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Database: UniProt
Entry: P04798
LinkDB: P04798
Original site: P04798 
ID   CP1A1_HUMAN             Reviewed;         512 AA.
AC   P04798; A4F3V9; A4F3W0; Q53G18;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   29-SEP-2021, entry version 226.
DE   RecName: Full=Cytochrome P450 1A1 {ECO:0000303|PubMed:11555828};
DE            Short=CYPIA1 {ECO:0000303|PubMed:10681376};
DE            EC=1.14.14.1 {ECO:0000269|PubMed:12865317, ECO:0000269|PubMed:15041462, ECO:0000269|PubMed:15805301, ECO:0000269|PubMed:18577768};
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 {ECO:0000305|PubMed:21068195};
DE            EC=4.2.1.152 {ECO:0000269|PubMed:21068195};
GN   Name=CYP1A1 {ECO:0000303|PubMed:10681376, ECO:0000312|HGNC:HGNC:2595};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2989797; DOI=10.1093/nar/13.12.4503;
RA   Jaiswal A.K., Gonzales F.J., Nebert D.W.;
RT   "Human P1-450 gene sequence and correlation of mRNA with genetic
RT   differences in benzo[a]pyrene metabolism.";
RL   Nucleic Acids Res. 13:4503-4520(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=3838385; DOI=10.1126/science.3838385;
RA   Jaiswal A.K., Gonzalez F.J., Nebert D.W.;
RT   "Human dioxin-inducible cytochrome P1-450: complementary DNA and amino acid
RT   sequence.";
RL   Science 228:80-83(1985).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Placenta;
RX   PubMed=3019683; DOI=10.1111/j.1432-1033.1986.tb09857.x;
RA   Kawajiri K., Watanabe J., Gotoh O., Tagashira Y., Sogawa K.,
RA   Fujii-Kuriyama Y.;
RT   "Structure and drug inducibility of the human cytochrome P-450c gene.";
RL   Eur. J. Biochem. 159:219-225(1986).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11207026; DOI=10.1097/00008571-200102000-00001;
RA   Corchero J., Pimprale S., Kimura S., Gonzalez F.J.;
RT   "Organization of the CYP1A cluster on human chromosome 15: implications for
RT   gene regulation.";
RL   Pharmacogenetics 11:1-6(2001).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
RC   TISSUE=Blood;
RA   Graebsch C., Bauer M.;
RT   "Cloning and sequencing of new alternative splicing variants of human
RT   CYP1A1 gene.";
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASP-45.
RA   Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA   Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16572171; DOI=10.1038/nature04601;
RA   Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA   Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA   FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA   Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA   Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA   DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA   Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA   Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA   Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA   O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA   Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA   Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT   "Analysis of the DNA sequence and duplication history of human chromosome
RT   15.";
RL   Nature 440:671-675(2006).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Cervix;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 282-425 (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=9500998; DOI=10.1006/bbrc.1998.8171;
RA   Yun C.H., Park H.J., Kim S.J., Kim H.K.;
RT   "Identification of cytochrome P450 1A1 in human brain.";
RL   Biochem. Biophys. Res. Commun. 243:808-810(1998).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 295-484 (ISOFORM 1).
RX   PubMed=3000715; DOI=10.1089/dna.1985.4.395;
RA   Quattrochi L.C., Okino S.T., Pendurthi U.R., Tukey R.H.;
RT   "Cloning and isolation of human cytochrome P-450 cDNAs homologous to
RT   dioxin-inducible rabbit mRNAs encoding P-450 4 and P-450 6.";
RL   DNA 4:395-400(1985).
RN   [11]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=10681376;
RA   Chen H., Howald W.N., Juchau M.R.;
RT   "Biosynthesis of all-trans-retinoic acid from all-trans-retinol: catalysis
RT   of all-trans-retinol oxidation by human P-450 cytochromes.";
RL   Drug Metab. Dispos. 28:315-322(2000).
RN   [12]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=11555828; DOI=10.1053/meta.2001.25592;
RA   Badawi A.F., Cavalieri E.L., Rogan E.G.;
RT   "Role of human cytochrome P450 1A1, 1A2, 1B1, and 3A4 in the 2-, 4-, and
RT   16alpha-hydroxylation of 17beta-estradiol.";
RL   Metabolism 50:1001-1003(2001).
RN   [13]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=14559847;
RA   Lee A.J., Conney A.H., Zhu B.T.;
RT   "Human cytochrome P450 3A7 has a distinct high catalytic activity for the
RT   16alpha-hydroxylation of estrone but not 17beta-estradiol.";
RL   Cancer Res. 63:6532-6536(2003).
RN   [14]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=12865317; DOI=10.1210/en.2003-0192;
RA   Lee A.J., Cai M.X., Thomas P.E., Conney A.H., Zhu B.T.;
RT   "Characterization of the oxidative metabolites of 17beta-estradiol and
RT   estrone formed by 15 selectively expressed human cytochrome p450
RT   isoforms.";
RL   Endocrinology 144:3382-3398(2003).
RN   [15]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=15041462; DOI=10.1016/j.bcp.2003.12.023;
RA   Schwarz D., Kisselev P., Ericksen S.S., Szklarz G.D., Chernogolov A.,
RA   Honeck H., Schunck W.H., Roots I.;
RT   "Arachidonic and eicosapentaenoic acid metabolism by human CYP1A1: highly
RT   stereoselective formation of 17(R),18(S)-epoxyeicosatetraenoic acid.";
RL   Biochem. Pharmacol. 67:1445-1457(2004).
RN   [16]
RP   FUNCTION, CATALYTIC ACTIVITY, CHARACTERIZATION OF VARIANT ASN-461 AND
RP   VARIANT VAL-462, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX   PubMed=15805301; DOI=10.1158/0008-5472.can-04-3543;
RA   Kisselev P., Schunck W.H., Roots I., Schwarz D.;
RT   "Association of CYP1A1 polymorphisms with differential metabolic activation
RT   of 17beta-estradiol and estrone.";
RL   Cancer Res. 65:2972-2978(2005).
RN   [17]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=18577768; DOI=10.1194/jlr.m800199-jlr200;
RA   Fer M., Corcos L., Dreano Y., Plee-Gautier E., Salaun J.P., Berthou F.,
RA   Amet Y.;
RT   "Cytochromes P450 from family 4 are the main omega hydroxylating enzymes in
RT   humans: CYP4F3B is the prominent player in PUFA metabolism.";
RL   J. Lipid Res. 49:2379-2389(2008).
RN   [18]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=19965576; DOI=10.1194/jlr.m003061;
RA   Lucas D., Goulitquer S., Marienhagen J., Fer M., Dreano Y., Schwaneberg U.,
RA   Amet Y., Corcos L.;
RT   "Stereoselective epoxidation of the last double bond of polyunsaturated
RT   fatty acids by human cytochromes P450.";
RL   J. Lipid Res. 51:1125-1133(2010).
RN   [19]
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   [20]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=21068195; DOI=10.1124/dmd.110.035121;
RA   Bui P., Imaizumi S., Beedanagari S.R., Reddy S.T., Hankinson O.;
RT   "Human CYP2S1 metabolizes cyclooxygenase- and lipoxygenase-derived
RT   eicosanoids.";
RL   Drug Metab. Dispos. 39:180-190(2011).
RN   [21]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [22]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 35-512 IN COMPLEX WITH HEME AND
RP   INHIBITOR ALPHA-NAPHTOFLAVONE, AND COFACTOR.
RX   PubMed=23508959; DOI=10.1074/jbc.m113.452953;
RA   Walsh A.A., Szklarz G.D., Scott E.E.;
RT   "Human cytochrome P450 1A1 structure and utility in understanding drug and
RT   xenobiotic metabolism.";
RL   J. Biol. Chem. 288:12932-12943(2013).
RN   [23]
RP   VARIANT VAL-462.
RX   PubMed=1722803; DOI=10.1093/oxfordjournals.jbchem.a123594;
RA   Hayashi S., Watanabe J., Nakachi K., Kawajiri K.;
RT   "Genetic linkage of lung cancer-associated MspI polymorphisms with amino
RT   acid replacement in the heme binding region of the human cytochrome P450IA1
RT   gene.";
RL   J. Biochem. 110:407-411(1991).
RN   [24]
RP   VARIANT ASN-461.
RX   PubMed=8895751;
RA   Cascorbi I., Brockmoller J., Roots I.;
RT   "A C4887A polymorphism in exon 7 of human CYP1A1: population frequency,
RT   mutation linkages, and impact on lung cancer susceptibility.";
RL   Cancer Res. 56:4965-4969(1996).
RN   [25]
RP   VARIANT TRP-279.
RX   PubMed=10739168; DOI=10.1097/00008571-200002000-00003;
RA   Smart J., Daly A.K.;
RT   "Variation in induced CYP1A1 levels: relationship to CYP1A1, Ah receptor
RT   and GSTM1 polymorphisms.";
RL   Pharmacogenetics 10:11-24(2000).
RN   [26]
RP   VARIANTS ILE-331 AND SER-464.
RX   PubMed=11295847; DOI=10.1002/humu.49;
RA   Chevalier D., Allorge D., Lo-Guidice J.-M., Cauffiez C., Lhermitte M.,
RA   Lafitte J.-J., Broly F.;
RT   "Detection of known and two novel (M331I and R464S) missense mutations in
RT   the human CYP1A1 gene in a French Caucasian population.";
RL   Hum. Mutat. 17:355-355(2001).
RN   [27]
RP   VARIANTS ASN-448; CYS-464; TRP-477 AND ARG-492.
RX   PubMed=15618738; DOI=10.2133/dmpk.18.218;
RA   Saito M., Egashira M., Kiyotani K., Fujieda M., Yamazaki H., Kiyohara C.,
RA   Kunitoh H., Kamataki T.;
RT   "Novel nonsynonymous polymorphisms of the CYP1A1 Gene in Japanese.";
RL   Drug Metab. Pharmacokinet. 18:218-222(2003).
RN   [28]
RP   VARIANTS ASP-45; THR-78; TRP-93; ARG-173; ASN-461; MET-482 AND ARG-492.
RX   PubMed=15469410; DOI=10.1517/14622416.5.7.895;
RA   Solus J.F., Arietta B.J., Harris J.R., Sexton D.P., Steward J.Q.,
RA   McMunn C., Ihrie P., Mehall J.M., Edwards T.L., Dawson E.P.;
RT   "Genetic variation in eleven phase I drug metabolism genes in an ethnically
RT   diverse population.";
RL   Pharmacogenomics 5:895-931(2004).
RN   [29]
RP   VARIANTS ASP-45; THR-78; ASN-461 AND VAL-462.
RX   PubMed=15643613; DOI=10.1002/humu.20134;
RA   Jiang Z., Dalton T.P., Jin L., Wang B., Tsuneoka Y., Shertzer H.G.,
RA   Deka R., Nebert D.W.;
RT   "Toward the evaluation of function in genetic variability: characterizing
RT   human SNP frequencies and establishing BAC-transgenic mice carrying the
RT   human CYP1A1_CYP1A2 locus.";
RL   Hum. Mutat. 25:196-206(2005).
RN   [30]
RP   VARIANT [LARGE SCALE ANALYSIS] TRP-477.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of
CC       various endogenous substrates, including fatty acids, steroid hormones
CC       and vitamins (PubMed:11555828, PubMed:14559847, PubMed:12865317,
CC       PubMed:15805301, PubMed:15041462, PubMed:18577768, PubMed:19965576,
CC       PubMed:20972997, PubMed:10681376). Mechanistically, uses molecular
CC       oxygen inserting one oxygen atom into a substrate, and reducing the
CC       second into a water molecule, with two electrons provided by NADPH via
CC       cytochrome P450 reductase (NADPH--hemoprotein reductase)
CC       (PubMed:11555828, PubMed:14559847, PubMed:12865317, PubMed:15805301,
CC       PubMed:15041462, PubMed:18577768, PubMed:19965576, PubMed:20972997,
CC       PubMed:10681376). Catalyzes the hydroxylation of carbon-hydrogen bonds.
CC       Exhibits high catalytic activity for the formation of hydroxyestrogens
CC       from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and
CC       E2, as well as D-ring hydroxylated E1 and E2 at the C15-alpha and C16-
CC       alpha positions (PubMed:11555828, PubMed:14559847, PubMed:12865317,
CC       PubMed:15805301). Displays different regioselectivities for
CC       polyunsaturated fatty acids (PUFA) hydroxylation (PubMed:15041462,
CC       PubMed:18577768). Catalyzes the epoxidation of double bonds of certain
CC       PUFA (PubMed:15041462, PubMed:19965576, 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 (PubMed:20972997). Displays an absolute
CC       stereoselectivity in the epoxidation of eicosapentaenoic acid (EPA)
CC       producing the 17(R),18(S) enantiomer (PubMed:15041462). May play an
CC       important role in all-trans retinoic acid biosynthesis in extrahepatic
CC       tissues. Catalyzes two successive oxidative transformation of all-trans
CC       retinol to all-trans retinal and then to the active form all-trans
CC       retinoic acid (PubMed:10681376). May also participate in eicosanoids
CC       metabolism by converting hydroperoxide species into oxo metabolites
CC       (lipoxygenase-like reaction, NADPH-independent) (PubMed:21068195).
CC       {ECO:0000269|PubMed:10681376, ECO:0000269|PubMed:11555828,
CC       ECO:0000269|PubMed:12865317, ECO:0000269|PubMed:14559847,
CC       ECO:0000269|PubMed:15041462, ECO:0000269|PubMed:15805301,
CC       ECO:0000269|PubMed:18577768, ECO:0000269|PubMed:19965576,
CC       ECO:0000269|PubMed:20972997, ECO:0000269|PubMed:21068195}.
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:0000269|PubMed:12865317, ECO:0000269|PubMed:15041462,
CC         ECO:0000269|PubMed:15805301, ECO:0000269|PubMed:18577768};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17151;
CC         Evidence={ECO:0000305|PubMed:12865317, ECO:0000305|PubMed:15041462,
CC         ECO:0000305|PubMed:15805301, ECO:0000305|PubMed:18577768};
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:0000269|PubMed:12865317,
CC         ECO:0000269|PubMed:15805301};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47209;
CC         Evidence={ECO:0000305|PubMed:12865317, ECO:0000305|PubMed:15805301};
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:0000269|PubMed:12865317,
CC         ECO:0000269|PubMed:15805301};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47293;
CC         Evidence={ECO:0000305|PubMed:12865317, ECO:0000305|PubMed:15805301};
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:0000269|PubMed:12865317,
CC         ECO:0000269|PubMed:15805301};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47309;
CC         Evidence={ECO:0000305|PubMed:12865317, ECO:0000305|PubMed:15805301};
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:0000269|PubMed:12865317,
CC         ECO:0000269|PubMed:15805301};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47313;
CC         Evidence={ECO:0000305|PubMed:12865317, ECO:0000305|PubMed:15805301};
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:0000269|PubMed:12865317,
CC         ECO:0000269|PubMed:14559847};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47205;
CC         Evidence={ECO:0000305|PubMed:12865317, ECO:0000305|PubMed:14559847};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase]
CC         = 2-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH--
CC         hemoprotein reductase]; Xref=Rhea:RHEA:47212, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16469, ChEBI:CHEBI:28744,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000269|PubMed:11555828, ECO:0000269|PubMed:12865317,
CC         ECO:0000269|PubMed:15805301};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47213;
CC         Evidence={ECO:0000305|PubMed:11555828, ECO:0000305|PubMed:12865317,
CC         ECO:0000305|PubMed:15805301};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase]
CC         = 4-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH--
CC         hemoprotein reductase]; Xref=Rhea:RHEA:47280, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16469, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:62845;
CC         Evidence={ECO:0000269|PubMed:12865317};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47281;
CC         Evidence={ECO:0000305|PubMed:12865317};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase]
CC         = 6alpha-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH--
CC         hemoprotein reductase]; Xref=Rhea:RHEA:47284, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16469, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:62847;
CC         Evidence={ECO:0000269|PubMed:12865317, ECO:0000269|PubMed:15805301};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47285;
CC         Evidence={ECO:0000305|PubMed:12865317, ECO:0000305|PubMed:15805301};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase]
CC         = 7alpha-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH--
CC         hemoprotein reductase]; Xref=Rhea:RHEA:47288, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16469, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:87598;
CC         Evidence={ECO:0000269|PubMed:12865317};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47289;
CC         Evidence={ECO:0000305|PubMed:12865317};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase]
CC         = 15alpha-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH--
CC         hemoprotein reductase]; Xref=Rhea:RHEA:47276, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16469, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:87593;
CC         Evidence={ECO:0000269|PubMed:12865317, ECO:0000269|PubMed:15805301};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47277;
CC         Evidence={ECO:0000305|PubMed:12865317, ECO:0000305|PubMed:15805301};
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:0000269|PubMed:18577768};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50077;
CC         Evidence={ECO:0000305|PubMed:18577768};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC         hemoprotein reductase] = 16-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate
CC         + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC         Xref=Rhea:RHEA:49972, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:132019; Evidence={ECO:0000269|PubMed:15041462};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49973;
CC         Evidence={ECO:0000305|PubMed:15041462};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC         hemoprotein reductase] = 17-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate
CC         + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC         Xref=Rhea:RHEA:49968, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:132016; Evidence={ECO:0000269|PubMed:15041462};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49969;
CC         Evidence={ECO:0000305|PubMed:15041462};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC         hemoprotein reductase] = 18-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate
CC         + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC         Xref=Rhea:RHEA:39811, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:63590; Evidence={ECO:0000269|PubMed:15041462};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39812;
CC         Evidence={ECO:0000305|PubMed:15041462};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC         hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate
CC         + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC         Xref=Rhea:RHEA:39759, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:76627; Evidence={ECO:0000269|PubMed:15041462,
CC         ECO:0000269|PubMed:18577768};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39760;
CC         Evidence={ECO:0000305|PubMed:15041462, ECO:0000305|PubMed:18577768};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--
CC         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:0000269|PubMed:15041462};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39788;
CC         Evidence={ECO:0000305|PubMed:15041462};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC         hemoprotein reductase] = (8R,9S)-epoxy-(5Z,11Z,14Z)-eicosatrienoate +
CC         H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC         Xref=Rhea:RHEA:49884, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI: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 [NADPH--
CC         hemoprotein reductase] = (11R,12S)-epoxy-(5Z,8Z,14Z)-eicosatrienoate
CC         + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC         Xref=Rhea:RHEA:49880, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI: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 [NADPH--
CC         hemoprotein reductase] = (14S,15R)-epoxy-(5Z,8Z,11Z)-eicosatrienoate
CC         + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC         Xref=Rhea:RHEA:49856, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:131964; Evidence={ECO:0000269|PubMed:19965576};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49857;
CC         Evidence={ECO:0000305|PubMed:19965576};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC         hemoprotein reductase] = (14R,15S)-epoxy-(5Z,8Z,11Z)-eicosatrienoate
CC         + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC         Xref=Rhea:RHEA:49860, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:131965; Evidence={ECO:0000269|PubMed:19965576,
CC         ECO:0000269|PubMed:20972997};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49861;
CC         Evidence={ECO:0000305|PubMed:19965576, ECO:0000305|PubMed:20972997};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--
CC         hemoprotein reductase] = (17R,18S)-epoxy-(5Z,8Z,11Z,14Z)-
CC         eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:39779, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:58562,
CC         ChEBI:CHEBI:76634; Evidence={ECO:0000269|PubMed:15041462,
CC         ECO:0000269|PubMed:19965576};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39780;
CC         Evidence={ECO:0000305|PubMed:15041462, ECO:0000305|PubMed:19965576};
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:0000269|PubMed:19965576};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52125;
CC         Evidence={ECO:0000305|PubMed:19965576};
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:0000269|PubMed:19965576};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52121;
CC         Evidence={ECO:0000305|PubMed:19965576};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=all-trans-retinol + O2 + reduced [NADPH--hemoprotein
CC         reductase] = all-trans-retinal + H(+) + 2 H2O + oxidized [NADPH--
CC         hemoprotein reductase]; Xref=Rhea:RHEA:42092, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:17336, ChEBI:CHEBI:17898,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000269|PubMed:10681376};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42093;
CC         Evidence={ECO:0000305|PubMed:10681376};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=all-trans-retinal + O2 + reduced [NADPH--hemoprotein
CC         reductase] = all-trans-retinoate + 2 H(+) + H2O + oxidized [NADPH--
CC         hemoprotein reductase]; Xref=Rhea:RHEA:42088, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:17898, ChEBI:CHEBI:35291,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000269|PubMed:10681376};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42089;
CC         Evidence={ECO:0000305|PubMed:10681376};
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:0000269|PubMed:21068195};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48717;
CC         Evidence={ECO:0000305|PubMed:21068195};
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:0000269|PubMed:21068195};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37948;
CC         Evidence={ECO:0000305|PubMed:21068195};
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:0000269|PubMed:21068195};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48637;
CC         Evidence={ECO:0000305|PubMed:21068195};
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:0000269|PubMed:21068195};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48633;
CC         Evidence={ECO:0000305|PubMed:21068195};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000269|PubMed:23508959};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=8 uM for all-trans retinol {ECO:0000269|PubMed:10681376};
CC         KM=9.5 uM for 17beta-estradiol (2-hydroxylation)
CC         {ECO:0000269|PubMed:15805301};
CC         KM=11.8 uM for 17beta-estradiol (4-hydroxylation)
CC         {ECO:0000269|PubMed:15805301};
CC         KM=79 uM for 17beta-estradiol (6alpha-hydroxylation)
CC         {ECO:0000269|PubMed:15805301};
CC         KM=19.6 uM for 17beta-estradiol (15alpha-hydroxylation)
CC         {ECO:0000269|PubMed:15805301};
CC         KM=12.2 uM for estrone (2-hydroxylation)
CC         {ECO:0000269|PubMed:15805301};
CC         KM=22.6 uM for estrone (4-hydroxylation)
CC         {ECO:0000269|PubMed:15805301};
CC         KM=86 uM for estrone (6alpha-hydroxylation)
CC         {ECO:0000269|PubMed:15805301};
CC         KM=85 uM for estrone (15alpha-hydroxylation)
CC         {ECO:0000269|PubMed:15805301};
CC         Vmax=507 pmol/min/nmol enzyme toward all-trans retinol
CC         {ECO:0000269|PubMed:10681376};
CC         Vmax=0.6 pmol/min/pmol enzyme toward 17beta-estradiol (2-
CC         hydroxylation) {ECO:0000269|PubMed:15805301};
CC         Vmax=0.02 pmol/min/pmol enzyme toward 17beta-estradiol (4-
CC         hydroxylation) {ECO:0000269|PubMed:15805301};
CC         Vmax=3.6 pmol/min/pmol enzyme toward 17beta-estradiol (6alpha-
CC         hydroxylation) {ECO:0000269|PubMed:15805301};
CC         Vmax=0.9 pmol/min/pmol enzyme toward 17beta-estradiol (15alpha-
CC         hydroxylation) {ECO:0000269|PubMed:15805301};
CC         Vmax=0.4 pmol/min/pmol enzyme toward estrone (2-hydroxylation)
CC         {ECO:0000269|PubMed:15805301};
CC         Vmax=0.1 pmol/min/pmol enzyme toward estrone (4-hydroxylation)
CC         {ECO:0000269|PubMed:15805301};
CC         Vmax=0.2 pmol/min/pmol enzyme toward estrone (6alpha-hydroxylation)
CC         {ECO:0000269|PubMed:15805301};
CC         Vmax=1.2 pmol/min/pmol enzyme toward estrone (15alpha-hydroxylation)
CC         {ECO:0000269|PubMed:15805301};
CC   -!- PATHWAY: Steroid hormone biosynthesis. {ECO:0000269|PubMed:11555828,
CC       ECO:0000269|PubMed:12865317, ECO:0000269|PubMed:14559847,
CC       ECO:0000269|PubMed:15805301}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC       {ECO:0000269|PubMed:15041462, ECO:0000269|PubMed:18577768,
CC       ECO:0000269|PubMed:19965576, ECO:0000269|PubMed:20972997,
CC       ECO:0000269|PubMed:21068195}.
CC   -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC       {ECO:0000269|PubMed:10681376}.
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   -!- INTERACTION:
CC       P04798; Q96DZ9: CMTM5; NbExp=3; IntAct=EBI-10194262, EBI-2548702;
CC       P04798; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-10194262, EBI-11522780;
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P04798-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P04798-2; Sequence=VSP_053364, VSP_053365;
CC       Name=3;
CC         IsoId=P04798-3; Sequence=VSP_053363, VSP_053366;
CC   -!- TISSUE SPECIFICITY: Lung, lymphocytes and placenta.
CC   -!- INDUCTION: By 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD).
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Cytochrome P450 Allele Nomenclature Committee;
CC       Note=CYP1A1 alleles;
CC       URL="http://www.cypalleles.ki.se/cyp1a1.htm";
CC   -!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
CC       polymorphism database;
CC       URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=CYP1A1";
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=CYP1A1 entry;
CC       URL="https://en.wikipedia.org/wiki/CYP1A1";
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DR   EMBL; X02612; CAA26458.1; -; Genomic_DNA.
DR   EMBL; K03191; AAA52139.1; -; mRNA.
DR   EMBL; X04300; CAA27843.1; -; Genomic_DNA.
DR   EMBL; AF253322; AAK25727.1; -; Genomic_DNA.
DR   EMBL; AM233518; CAJ80721.1; -; mRNA.
DR   EMBL; AM233519; CAJ80722.1; -; mRNA.
DR   EMBL; AM233520; CAJ80723.1; -; mRNA.
DR   EMBL; AK223113; BAD96833.1; -; mRNA.
DR   EMBL; AC091230; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC023019; AAH23019.1; -; mRNA.
DR   EMBL; M12079; AAA52152.1; -; mRNA.
DR   EMBL; AF040259; AAD10199.1; -; mRNA.
DR   CCDS; CCDS10268.1; -. [P04798-1]
DR   PIR; A24797; O4HU6.
DR   RefSeq; NP_000490.1; NM_000499.4. [P04798-1]
DR   RefSeq; NP_001306145.1; NM_001319216.1.
DR   RefSeq; NP_001306146.1; NM_001319217.1. [P04798-1]
DR   PDB; 4I8V; X-ray; 2.60 A; A/B/C/D=35-512.
DR   PDB; 6DWM; X-ray; 2.85 A; A/B/C/D=35-512.
DR   PDB; 6DWN; X-ray; 3.00 A; A/B/C/D=35-512.
DR   PDB; 6O5Y; X-ray; 3.17 A; A/B/C/D=35-512.
DR   PDB; 6UDL; X-ray; 2.85 A; A/B/C/D=35-512.
DR   PDB; 6UDM; X-ray; 3.08 A; A/B/C/D=35-512.
DR   PDBsum; 4I8V; -.
DR   PDBsum; 6DWM; -.
DR   PDBsum; 6DWN; -.
DR   PDBsum; 6O5Y; -.
DR   PDBsum; 6UDL; -.
DR   PDBsum; 6UDM; -.
DR   SMR; P04798; -.
DR   BioGRID; 107923; 76.
DR   IntAct; P04798; 48.
DR   STRING; 9606.ENSP00000369050; -.
DR   BindingDB; P04798; -.
DR   ChEMBL; CHEMBL2231; -.
DR   DrugBank; DB08496; (R)-warfarin.
DR   DrugBank; DB02342; 2-Methoxyestradiol.
DR   DrugBank; DB00518; Albendazole.
DR   DrugBank; DB01118; Amiodarone.
DR   DrugBank; DB00381; Amlodipine.
DR   DrugBank; DB00613; Amodiaquine.
DR   DrugBank; DB00972; Azelastine.
DR   DrugBank; DB04957; Azimilide.
DR   DrugBank; DB04975; Banoxantrone.
DR   DrugBank; DB06770; Benzyl alcohol.
DR   DrugBank; DB01393; Bezafibrate.
DR   DrugBank; DB00201; Caffeine.
DR   DrugBank; DB09061; Cannabidiol.
DR   DrugBank; DB01136; Carvedilol.
DR   DrugBank; DB00608; Chloroquine.
DR   DrugBank; DB00356; Chlorzoxazone.
DR   DrugBank; DB00169; Cholecalciferol.
DR   DrugBank; DB00568; Cinnarizine.
DR   DrugBank; DB01407; Clenbuterol.
DR   DrugBank; DB00636; Clofibrate.
DR   DrugBank; DB00575; Clonidine.
DR   DrugBank; DB00363; Clozapine.
DR   DrugBank; DB12483; Copanlisib.
DR   DrugBank; DB00851; Dacarbazine.
DR   DrugBank; DB06292; Dapagliflozin.
DR   DrugBank; DB01254; Dasatinib.
DR   DrugBank; DB00694; Daunorubicin.
DR   DrugBank; DB04840; Debrisoquine.
DR   DrugBank; DB01234; Dexamethasone.
DR   DrugBank; DB14649; Dexamethasone acetate.
DR   DrugBank; DB00633; Dexmedetomidine.
DR   DrugBank; DB11511; Difloxacin.
DR   DrugBank; DB05928; Dovitinib.
DR   DrugBank; DB08846; Ellagic acid.
DR   DrugBank; DB00530; Erlotinib.
DR   DrugBank; DB00783; Estradiol.
DR   DrugBank; DB13952; Estradiol acetate.
DR   DrugBank; DB13953; Estradiol benzoate.
DR   DrugBank; DB13954; Estradiol cypionate.
DR   DrugBank; DB13955; Estradiol dienanthate.
DR   DrugBank; DB13956; Estradiol valerate.
DR   DrugBank; DB00655; Estrone.
DR   DrugBank; DB00898; Ethanol.
DR   DrugBank; DB04841; Flunarizine.
DR   DrugBank; DB00499; Flutamide.
DR   DrugBank; DB01095; Fluvastatin.
DR   DrugBank; DB00176; Fluvoxamine.
DR   DrugBank; DB00317; Gefitinib.
DR   DrugBank; DB00889; Granisetron.
DR   DrugBank; DB00502; Haloperidol.
DR   DrugBank; DB12379; Indirubin.
DR   DrugBank; DB01064; Isoprenaline.
DR   DrugBank; DB11757; Istradefylline.
DR   DrugBank; DB01167; Itraconazole.
DR   DrugBank; DB01026; Ketoconazole.
DR   DrugBank; DB00448; Lansoprazole.
DR   DrugBank; DB00455; Loratadine.
DR   DrugBank; DB04871; Lorcaserin.
DR   DrugBank; DB09238; Manidipine.
DR   DrugBank; DB00643; Mebendazole.
DR   DrugBank; DB14009; Medical Cannabis.
DR   DrugBank; DB01065; Melatonin.
DR   DrugBank; DB00170; Menadione.
DR   DrugBank; DB00553; Methoxsalen.
DR   DrugBank; DB14011; Nabiximols.
DR   DrugBank; DB00184; Nicotine.
DR   DrugBank; DB01115; Nifedipine.
DR   DrugBank; DB00325; Nitroprusside.
DR   DrugBank; DB01059; Norfloxacin.
DR   DrugBank; DB00338; Omeprazole.
DR   DrugBank; DB00738; Pentamidine.
DR   DrugBank; DB08922; Perospirone.
DR   DrugBank; DB03783; Phenacetin.
DR   DrugBank; DB01174; Phenobarbital.
DR   DrugBank; DB00466; Picrotoxin.
DR   DrugBank; DB01132; Pioglitazone.
DR   DrugBank; DB01087; Primaquine.
DR   DrugBank; DB00396; Progesterone.
DR   DrugBank; DB00818; Propofol.
DR   DrugBank; DB00571; Propranolol.
DR   DrugBank; DB00550; Propylthiouracil.
DR   DrugBank; DB00165; Pyridoxine.
DR   DrugBank; DB00908; Quinidine.
DR   DrugBank; DB00468; Quinine.
DR   DrugBank; DB01129; Rabeprazole.
DR   DrugBank; DB02709; Resveratrol.
DR   DrugBank; DB00740; Riluzole.
DR   DrugBank; DB08931; Riociguat.
DR   DrugBank; DB15305; Risdiplam.
DR   DrugBank; DB06176; Romidepsin.
DR   DrugBank; DB06654; Safinamide.
DR   DrugBank; DB01591; Solifenacin.
DR   DrugBank; DB00428; Streptozocin.
DR   DrugBank; DB00605; Sulindac.
DR   DrugBank; DB00675; Tamoxifen.
DR   DrugBank; DB04905; Tesmilifene.
DR   DrugBank; DB00624; Testosterone.
DR   DrugBank; DB13943; Testosterone cypionate.
DR   DrugBank; DB13944; Testosterone enanthate.
DR   DrugBank; DB13946; Testosterone undecanoate.
DR   DrugBank; DB01041; Thalidomide.
DR   DrugBank; DB00277; Theophylline.
DR   DrugBank; DB00730; Thiabendazole.
DR   DrugBank; DB01685; Topiroxostat.
DR   DrugBank; DB00539; Toremifene.
DR   DrugBank; DB00755; Tretinoin.
DR   DrugBank; DB12245; Triclabendazole.
DR   DrugBank; DB11155; Triclocarban.
DR   DrugBank; DB00197; Troglitazone.
DR   GuidetoPHARMACOLOGY; 1318; -.
DR   SwissLipids; SLP:000001329; -.
DR   GlyGen; P04798; 1 site.
DR   iPTMnet; P04798; -.
DR   PhosphoSitePlus; P04798; -.
DR   BioMuta; CYP1A1; -.
DR   DMDM; 117139; -.
DR   EPD; P04798; -.
DR   MassIVE; P04798; -.
DR   MaxQB; P04798; -.
DR   PaxDb; P04798; -.
DR   PeptideAtlas; P04798; -.
DR   PRIDE; P04798; -.
DR   ProteomicsDB; 51744; -. [P04798-1]
DR   ProteomicsDB; 654; -.
DR   ProteomicsDB; 655; -.
DR   Antibodypedia; 4356; 535 antibodies.
DR   DNASU; 1543; -.
DR   Ensembl; ENST00000379727; ENSP00000369050; ENSG00000140465. [P04798-1]
DR   Ensembl; ENST00000395048; ENSP00000378488; ENSG00000140465. [P04798-1]
DR   Ensembl; ENST00000562201; ENSP00000455340; ENSG00000140465. [P04798-2]
DR   Ensembl; ENST00000564596; ENSP00000457668; ENSG00000140465. [P04798-3]
DR   Ensembl; ENST00000567032; ENSP00000456585; ENSG00000140465. [P04798-1]
DR   Ensembl; ENST00000569630; ENSP00000455051; ENSG00000140465. [P04798-2]
DR   GeneID; 1543; -.
DR   KEGG; hsa:1543; -.
DR   UCSC; uc002ayp.4; human. [P04798-1]
DR   CTD; 1543; -.
DR   DisGeNET; 1543; -.
DR   GeneCards; CYP1A1; -.
DR   HGNC; HGNC:2595; CYP1A1.
DR   HPA; ENSG00000140465; Group enriched (liver, lung, urinary bladder).
DR   MIM; 108330; gene.
DR   neXtProt; NX_P04798; -.
DR   OpenTargets; ENSG00000140465; -.
DR   PharmGKB; PA27092; -.
DR   VEuPathDB; HostDB:ENSG00000140465; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   GeneTree; ENSGT00950000183037; -.
DR   HOGENOM; CLU_1209426_0_0_1; -.
DR   InParanoid; P04798; -.
DR   OMA; NYGFRIE; -.
DR   OrthoDB; 1389393at2759; -.
DR   PhylomeDB; P04798; -.
DR   TreeFam; TF105095; -.
DR   PathwayCommons; P04798; -.
DR   Reactome; R-HSA-1989781; PPARA activates gene expression.
DR   Reactome; R-HSA-211981; Xenobiotics.
DR   Reactome; R-HSA-2142670; Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET).
DR   Reactome; R-HSA-2142816; Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE).
DR   Reactome; R-HSA-9018681; Biosynthesis of protectins.
DR   SABIO-RK; P04798; -.
DR   SIGNOR; P04798; -.
DR   UniPathway; UPA00199; -.
DR   UniPathway; UPA00912; -.
DR   BioGRID-ORCS; 1543; 4 hits in 1012 CRISPR screens.
DR   ChiTaRS; CYP1A1; human.
DR   GeneWiki; Cytochrome_P450,_family_1,_member_A1; -.
DR   GenomeRNAi; 1543; -.
DR   Pharos; P04798; Tchem.
DR   PRO; PR:P04798; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; P04798; protein.
DR   Bgee; ENSG00000140465; Expressed in islet of Langerhans and 129 other tissues.
DR   ExpressionAtlas; P04798; baseline and differential.
DR   Genevisible; P04798; HS.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0008391; F:arachidonic acid monooxygenase activity; IDA:UniProtKB.
DR   GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032451; F:demethylase activity; IEA:Ensembl.
DR   GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR   GO; GO:0101020; F:estrogen 16-alpha-hydroxylase activity; IDA:UniProtKB.
DR   GO; GO:0101021; F:estrogen 2-hydroxylase activity; IDA:UniProtKB.
DR   GO; GO:0016711; F:flavonoid 3'-monooxygenase activity; IEA:Ensembl.
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:0004497; F:monooxygenase activity; IBA:GO_Central.
DR   GO; GO:0016491; F:oxidoreductase activity; IDA:BHF-UCL.
DR   GO; GO:0016679; F:oxidoreductase activity, acting on diphenols and related substances as donors; IEA:Ensembl.
DR   GO; GO:0019825; F:oxygen binding; TAS:ProtInc.
DR   GO; GO:0070576; F:vitamin D 24-hydroxylase activity; IDA:BHF-UCL.
DR   GO; GO:0042904; P:9-cis-retinoic acid biosynthetic process; IEA:Ensembl.
DR   GO; GO:0007568; P:aging; IEA:Ensembl.
DR   GO; GO:0009308; P:amine metabolic process; IEA:Ensembl.
DR   GO; GO:0043010; P:camera-type eye development; IEA:Ensembl.
DR   GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR   GO; GO:0071280; P:cellular response to copper ion; IEA:Ensembl.
DR   GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
DR   GO; GO:0009804; P:coumarin metabolic process; IEA:Ensembl.
DR   GO; GO:0019341; P:dibenzo-p-dioxin catabolic process; IEA:Ensembl.
DR   GO; GO:0048565; P:digestive tract development; IEA:Ensembl.
DR   GO; GO:0006306; P:DNA methylation; IEA:Ensembl.
DR   GO; GO:0017144; P:drug metabolic process; IDA:BHF-UCL.
DR   GO; GO:0019373; P:epoxygenase P450 pathway; TAS:Reactome.
DR   GO; GO:0008210; P:estrogen metabolic process; IDA:UniProtKB.
DR   GO; GO:0009692; P:ethylene metabolic process; TAS:Reactome.
DR   GO; GO:0006631; P:fatty acid metabolic process; IDA:UniProtKB.
DR   GO; GO:0009812; P:flavonoid metabolic process; IEA:Ensembl.
DR   GO; GO:0070365; P:hepatocyte differentiation; IEA:Ensembl.
DR   GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IEA:Ensembl.
DR   GO; GO:0017143; P:insecticide metabolic process; IEA:Ensembl.
DR   GO; GO:0002933; P:lipid hydroxylation; IDA:BHF-UCL.
DR   GO; GO:0042759; P:long-chain fatty acid biosynthetic process; TAS:Reactome.
DR   GO; GO:0060137; P:maternal process involved in parturition; IEA:Ensembl.
DR   GO; GO:0097267; P:omega-hydroxylase P450 pathway; TAS:Reactome.
DR   GO; GO:0006778; P:porphyrin-containing compound metabolic process; IEA:Ensembl.
DR   GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0046677; P:response to antibiotic; IEA:Ensembl.
DR   GO; GO:0046685; P:response to arsenic-containing substance; IEA:Ensembl.
DR   GO; GO:0042493; P:response to drug; IEA:Ensembl.
DR   GO; GO:0032094; P:response to food; IEA:Ensembl.
DR   GO; GO:0009635; P:response to herbicide; IEA:Ensembl.
DR   GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl.
DR   GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR   GO; GO:0035902; P:response to immobilization stress; IEA:Ensembl.
DR   GO; GO:0010041; P:response to iron(III) ion; IEA:Ensembl.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0009624; P:response to nematode; IEA:Ensembl.
DR   GO; GO:0009615; P:response to virus; IEA:Ensembl.
DR   GO; GO:0033189; P:response to vitamin A; IEA:Ensembl.
DR   GO; GO:0009611; P:response to wounding; IEA:Ensembl.
DR   GO; GO:0042572; P:retinol metabolic process; IDA:UniProtKB.
DR   GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008202; P:steroid metabolic process; IDA:BHF-UCL.
DR   GO; GO:0042359; P:vitamin D metabolic process; IC:BHF-UCL.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR008066; Cyt_P450_E_grp-I_CYP1.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR01683; EP450ICYP1A.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Endoplasmic reticulum;
KW   Fatty acid metabolism; Glycoprotein; Heme; Iron; Lipid biosynthesis;
KW   Lipid metabolism; Lyase; Membrane; Metal-binding; Microsome; Mitochondrion;
KW   Mitochondrion inner membrane; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Steroid biosynthesis.
FT   CHAIN           1..512
FT                   /note="Cytochrome P450 1A1"
FT                   /id="PRO_0000051627"
FT   REGION          29..40
FT                   /note="Mitochondrial targeting signal"
FT                   /evidence="ECO:0000250|UniProtKB:P00185"
FT   METAL           457
FT                   /note="Iron (heme axial ligand)"
FT                   /evidence="ECO:0000269|PubMed:23508959"
FT   BINDING         224
FT                   /note="Substrate"
FT                   /evidence="ECO:0000269|PubMed:23508959"
FT   CARBOHYD        67
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..261
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.5"
FT                   /id="VSP_053363"
FT   VAR_SEQ         189
FT                   /note="Y -> T (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.5"
FT                   /id="VSP_053364"
FT   VAR_SEQ         190..512
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.5"
FT                   /id="VSP_053365"
FT   VAR_SEQ         419..512
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.5"
FT                   /id="VSP_053366"
FT   VARIANT         45
FT                   /note="G -> D (in dbSNP:rs4646422)"
FT                   /evidence="ECO:0000269|PubMed:15469410,
FT                   ECO:0000269|PubMed:15643613, ECO:0000269|Ref.6"
FT                   /id="VAR_023194"
FT   VARIANT         66
FT                   /note="M -> V (in dbSNP:rs35035798)"
FT                   /id="VAR_033817"
FT   VARIANT         78
FT                   /note="I -> T (in dbSNP:rs17861094)"
FT                   /evidence="ECO:0000269|PubMed:15469410,
FT                   ECO:0000269|PubMed:15643613"
FT                   /id="VAR_023195"
FT   VARIANT         93
FT                   /note="R -> W (in dbSNP:rs2229150)"
FT                   /evidence="ECO:0000269|PubMed:15469410"
FT                   /id="VAR_024706"
FT   VARIANT         173
FT                   /note="T -> R (in dbSNP:rs28399427)"
FT                   /evidence="ECO:0000269|PubMed:15469410"
FT                   /id="VAR_024707"
FT   VARIANT         279
FT                   /note="R -> W (in dbSNP:rs34260157)"
FT                   /evidence="ECO:0000269|PubMed:10739168"
FT                   /id="VAR_009280"
FT   VARIANT         286
FT                   /note="I -> T (in dbSNP:rs4987133)"
FT                   /id="VAR_020122"
FT   VARIANT         331
FT                   /note="M -> I (in allele CYP1A1*6; dbSNP:rs56313657)"
FT                   /evidence="ECO:0000269|PubMed:11295847"
FT                   /id="VAR_016937"
FT   VARIANT         448
FT                   /note="I -> N (in allele CYP1A1*8; dbSNP:rs72547509)"
FT                   /evidence="ECO:0000269|PubMed:15618738"
FT                   /id="VAR_016938"
FT   VARIANT         461
FT                   /note="T -> N (in allele CYP1A1*4; displays similar
FT                   catalytic efficiency toward estrogens when compared to the
FT                   wild-type enzyme.; dbSNP:rs1799814)"
FT                   /evidence="ECO:0000269|PubMed:15469410,
FT                   ECO:0000269|PubMed:15643613, ECO:0000269|PubMed:15805301,
FT                   ECO:0000269|PubMed:8895751"
FT                   /id="VAR_008342"
FT   VARIANT         462
FT                   /note="I -> V (in allele CYP1A1*2B and allele CYP1A1*2C;
FT                   displays 5.7- and 12-fold increase in catalytic efficiency
FT                   in the formation of 2-hydroxylated estrogens, 17beta-
FT                   estradiol and estrone respectively.; dbSNP:rs1048943)"
FT                   /evidence="ECO:0000269|PubMed:15643613,
FT                   ECO:0000269|PubMed:15805301, ECO:0000269|PubMed:1722803"
FT                   /id="VAR_001243"
FT   VARIANT         464
FT                   /note="R -> C (in allele CYP1A1*9; dbSNP:rs41279188)"
FT                   /evidence="ECO:0000269|PubMed:15618738"
FT                   /id="VAR_016939"
FT   VARIANT         464
FT                   /note="R -> S (in allele CYP1A1*5; dbSNP:rs41279188)"
FT                   /evidence="ECO:0000269|PubMed:11295847"
FT                   /id="VAR_016940"
FT   VARIANT         470
FT                   /note="F -> V (in dbSNP:rs36121583)"
FT                   /id="VAR_033818"
FT   VARIANT         477
FT                   /note="R -> W (in allele CYP1A1*10; dbSNP:rs56240201)"
FT                   /evidence="ECO:0000269|PubMed:15618738,
FT                   ECO:0000269|PubMed:16959974"
FT                   /id="VAR_016941"
FT   VARIANT         482
FT                   /note="V -> M (in dbSNP:rs28399429)"
FT                   /evidence="ECO:0000269|PubMed:15469410"
FT                   /id="VAR_024708"
FT   VARIANT         492
FT                   /note="P -> R (in allele CYP1A1*11; dbSNP:rs28399430)"
FT                   /evidence="ECO:0000269|PubMed:15469410,
FT                   ECO:0000269|PubMed:15618738"
FT                   /id="VAR_016942"
FT   CONFLICT        26
FT                   /note="I -> M (in Ref. 2; AAA52139)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        235
FT                   /note="D -> E (in Ref. 2; AAA52139)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        381
FT                   /note="F -> L (in Ref. 1; CAA26458)"
FT                   /evidence="ECO:0000305"
FT   TURN            47..49
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   HELIX           52..55
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   HELIX           59..70
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   STRAND          72..78
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   STRAND          81..86
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   HELIX           89..96
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   TURN            97..99
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   HELIX           100..103
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   HELIX           110..114
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   HELIX           116..118
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   TURN            121..123
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   HELIX           129..145
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   STRAND          154..157
FT                   /evidence="ECO:0007829|PDB:6DWM"
FT   HELIX           158..179
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   HELIX           186..203
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   HELIX           212..218
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   STRAND          219..221
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   HELIX           224..228
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   HELIX           233..235
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   HELIX           238..242
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   HELIX           246..271
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   HELIX           281..292
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   STRAND          296..298
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   STRAND          300..302
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   HELIX           304..308
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   HELIX           310..334
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   HELIX           337..350
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   TURN            351..353
FT                   /evidence="ECO:0007829|PDB:6UDL"
FT   HELIX           359..364
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   HELIX           366..379
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   STRAND          394..396
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   STRAND          399..401
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   STRAND          406..410
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   HELIX           411..415
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   TURN            418..420
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   STRAND          421..423
FT                   /evidence="ECO:0007829|PDB:6UDL"
FT   HELIX           429..432
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   STRAND          435..437
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   HELIX           441..444
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   HELIX           453..455
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   HELIX           460..477
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   STRAND          478..481
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   STRAND          495..497
FT                   /evidence="ECO:0007829|PDB:4I8V"
FT   STRAND          506..510
FT                   /evidence="ECO:0007829|PDB:4I8V"
SQ   SEQUENCE   512 AA;  58165 MW;  3C62366044148EFD CRC64;
     MLFPISMSAT EFLLASVIFC LVFWVIRASR PQVPKGLKNP PGPWGWPLIG HMLTLGKNPH
     LALSRMSQQY GDVLQIRIGS TPVVVLSGLD TIRQALVRQG DDFKGRPDLY TFTLISNGQS
     MSFSPDSGPV WAARRRLAQN GLKSFSIASD PASSTSCYLE EHVSKEAEVL ISTLQELMAG
     PGHFNPYRYV VVSVTNVICA ICFGRRYDHN HQELLSLVNL NNNFGEVVGS GNPADFIPIL
     RYLPNPSLNA FKDLNEKFYS FMQKMVKEHY KTFEKGHIRD ITDSLIEHCQ EKQLDENANV
     QLSDEKIINI VLDLFGAGFD TVTTAISWSL MYLVMNPRVQ RKIQEELDTV IGRSRRPRLS
     DRSHLPYMEA FILETFRHSS FVPFTIPHST TRDTSLKGFY IPKGRCVFVN QWQINHDQKL
     WVNPSEFLPE RFLTPDGAID KVLSEKVIIF GMGKRKCIGE TIARWEVFLF LAILLQRVEF
     SVPLGVKVDM TPIYGLTMKH ACCEHFQMQL RS
//
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