ID   CP1A1_MACFA             Reviewed;         512 AA.
AC   P33616; Q29489;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   27-MAR-2024, entry version 117.
DE   RecName: Full=Cytochrome P450 1A1;
DE            EC=1.14.14.1 {ECO:0000250|UniProtKB:P04798};
DE   AltName: Full=CYPIA1;
DE   AltName: Full=Cytochrome P450 form 6;
DE   AltName: Full=Cytochrome P450-C;
DE   AltName: Full=Cytochrome P450-P1;
DE   AltName: Full=Hydroperoxy icosatetraenoate dehydratase;
DE            EC=4.2.1.152 {ECO:0000250|UniProtKB:P04798};
GN   Name=CYP1A1;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1581357; DOI=10.1016/0167-4781(92)90093-f;
RA   Komori M., Kikuchi O., Kitada M., Kamataki T.;
RT   "Molecular cloning of monkey P450 1A1 cDNA and expression in yeast.";
RL   Biochim. Biophys. Acta 1131:23-29(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Ohmachi T., Sagami I., Kikuchi H., Fujii H., Suzaki Y., Fujiwara T.,
RA   Watanabe M.;
RT   "Molecular cloning and sequence analysis of cDNA encoding a crab-eating
RT   monkey (Macaca irus) cytochrome P-450.";
RL   Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
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 (CPR; NADPH-ferrihemoprotein reductase). Catalyzes the
CC       hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic
CC       activity for the formation of hydroxyestrogens from estrone (E1) and
CC       17beta-estradiol (E2), namely 2-hydroxy E1 and E2, as well as D-ring
CC       hydroxylated E1 and E2 at the C15alpha and C16alpha positions. Displays
CC       different regioselectivities for polyunsaturated fatty acids (PUFA)
CC       hydroxylation. Catalyzes the epoxidation of double bonds of certain
CC       PUFA. Converts arachidonic acid toward epoxyeicosatrienoic acid (EET)
CC       regioisomers, 8,9-, 11,12-, and 14,15-EET, that function as lipid
CC       mediators in the vascular system. Displays an absolute
CC       stereoselectivity in the epoxidation of eicosapentaenoic acid (EPA)
CC       producing the 17(R),18(S) enantiomer. May play an important role in
CC       all-trans retinoic acid biosynthesis in extrahepatic tissues. Catalyzes
CC       two successive oxidative transformation of all-trans retinol to all-
CC       trans retinal and then to the active form all-trans retinoic acid. May
CC       also participate in eicosanoids metabolism by converting hydroperoxide
CC       species into oxo metabolites (lipoxygenase-like reaction, NADPH-
CC       independent). {ECO:0000250|UniProtKB:P04798}.
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:P04798};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17151;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
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:P04798};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47209;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
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:P04798};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47293;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=estrone + O2 + reduced [NADPH--hemoprotein reductase] =
CC         6alpha-hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:47308, 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:87605; Evidence={ECO:0000250|UniProtKB:P04798};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47309;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=estrone + O2 + reduced [NADPH--hemoprotein reductase] =
CC         15alpha-hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:47312, 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:87618; Evidence={ECO:0000250|UniProtKB:P04798};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47313;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=estrone + O2 + reduced [NADPH--hemoprotein reductase] =
CC         16alpha-hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:47204, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:776, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:17263, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:P04798};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47205;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
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:P04798};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47213;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
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:P04798};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47281;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase]
CC         = 6alpha-hydroxy-17beta-estradiol + H(+) + H2O + oxidized
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47284, 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:62847;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47285;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase]
CC         = 7alpha-hydroxy-17beta-estradiol + H(+) + H2O + oxidized
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47288, 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:87598;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47289;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase]
CC         = 15alpha-hydroxy-17beta-estradiol + H(+) + H2O + oxidized
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47276, 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:87593;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47277;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z)-eicosatrienoate + O2 + reduced [NADPH--hemoprotein
CC         reductase] = 19-hydroxy-(5Z,8Z,11Z)-eicosatrienoate + H(+) + H2O +
CC         oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50076,
CC         Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:78043, ChEBI:CHEBI:132024;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50077;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced
CC         [NADPH--hemoprotein reductase] = 16-hydroxy-(5Z,8Z,11Z,14Z)-
CC         eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:49972, 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:132019; Evidence={ECO:0000250|UniProtKB:P04798};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49973;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced
CC         [NADPH--hemoprotein reductase] = 17-hydroxy-(5Z,8Z,11Z,14Z)-
CC         eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:49968, 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:132016; Evidence={ECO:0000250|UniProtKB:P04798};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49969;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced
CC         [NADPH--hemoprotein reductase] = 18-hydroxy-(5Z,8Z,11Z,14Z)-
CC         eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:39811, 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:63590; Evidence={ECO:0000250|UniProtKB:P04798};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39812;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
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:P04798};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39760;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced
CC         [NADPH--hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z,17Z)-
CC         eicosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:39787, 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:76636; Evidence={ECO:0000250|UniProtKB:P04798};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39788;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced
CC         [NADPH--hemoprotein reductase] = (8R,9S)-epoxy-(5Z,11Z,14Z)-
CC         eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:49884, 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:131975; Evidence={ECO:0000250|UniProtKB:P04798};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49885;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced
CC         [NADPH--hemoprotein reductase] = (11R,12S)-epoxy-(5Z,8Z,14Z)-
CC         eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:49880, 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:131970; Evidence={ECO:0000250|UniProtKB:P04798};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49881;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
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:P04798};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49857;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
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:P04798};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49861;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
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:P04798};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39780;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced
CC         [NADPH--hemoprotein reductase] = (19S,20R)-epoxy-(4Z,7Z,10Z,13Z,16Z)-
CC         docosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:52124, 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:136411; Evidence={ECO:0000250|UniProtKB:P04798};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52125;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
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:P04798};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52121;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
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:P04798};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42093;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
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:P04798};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42089;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
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:P04798};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48717;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
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:P04798};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37948;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
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:P04798};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48637;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
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:P04798};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48633;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- PATHWAY: Steroid hormone biosynthesis. {ECO:0000250|UniProtKB:P04798}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC       {ECO:0000250|UniProtKB:P04798}.
CC   -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC       {ECO:0000250|UniProtKB:P04798}.
CC   -!- SUBUNIT: Interacts with cytosolic chaperones HSP70 and HSP90; this
CC       interaction is required for initial targeting to mitochondria.
CC       Interacts (via mitochondrial targeting signal) with TOMM40 (via N-
CC       terminus); this interaction is required for translocation across the
CC       mitochondrial outer membrane. {ECO:0000250|UniProtKB:P00185}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P00185}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P00185}. Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P00185}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P00185}. Microsome membrane
CC       {ECO:0000250|UniProtKB:P00185}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P00185}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P00185}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; D17575; BAA04500.1; -; mRNA.
DR   PIR; S21761; S21761.
DR   RefSeq; NP_001306411.1; NM_001319482.1.
DR   AlphaFoldDB; P33616; -.
DR   SMR; P33616; -.
DR   STRING; 9541.ENSMFAP00000021776; -.
DR   GlyCosmos; P33616; 1 site, No reported glycans.
DR   eggNOG; KOG0156; Eukaryota.
DR   OrthoDB; 2900138at2759; -.
DR   UniPathway; UPA00199; -.
DR   UniPathway; UPA00912; -.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
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; IEA:InterPro.
DR   GO; GO:0030544; F:Hsp70 protein binding; ISS:UniProtKB.
DR   GO; GO:0051879; F:Hsp90 protein 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:0008210; P:estrogen metabolic process; ISS:UniProtKB.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0042572; P:retinol metabolic process; ISS:UniProtKB.
DR   GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Cytoplasm; Endoplasmic reticulum; Glycoprotein; Heme; Iron;
KW   Lipid biosynthesis; Lipid metabolism; Lyase; Membrane; Metal-binding;
KW   Microsome; Mitochondrion; Mitochondrion inner membrane; Monooxygenase;
KW   Oxidoreductase; Reference proteome; Steroid biosynthesis.
FT   CHAIN           1..512
FT                   /note="Cytochrome P450 1A1"
FT                   /id="PRO_0000051628"
FT   REGION          29..40
FT                   /note="Mitochondrial targeting signal"
FT                   /evidence="ECO:0000250|UniProtKB:P00185"
FT   BINDING         224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         457
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        67
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        277
FT                   /note="Y -> H (in Ref. 2; BAA04500)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        490
FT                   /note="M -> V (in Ref. 2; BAA04500)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   512 AA;  58155 MW;  239A3237E3870ED7 CRC64;
     MLFRISMSAT EFLLASLIFC LVFWVIRASR PRVPKGLKNP PGPWGWPLIG HILTLGKNPH
     LALSRMSQRY GDVLQIRIGS TPVLVLSGLD TIRQALVQQG DDFKGRPNLY SFTLISNGQS
     MSFGPDSGPV WAARRRLAQN GLKSFSIASD PASSSSCYLE EHVSKEAEVL ISKLQEQMAG
     PGHFNPYRYV VISVANVICA ICFGQRYDHN HQELLSLVNL SNNFGEVVGS GNPADFIPIL
     RYLPNRSLNG FKDLNEKFHS FMQKMIKEHY KTFEKGYIRD ITDSLIEHCQ EKQLDENANI
     QLSDEKIVNV VLDLFGAGFD TVTTAISWSL MYLVTNPRVQ RKIQEELDTV IGRSRRPRLS
     DRSHLPYMEA FILETFRHSS FVPFTIPHST TRDTSLKGFY IPKGRCVFVN QWQINHDQKL
     WVNPSEFLPE RFITPDGAID KVLSEKVILF GLGKRKCIGE TIARWEVFLF LAILLQRVEF
     SVPPGVKVDM TPIYGLTMKH ACCEHFQMQL RS
//