ID   CP1A2_MESAU             Reviewed;         513 AA.
AC   P24453;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   27-MAR-2024, entry version 130.
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-MC4;
DE   AltName: Full=Hepatic cytochrome P-450MC1;
DE   AltName: Full=Hydroperoxy icosatetraenoate dehydratase;
DE            EC=4.2.1.152 {ECO:0000250|UniProtKB:P05177};
GN   Name=CYP1A2;
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=2275554; DOI=10.1016/0003-9861(90)90664-k;
RA   Lai T.S., Chiang J.Y.L.;
RT   "Cloning and characterization of two major 3-methylcholanthrene inducible
RT   hamster liver cytochrome P450s.";
RL   Arch. Biochem. Biophys. 283:429-439(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1778988; DOI=10.1093/oxfordjournals.jbchem.a123633;
RA   Sagami I., Ohmachi T., Fujii H., Kikuchi H., Watanabe M.;
RT   "Hamster cytochrome P-450 IA gene family, P-450IA1 and P-450IA2 in lung and
RT   liver: cDNA cloning and sequence analysis.";
RL   J. Biochem. 110:641-647(1991).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-19.
RC   TISSUE=Liver;
RX   PubMed=2391346; DOI=10.1093/oxfordjournals.jbchem.a123133;
RA   Koga N., Ariyoshi N., Nakashima H., Yoshimura H.;
RT   "Purification and characterization of two forms of 2,3,4,7,8-
RT   pentachlorodibenzofuran-inducible cytochrome P-450 in hamster liver.";
RL   J. Biochem. 107:826-833(1990).
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   -!- TISSUE SPECIFICITY: Found in lung and liver.
CC   -!- INDUCTION: By 3-methylcholanthrene (3MC).
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; M63787; AAA37070.1; -; mRNA.
DR   EMBL; D10252; BAA01097.1; -; mRNA.
DR   EMBL; D10914; BAA01718.1; -; Genomic_DNA.
DR   PIR; JX0190; JX0190.
DR   RefSeq; NP_001268302.1; NM_001281373.1.
DR   AlphaFoldDB; P24453; -.
DR   SMR; P24453; -.
DR   STRING; 10036.ENSMAUP00000007198; -.
DR   GlyCosmos; P24453; 1 site, No reported glycans.
DR   GeneID; 101825565; -.
DR   KEGG; maua:101825565; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   OrthoDB; 2900138at2759; -.
DR   UniPathway; UPA00296; -.
DR   UniPathway; UPA00383; -.
DR   UniPathway; UPA00912; -.
DR   Proteomes; UP000189706; 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:2391346"
FT   CHAIN           2..513
FT                   /note="Cytochrome P450 1A2"
FT                   /id="PRO_0000051653"
FT   BINDING         225
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
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                   /evidence="ECO:0000250"
FT   CARBOHYD        68
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        49
FT                   /note="I -> F (in Ref. 1; AAA37070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        52..53
FT                   /note="HV -> MC (in Ref. 1; AAA37070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        253..254
FT                   /note="KN -> GG (in Ref. 1; AAA37070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        326
FT                   /note="L -> W (in Ref. 1; AAA37070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        356
FT                   /note="R -> L (in Ref. 1; AAA37070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        485
FT                   /note="T -> Q (in Ref. 1; AAA37070)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   513 AA;  58082 MW;  D179B43386C19815 CRC64;
     MALSQYTSLS TELVLATAIF CIVFWVARAL RTQVPKGLKT PPGPWGLPIL GHVLTLGKNP
     HLSLTKLSKQ YGDVLQIRIG STPVVVLSGL DTIRQALVRQ GDDFKGRPDL YSFTLITNGK
     SMTFNPDCGP VWAARRRLAQ DALKSFSIAS DPTSASSCYL EDHVIKEANH LVSKLQKLTA
     EVGHFEPVNQ VVESVANVIG AMCFGKNFPR KSEEMLRIVK GSSDFVENVS SGNAVDFFPI
     LRYLPNPDLK RFKNFNDNFV LFLQKTVQEH YQDFNKNSIQ DITGALFKHS ENSKDSGGLI
     PQEKIVNIVN DLFGAGFDTV TTAITLSILL LVTWPNVQRK IHKELDTVIG RDRQPRLSDR
     LQLPYMEAFI LELYRYTSFV PFTIPHSTTR DTSLNGFYIP KDRCIFINQW QVNHDEKQWK
     DPFVFRPERF LTDNDTVINK TLSEKVMLFG LGKRRCIGEI PAKWEVFLFL AILLQQLEFS
     VPPGTKVDLT PTYGLTMKPQ TCKYIQAWPR FSK
//