ID   CP1A1_RAT               Reviewed;         524 AA.
AC   P00185;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   27-MAR-2024, entry version 194.
DE   RecName: Full=Cytochrome P450 1A1;
DE            Short=CYP1A1;
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=Cytochrome P450MT2;
DE   AltName: Full=Hydroperoxy icosatetraenoate dehydratase;
DE            EC=4.2.1.152 {ECO:0000250|UniProtKB:P04798};
DE   Contains:
DE     RecName: Full=Cytochrome P450MT2A;
DE   Contains:
DE     RecName: Full=Cytochrome P450MT2B;
GN   Name=Cyp1a1 {ECO:0000303|PubMed:19401463, ECO:0000312|RGD:2458};
GN   Synonyms=Cyp1a-1;
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 [GENOMIC DNA].
RX   PubMed=6089174; DOI=10.1073/pnas.81.16.5066;
RA   Sogawa K., Gotoh O., Kawajiri K., Fujii-Kuriyama Y.;
RT   "Distinct organization of methylcholanthrene- and phenobarbital-inducible
RT   cytochrome P-450 genes in the rat.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:5066-5070(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=6324135; DOI=10.1093/nar/12.6.2929;
RA   Yabusaki Y., Shimizu M., Murakami H., Nakamura K., Oeda K., Ohkawa H.;
RT   "Nucleotide sequence of a full-length cDNA coding for 3-methylcholanthrene-
RT   induced rat liver cytochrome P-450MC.";
RL   Nucleic Acids Res. 12:2929-2938(1984).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3838427; DOI=10.1016/0003-9861(85)90300-5;
RA   Hines R.N., Levy J.B., Conrad R.D., Iversen P.L., Shen M.-L., Renli A.M.,
RA   Bresnick E.;
RT   "Gene structure and nucleotide sequence for rat cytochrome P-450c.";
RL   Arch. Biochem. Biophys. 237:465-476(1985).
RN   [4]
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   [5]
RP   PROTEIN SEQUENCE OF 2-22.
RX   PubMed=3041969; DOI=10.1016/0006-2952(88)90634-x;
RA   Amelizad Z., Narbonne J.F., Wolf C.R., Robertson L.W., Oesch F.;
RT   "Effect of nutritional imbalances on cytochrome P-450 isozymes in rat
RT   liver.";
RL   Biochem. Pharmacol. 37:3245-3249(1988).
RN   [6]
RP   PARTIAL PROTEIN SEQUENCE.
RX   PubMed=8651689; DOI=10.1006/abbi.1996.0236;
RA   Cvrk T., Hodek P., Strobel H.W.;
RT   "Identification and characterization of cytochrome P4501A1 amino acid
RT   residues interacting with a radiolabeled photoaffinity diazido-
RT   benzphetamine analogue.";
RL   Arch. Biochem. Biophys. 330:142-152(1996).
RN   [7]
RP   SUBCELLULAR LOCATION, MUTAGENESIS OF 32-VAL-THR-33, AND TOPOLOGY.
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=9348277; DOI=10.1083/jcb.139.3.589;
RA   Addya S., Anandatheerthavarada H.K., Biswas G., Bhagwat S.V., Mullick J.,
RA   Avadhani N.G.;
RT   "Targeting of NH2-terminal-processed microsomal protein to mitochondria: a
RT   novel pathway for the biogenesis of hepatic mitochondrial P450MT2.";
RL   J. Cell Biol. 139:589-599(1997).
RN   [8]
RP   SUBCELLULAR LOCATION, INTERACTION WITH HSP70, INTERACTION WITH HSP90,
RP   INTERACTION WITH TOMM40, AND TOPOLOGY.
RX   PubMed=19401463; DOI=10.1074/jbc.m109.007492;
RA   Anandatheerthavarada H.K., Sepuri N.B., Avadhani N.G.;
RT   "Mitochondrial targeting of cytochrome P450 proteins containing NH2-
RT   terminal chimeric signals involves an unusual TOM20/TOM22 bypass
RT   mechanism.";
RL   J. Biol. Chem. 284:17352-17363(2009).
RN   [9]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=20972997; DOI=10.1002/rcm.4760;
RA   Mesaros C., Lee S.H., Blair I.A.;
RT   "Analysis of epoxyeicosatrienoic acids by chiral liquid
RT   chromatography/electron capture atmospheric pressure chemical ionization
RT   mass spectrometry using [13C]-analog internal standards.";
RL   Rapid Commun. Mass Spectrom. 24:3237-3247(2010).
RN   [10]
RP   GLYCOSYLATION AT SER-71.
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 (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 (By
CC       similarity). Displays different regioselectivities for polyunsaturated
CC       fatty acids (PUFA) hydroxylation (By similarity). Catalyzes the
CC       epoxidation of double bonds of certain PUFA (PubMed:20972997). Converts
CC       arachidonic acid toward epoxyeicosatrienoic acid (EET) regioisomers,
CC       8,9-, 11,12-, and 14,15-EET, that function as lipid mediators in the
CC       vascular system. Displays an absolute stereoselectivity in the
CC       epoxidation of eicosapentaenoic acid (EPA) producing the 17(R),18(S)
CC       enantiomer (By similarity). May play an important role in all-trans
CC       retinoic acid biosynthesis in extrahepatic tissues. Catalyzes two
CC       successive oxidative transformation of all-trans retinol to all-trans
CC       retinal and then to the active form all-trans retinoic acid (By
CC       similarity). May also participate in eicosanoids metabolism by
CC       converting hydroperoxide species into oxo metabolites (lipoxygenase-
CC       like reaction, NADPH-independent) (By similarity).
CC       {ECO:0000250|UniProtKB:P04798, ECO:0000269|PubMed:20972997}.
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:0000269|PubMed:20972997};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49885;
CC         Evidence={ECO:0000305|PubMed:20972997};
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:0000269|PubMed:20972997};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49881;
CC         Evidence={ECO:0000305|PubMed:20972997};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced
CC         [NADPH--hemoprotein reductase] = (11S,12R)-epoxy-(5Z,8Z,14Z)-
CC         eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:49876, 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:131969; Evidence={ECO:0000269|PubMed:20972997};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49877;
CC         Evidence={ECO:0000305|PubMed:20972997};
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:0000269|PubMed:20972997};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49861;
CC         Evidence={ECO:0000305|PubMed:20972997};
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:0000269|PubMed:20972997}.
CC   -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC       {ECO:0000250|UniProtKB:P04798}.
CC   -!- SUBUNIT: Both Cytochrome P450MT2A and Cytochrome P450MT2B interact with
CC       cytosolic chaperones HSP70 and HSP90; this interaction is required for
CC       initial targeting to mitochondria. P450MT2B interacts (via
CC       mitochondrial targeting signal) with TOMM40 (via N-terminus); this
CC       interaction is required for translocation across the mitochondrial
CC       outer membrane. {ECO:0000269|PubMed:19401463}.
CC   -!- SUBCELLULAR LOCATION: [Cytochrome P450 1A1]: Cytoplasm
CC       {ECO:0000269|PubMed:9348277}.
CC   -!- SUBCELLULAR LOCATION: [Cytochrome P450MT2A]: Endoplasmic reticulum
CC       membrane {ECO:0000269|PubMed:9348277}; Peripheral membrane protein
CC       {ECO:0000305|PubMed:19401463, ECO:0000305|PubMed:9348277}.
CC       Mitochondrion inner membrane {ECO:0000269|PubMed:9348277}; Peripheral
CC       membrane protein {ECO:0000305|PubMed:19401463,
CC       ECO:0000305|PubMed:9348277}. Microsome membrane
CC       {ECO:0000269|PubMed:9348277}; Peripheral membrane protein
CC       {ECO:0000305|PubMed:19401463, ECO:0000305|PubMed:9348277}.
CC   -!- SUBCELLULAR LOCATION: [Cytochrome P450MT2B]: Endoplasmic reticulum
CC       membrane; Peripheral membrane protein. Mitochondrion inner membrane
CC       {ECO:0000305|PubMed:19401463}; Peripheral membrane protein
CC       {ECO:0000305|PubMed:19401463, ECO:0000305|PubMed:9348277}. Microsome
CC       membrane {ECO:0000269|PubMed:9348277}; Peripheral membrane protein
CC       {ECO:0000305|PubMed:19401463, ECO:0000305|PubMed:9348277}.
CC   -!- TISSUE SPECIFICITY: Liver.
CC   -!- INDUCTION: By 3-methylcholanthrene (3MC) and beta-naphthoflavone (BNF).
CC   -!- DOMAIN: Contains a chimeric signal that facilitates targeting of the
CC       protein to both the endoplasmic reticulum and mitochondria. A 12 amino
CC       acid sequence between 33 and 44 functions as a putative mitochondrial-
CC       targeting signal. The removal of the first 4- or 32-amino acid residues
CC       from the intact protein positions the mitochondrial targeting signal
CC       for efficient binding to the mitochondrial import receptors. The
CC       membrane-free P4501A1 seems to be more sensitive to proteolysis.
CC   -!- PTM: Two forms; MT2A (long form) and MT2B (short form); are produced by
CC       NH2-terminal proteolytic cleavage. This cleavage activates a cryptic
CC       mitochondrial targeting signal.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; K02246; AAA41027.1; -; Genomic_DNA.
DR   EMBL; X00469; CAA25153.1; -; mRNA.
DR   EMBL; M26129; AAA41025.1; -; Genomic_DNA.
DR   PIR; A00185; O4RTMC.
DR   RefSeq; NP_036672.2; NM_012540.2.
DR   RefSeq; XP_006243212.1; XM_006243150.2.
DR   AlphaFoldDB; P00185; -.
DR   SMR; P00185; -.
DR   BioGRID; 246477; 2.
DR   STRING; 10116.ENSRNOP00000026473; -.
DR   BindingDB; P00185; -.
DR   ChEMBL; CHEMBL2922; -.
DR   DrugBank; DB13746; Bioallethrin.
DR   DrugBank; DB01645; Genistein.
DR   SwissLipids; SLP:000001590; -.
DR   GlyCosmos; P00185; 1 site, No reported glycans.
DR   GlyGen; P00185; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P00185; -.
DR   PhosphoSitePlus; P00185; -.
DR   PaxDb; 10116-ENSRNOP00000026473; -.
DR   Ensembl; ENSRNOT00000026473.5; ENSRNOP00000026473.2; ENSRNOG00000019500.5.
DR   Ensembl; ENSRNOT00055051799; ENSRNOP00055042736; ENSRNOG00055029892.
DR   Ensembl; ENSRNOT00060036849; ENSRNOP00060030361; ENSRNOG00060021246.
DR   Ensembl; ENSRNOT00065029266; ENSRNOP00065023214; ENSRNOG00065017500.
DR   GeneID; 24296; -.
DR   KEGG; rno:24296; -.
DR   UCSC; RGD:2458; rat.
DR   AGR; RGD:2458; -.
DR   CTD; 1543; -.
DR   RGD; 2458; Cyp1a1.
DR   eggNOG; KOG0156; Eukaryota.
DR   GeneTree; ENSGT00950000183037; -.
DR   HOGENOM; CLU_001570_22_0_1; -.
DR   InParanoid; P00185; -.
DR   OMA; DPRAYWQ; -.
DR   OrthoDB; 2900138at2759; -.
DR   PhylomeDB; P00185; -.
DR   TreeFam; TF105095; -.
DR   Reactome; R-RNO-211981; Xenobiotics.
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-9018681; Biosynthesis of protectins.
DR   SABIO-RK; P00185; -.
DR   UniPathway; UPA00199; -.
DR   UniPathway; UPA00912; -.
DR   PRO; PR:P00185; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000019500; Expressed in duodenum and 10 other cell types or tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR   GO; GO:0008391; F:arachidonic acid monooxygenase activity; ISO:RGD.
DR   GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003824; F:catalytic activity; IDA:RGD.
DR   GO; GO:0032451; F:demethylase activity; IDA:RGD.
DR   GO; GO:0019899; F:enzyme binding; IDA: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:0016711; F:flavonoid 3'-monooxygenase activity; IDA:RGD.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0030544; F:Hsp70 protein binding; IDA:UniProtKB.
DR   GO; GO:0051879; F:Hsp90 protein binding; IDA: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:0120319; F:long-chain fatty acid omega-1 hydroxylase activity; ISO:RGD.
DR   GO; GO:0102033; F:long-chain fatty acid omega-hydroxylase activity; ISO:RGD.
DR   GO; GO:0004497; F:monooxygenase activity; IDA:RGD.
DR   GO; GO:0016491; F:oxidoreductase activity; IDA:RGD.
DR   GO; GO:0016679; F:oxidoreductase activity, acting on diphenols and related substances as donors; IDA: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; ISO:RGD.
DR   GO; GO:0008395; F:steroid hydroxylase activity; IDA:RGD.
DR   GO; GO:0070576; F:vitamin D 24-hydroxylase activity; ISO:RGD.
DR   GO; GO:0042904; P:9-cis-retinoic acid biosynthetic process; IDA:RGD.
DR   GO; GO:0009308; P:amine metabolic process; ISO:RGD.
DR   GO; GO:0043010; P:camera-type eye development; IEP:RGD.
DR   GO; GO:0071280; P:cellular response to copper ion; IEP:RGD.
DR   GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:RGD.
DR   GO; GO:0009804; P:coumarin metabolic process; IDA:RGD.
DR   GO; GO:0019341; P:dibenzo-p-dioxin catabolic process; IDA:RGD.
DR   GO; GO:0018894; P:dibenzo-p-dioxin metabolic process; IDA:RGD.
DR   GO; GO:0048565; P:digestive tract development; IEP:RGD.
DR   GO; GO:0008210; P:estrogen metabolic process; ISS:UniProtKB.
DR   GO; GO:0006631; P:fatty acid metabolic process; ISO:RGD.
DR   GO; GO:0009812; P:flavonoid metabolic process; IDA:RGD.
DR   GO; GO:0070365; P:hepatocyte differentiation; IEP:RGD.
DR   GO; GO:0046483; P:heterocycle metabolic process; ISO:RGD.
DR   GO; GO:0050665; P:hydrogen peroxide biosynthetic process; ISO:RGD.
DR   GO; GO:0017143; P:insecticide metabolic process; IDA:RGD.
DR   GO; GO:0002933; P:lipid hydroxylation; ISO:RGD.
DR   GO; GO:0001889; P:liver development; IEP:RGD.
DR   GO; GO:0001676; P:long-chain fatty acid metabolic process; ISO:RGD.
DR   GO; GO:0060137; P:maternal process involved in parturition; IEP:RGD.
DR   GO; GO:0046209; P:nitric oxide metabolic process; IEP:RGD.
DR   GO; GO:0006778; P:porphyrin-containing compound metabolic process; IDA:RGD.
DR   GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IDA:RGD.
DR   GO; GO:1904681; P:response to 3-methylcholanthrene; IEP:RGD.
DR   GO; GO:0046685; P:response to arsenic-containing substance; IEP:RGD.
DR   GO; GO:0032094; P:response to food; IEP:RGD.
DR   GO; GO:0009635; P:response to herbicide; IEP:RGD.
DR   GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
DR   GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR   GO; GO:0035902; P:response to immobilization stress; IEP:RGD.
DR   GO; GO:0010041; P:response to iron(III) ion; IEP:RGD.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR   GO; GO:0009624; P:response to nematode; 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:0009636; P:response to toxic substance; ISO:RGD.
DR   GO; GO:0033189; P:response to vitamin A; 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:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008202; P:steroid metabolic process; ISO:RGD.
DR   GO; GO:0048771; P:tissue remodeling; IEP:RGD.
DR   GO; GO:0009404; P:toxin metabolic process; ISO:RGD.
DR   GO; GO:0006805; P:xenobiotic metabolic process; ISO:RGD.
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.
DR   Genevisible; P00185; RN.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Endoplasmic reticulum; Glycoprotein;
KW   Heme; Iron; Lipid biosynthesis; Lipid metabolism; Lyase; Membrane;
KW   Metal-binding; Microsome; Mitochondrion; Mitochondrion inner membrane;
KW   Monooxygenase; Oxidoreductase; Reference proteome; Steroid biosynthesis.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000305"
FT   CHAIN           2..524
FT                   /note="Cytochrome P450 1A1"
FT                   /id="PRO_0000003564"
FT   CHAIN           5..524
FT                   /note="Cytochrome P450MT2A"
FT                   /id="PRO_0000003565"
FT   CHAIN           33..524
FT                   /note="Cytochrome P450MT2B"
FT                   /id="PRO_0000003566"
FT   REGION          33..44
FT                   /note="Mitochondrial targeting signal"
FT                   /evidence="ECO:0000269|PubMed:19401463,
FT                   ECO:0000269|PubMed:9348277"
FT   BINDING         228
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         461
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        71
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000269|PubMed:24098488"
FT   MUTAGEN         32..33
FT                   /note="VT->AI: No proteolytic cleavage."
FT                   /evidence="ECO:0000269|PubMed:9348277"
FT   CONFLICT        21..22
FT                   /note="TT -> VV (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        53
FT                   /note="I -> M (in Ref. 2; CAA25153)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        494
FT                   /note="M -> S (in Ref. 3; AAA41025)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   524 AA;  59393 MW;  C766DF8044D598C5 CRC64;
     MPSVYGFPAF TSATELLLAV TTFCLGFWVV RVTRTWVPKG LKSPPGPWGL PFIGHVLTLG
     KNPHLSLTKL SQQYGDVLQI RIGSTPVVVL SGLNTIKQAL VKQGDDFKGR PDLYSFTLIA
     NGQSMTFNPD SGPLWAARRR LAQNALKSFS IASDPTLASS CYLEEHVSKE AEYLISKFQK
     LMAEVGHFDP FKYLVVSVAN VICAICFGRR YDHDDQELLS IVNLSNEFGE VTGSGYPADF
     IPILRYLPNS SLDAFKDLNK KFYSFMKKLI KEHYRTFEKG HIRDITDSLI EHCQDRRLDE
     NANVQLSDDK VITIVFDLFG AGFDTITTAI SWSLMYLVTN PRIQRKIQEE LDTVIGRDRQ
     PRLSDRPQLP YLEAFILETF RHSSFVPFTI PHSTIRDTSL NGFYIPKGHC VFVNQWQVNH
     DQELWGDPNE FRPERFLTSS GTLDKHLSEK VILFGLGKRK CIGETIGRLE VFLFLAILLQ
     QMEFNVSPGE KVDMTPAYGL TLKHARCEHF QVQMRSSGPQ HLQA
//