000183037; -.
DR HOGENOM; CLU_001570_22_0_1; -.
DR InParanoid; P04799; -.
DR OMA; AKWEIFL; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; P04799; -.
DR BRENDA; 1.14.14.1; 5301.
DR Reactome; R-RNO-156581; Methylation.
DR Reactome; R-RNO-211957; Aromatic amines can be N-hydroxylated or N-dealkylated by CYP1A2.
DR Reactome; R-RNO-2142670; Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET).
DR Reactome; R-RNO-2142816; Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE).
DR Reactome; R-RNO-5423646; Aflatoxin activation and detoxification.
DR Reactome; R-RNO-9018681; Biosynthesis of protectins.
DR Reactome; R-RNO-9027307; Biosynthesis of maresin-like SPMs.
DR SABIO-RK; P04799; -.
DR UniPathway; UPA00296; -.
DR UniPathway; UPA00383; -.
DR UniPathway; UPA00912; -.
DR PRO; PR:P04799; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000016173; Expressed in liver and 11 other tissues.
DR Genevisible; P04799; RN.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR GO; GO:0034875; F:caffeine oxidase activity; ISO:RGD.
DR GO; GO:0032451; F:demethylase activity; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0101020; F:estrogen 16-alpha-hydroxylase activity; ISS:UniProtKB.
DR GO; GO:0101021; F:estrogen 2-hydroxylase activity; ISS:UniProtKB.
DR GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR GO; GO:0106256; F:hydroperoxy icosatetraenoate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IDA:RGD.
DR GO; GO:0016491; F:oxidoreductase activity; ISO:RGD.
DR GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IDA:RGD.
DR GO; GO:0009820; P:alkaloid metabolic process; ISO:RGD.
DR GO; GO:0019369; P:arachidonic acid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006725; P:cellular aromatic compound metabolic process; ISO:RGD.
DR GO; GO:0045333; P:cellular respiration; ISO:RGD.
DR GO; GO:0071276; P:cellular response to cadmium ion; ISO:RGD.
DR GO; GO:0071280; P:cellular response to copper ion; IEP:RGD.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0018894; P:dibenzo-p-dioxin metabolic process; ISO:RGD.
DR GO; GO:0008210; P:estrogen metabolic process; ISS:UniProtKB.
DR GO; GO:0046483; P:heterocycle metabolic process; ISO:RGD.
DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; ISO:RGD.
DR GO; GO:0030324; P:lung development; ISO:RGD.
DR GO; GO:0032787; P:monocarboxylic acid metabolic process; ISO:RGD.
DR GO; GO:0016098; P:monoterpenoid metabolic process; ISO:RGD.
DR GO; GO:0070989; P:oxidative demethylation; ISO:RGD.
DR GO; GO:0006778; P:porphyrin-containing compound metabolic process; ISO:RGD.
DR GO; GO:0009791; P:post-embryonic development; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0035902; P:response to immobilization stress; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0042572; P:retinol metabolic process; ISS:UniProtKB.
DR GO; GO:0006706; P:steroid catabolic process; ISO:RGD.
DR GO; GO:0009403; P:toxin biosynthetic process; ISO:RGD.
DR GO; GO:0009404; P:toxin metabolic process; ISO:RGD.
DR GO; GO:0042178; P:xenobiotic catabolic process; ISO:RGD.
DR GO; GO:0006805; P:xenobiotic metabolic process; IDA:RGD.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR008066; Cyt_P450_E_grp-I_CYP1.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR01683; EP450ICYP1A.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Endoplasmic reticulum; Fatty acid metabolism;
KW Glycoprotein; Heme; Iron; Lipid metabolism; Lyase; Membrane; Metal-binding;
KW Microsome; Monooxygenase; Oxidoreductase; Reference proteome;
KW Steroid metabolism; Sterol metabolism.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P56592"
FT CHAIN 2..513
FT /note="Cytochrome P450 1A2"
FT /id="PRO_0000051656"
FT BINDING 456
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT CARBOHYD 68
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000269|PubMed:24098488"
FT CONFLICT 26
FT /note="V -> M (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="R -> H (in Ref. 2; AAA41053 and 3; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="F -> L (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="F -> S (in Ref. 1; AAA41028)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="C -> R (in Ref. 2; AAA41053)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 513 AA; 58259 MW; B1F06FDE9B7B6FA7 CRC64;
MAFSQYISLA PELLLATAIF CLVFWVLRGT RTQVPKGLKS PPGPWGLPFI GHMLTLGKNP
HLSLTKLSQQ YGDVLQIRIG STPVVVLSGL NTIKQALVKQ GDDFKGRPDL YSFTLITNGK
SMTFNPDSGP VWAARRRLAQ DALKSFSIAS DPTSVSSCYL EEHVSKEANH LISKFQKLMA
EVGHFEPVNQ VVESVANVIG AMCFGKNFPR KSEEMLNLVK SSKDFVENVT SGNAVDFFPV
LRYLPNPALK RFKNFNDNFV LFLQKTVQEH YQDFNKNSIQ DITGALFKHS ENYKDNGGLI
PQEKIVNIVN DIFGAGFETV TTAIFWSILL LVTEPKVQRK IHEELDTVIG RDRQPRLSDR
PQLPYLEAFI LEIYRYTSFV PFTIPHSTTR DTSLNGFHIP KECCIFINQW QVNHDEKQWK
DPFVFRPERF LTNDNTAIDK TLSEKVMLFG LGKRRCIGEI PAKWEVFLFL AILLHQLEFT
VPPGVKVDLT PSYGLTMKPR TCEHVQAWPR FSK
