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   27-MAR-2024, entry version 161.
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
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47212, Rhea:RHEA-
CC         COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16469,
CC         ChEBI:CHEBI:28744, 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
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47280, Rhea:RHEA-
CC         COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16469,
CC         ChEBI:CHEBI:57618, 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
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:42092, Rhea:RHEA-
CC         COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17336,
CC         ChEBI:CHEBI:17898, 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
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:42088, Rhea:RHEA-
CC         COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17898,
CC         ChEBI:CHEBI:35291, 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
CC         [NADPH--hemoprotein reductase] = (14R,15S)-epoxy-(5Z,8Z,11Z)-
CC         eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:49860, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, 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
CC         [NADPH--hemoprotein reductase] = (14S,15R)-epoxy-(5Z,8Z,11Z)-
CC         eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:49856, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, 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
CC         [NADPH--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
CC         [NADPH--hemoprotein reductase] = 13-hydroxy-(5Z,8Z,11Z,14Z)-
CC         eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:52292, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, 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
CC         [NADPH--hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z)-
CC         eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:39759, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, 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   GlyCosmos; P00187; 1 site, No reported glycans.
DR   PaxDb; 9986-ENSOCUP00000008665; -.
DR   GeneID; 100328937; -.
DR   KEGG; ocu:100328937; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   InParanoid; P00187; -.
DR   OrthoDB; 2900138at2759; -.
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   CDD; cd20676; CYP1A; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 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   PANTHER; PTHR24289:SF18; CYTOCHROME P450 1A2; 1.
DR   PANTHER; PTHR24289; STEROID 17-ALPHA-HYDROXYLASE/17,20 LYASE; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR01683; EP450ICYP1A.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 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
//