CP1A2_RABIT
ID CP1A2_RABIT Reviewed; 516 AA.
AC P00187; Q29526;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 156.
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 P450 isozyme 4;
DE Short=Cytochrome P450 LM4;
DE AltName: Full=Cytochrome P450-PM4;
DE AltName: Full=Hydroperoxy icosatetraenoate dehydratase;
DE EC=4.2.1.152 {ECO:0000250|UniProtKB:P05177};
GN Name=CYP1A2;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS SER-174; SER-233 AND GLY-299.
RC STRAIN=New Zealand white;
RX PubMed=2847925; DOI=10.1111/j.1432-1033.1988.tb14375.x;
RA Pompon D.;
RT "cDNA cloning and functional expression in yeast Saccharomyces cerevisiae
RT of beta-naphthoflavone-induced rabbit liver P-450 LM4 and LM6.";
RL Eur. J. Biochem. 177:285-293(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=3667560; DOI=10.1093/oxfordjournals.jbchem.a122017;
RA Kagawa N., Mihara K., Sato R.;
RT "Structural analysis of cloned cDNAs for polycyclic hydrocarbon-inducible
RT forms of rabbit liver microsomal cytochrome P-450.";
RL J. Biochem. 101:1471-1479(1987).
RN [3]
RP PROTEIN SEQUENCE OF 2-516.
RX PubMed=3949797; DOI=10.1016/s0021-9258(17)35609-0;
RA Ozols J.;
RT "Complete amino acid sequence of a cytochrome P-450 isolated from beta-
RT naphthoflavone-induced rabbit liver microsomes. Comparison with
RT phenobarbital-induced and constitutive isozymes and identification of
RT invariant residues.";
RL J. Biol. Chem. 261:3965-3979(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 92-515.
RX PubMed=2991917; DOI=10.1073/pnas.82.16.5310;
RA Okino S.T., Quattrochi L.C., Barnes H.J., Osanto S., Griffin K.J.,
RA Johnson E.F., Tukey R.H.;
RT "Cloning and characterization of cDNAs encoding 2,3,7,8-tetrachlorodibenzo-
RT p-dioxin-inducible rabbit mRNAs for cytochrome P-450 isozymes 4 and 6.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:5310-5314(1985).
RN [5]
RP PROTEIN SEQUENCE OF 176-185.
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 [6]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=6589592; DOI=10.1073/pnas.81.14.4260;
RA Fujita V.S., Black S.D., Tarr G.E., Koop D.R., Coon M.J.;
RT "On the amino acid sequence of cytochrome P-450 isozyme 4 from rabbit liver
RT microsomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:4260-4264(1984).
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 beta-naphthoflavone and 2,3,7,8-tetrachlorodibenzo-p-
CC dioxin (TCDD).
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; M36538; AAA31437.1; -; mRNA.
DR EMBL; X13853; CAA32066.1; -; mRNA.
DR EMBL; X05686; CAA29171.1; -; mRNA.
DR EMBL; M11728; AAA31433.1; -; mRNA.
DR PIR; B27821; O4RBBN.
DR RefSeq; NP_001164592.1; NM_001171121.1.
DR AlphaFoldDB; P00187; -.
DR SMR; P00187; -.
DR STRING; 9986.ENSOCUP00000008665; -.
DR PRIDE; P00187; -.
DR GeneID; 100328937; -.
DR KEGG; ocu:100328937; -.
DR eggNOG; KOG0156; Eukaryota.
DR InParanoid; P00187; -.
DR UniPathway; UPA00296; -.
DR UniPathway; UPA00383; -.
DR UniPathway; UPA00912; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
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:0019369; P:arachidonic acid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008210; P:estrogen metabolic process; ISS:UniProtKB.
DR GO; GO:0042572; P:retinol metabolic process; ISS:UniProtKB.
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:0000269|PubMed:3949797"
FT CHAIN 2..516
FT /note="Cytochrome P450 1A2"
FT /id="PRO_0000051655"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 361..365
FT /ligand="substrate"
FT BINDING 458
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 SITE 403
FT /note="Involved in electron transfer with reductase"
FT CARBOHYD 69
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT VARIANT 174
FT /note="G -> S"
FT /evidence="ECO:0000269|PubMed:2847925"
FT VARIANT 233
FT /note="G -> S"
FT /evidence="ECO:0000269|PubMed:2847925"
FT VARIANT 299
FT /note="S -> G"
FT /evidence="ECO:0000269|PubMed:2847925"
FT CONFLICT 22
FT /note="C -> S (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="R -> P (in Ref. 1; AAA31437)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="R -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="D -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="T -> H (in Ref. 4; AAA31433)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="Q -> H (in Ref. 2; CAA29171)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="L -> F (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="V -> S (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 208..212
FT /note="RFPQG -> FPQGM (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="R -> H (in Ref. 1; AAA31437/CAA32066 and 4;
FT AAA31433)"
FT /evidence="ECO:0000305"
FT CONFLICT 247..251
FT /note="NRPLQ -> QPNLR (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="F -> I (in Ref. 4; AAA31433)"
FT /evidence="ECO:0000305"
FT CONFLICT 291..302
FT /note="SEKNSKANSGLI -> NEMDSMDDGAHV (in Ref. 4; AAA31433)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="N -> T (in Ref. 4; AAA31433)"
FT /evidence="ECO:0000305"
FT CONFLICT 354..355
FT /note="AR -> PG (in Ref. 1; AAA31437/CAA32066)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="R -> L (in Ref. 4; AAA31433)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="L -> I (in Ref. 3; AA sequence and 4; AAA31433)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="T -> I (in Ref. 4; AAA31433)"
FT /evidence="ECO:0000305"
FT CONFLICT 494
FT /note="I -> T (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 516 AA; 58334 MW; 3FD074D74A47C3EF CRC64;
MAMSPAAPLS VTELLLVSAV FCLVFWAVRA SRPKVPKGLK RLPGPWGWPL LGHLLTLGKN
PHVALARLSR RYGDVFQIRL GSTPVVVLSG LDTIKQALVR QGDDFKGRPD LYSSSFITEG
QSMTFSPDSG PVWAARRRLA QDSLKSFSIA SNPASSSSCY LEEHVSQEAE NLIGRFQELM
AAVGRFDPYS QLVVSAARVI GAMCFGRRFP QGSEEMLDVV RNSSKFVETA SSGSPVDFFP
ILRYLPNRPL QRFKDFNQRF LRFLQKTVRE HYEDFDRNSI QDITGALFKH SEKNSKANSG
LIPQEKIVNL VNDIFGAGFD TITTALSWSL MYLVTNPRRQ RKIQEELDAV VGRARQPRLS
DRPQLPYLEA FILELFRHTS FVPFTIPHST TRDTTLNGFH IPKECCIFIN QWQINHDPQL
WGDPEEFRPE RFLTADGAAI NKPLSEKVTL FGLGKRRCIG ETLARWEVFL FLAILLQRLE
FSVPPGVPVD LTPIYGLTMK HPRCEHVQAR PRFSDQ
