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 27-MAR-2024, entry version 238. 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 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: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 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: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 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: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 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: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 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: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 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: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 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: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 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: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 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: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 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: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 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] = (14S,15R)-epoxy-(5Z,8Z,11Z)- CC eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein CC reductase]; Xref=Rhea:RHEA:49856, Rhea:RHEA-COMP:11964, Rhea:RHEA- CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, CC ChEBI:CHEBI:131964; Evidence={ECO: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 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: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 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: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 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: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 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: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 CC (2-hydroxylation) {ECO:0000269|PubMed:15805301}; CC Vmax=0.02 pmol/min/pmol enzyme toward 17beta-estradiol CC (4-hydroxylation) {ECO:0000269|PubMed:15805301}; CC Vmax=3.6 pmol/min/pmol enzyme toward 17beta-estradiol CC (6alpha-hydroxylation) {ECO:0000269|PubMed:15805301}; CC Vmax=0.9 pmol/min/pmol enzyme toward 17beta-estradiol CC (15alpha-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=PharmVar Pharmacogen Variation Consortium; CC Note=CYP1A1 alleles; CC URL="https://www.pharmvar.org/gene/CYP1A1"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=CYP1A1 entry; CC URL="https://en.wikipedia.org/wiki/CYP1A1"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 AlphaFoldDB; P04798; -. DR SMR; P04798; -. DR BioGRID; 107923; 79. DR IntAct; P04798; 48. DR STRING; 9606.ENSP00000378488; -. 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; DB14737; Cannabinol. 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; DB04840; Debrisoquine. DR DrugBank; DB01234; Dexamethasone. DR DrugBank; DB14649; Dexamethasone acetate. DR DrugBank; DB00633; Dexmedetomidine. DR DrugBank; DB11511; Difloxacin. DR DrugBank; DB08995; Diosmin. DR DrugBank; DB05928; Dovitinib. DR DrugBank; DB00470; Dronabinol. 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; DB16165; Finerenone. DR DrugBank; DB04841; Flunarizine. DR DrugBank; DB00499; Flutamide. DR DrugBank; DB01095; Fluvastatin. DR DrugBank; DB00176; Fluvoxamine. DR DrugBank; DB00317; Gefitinib. DR DrugBank; DB01381; Ginkgo biloba. 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 GlyCosmos; P04798; 1 site, No reported glycans. 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; 9606-ENSP00000369050; -. DR PeptideAtlas; P04798; -. DR ProteomicsDB; 51744; -. [P04798-1] DR ProteomicsDB; 654; -. DR ProteomicsDB; 655; -. DR Antibodypedia; 4356; 575 antibodies from 37 providers. DR DNASU; 1543; -. DR Ensembl; ENST00000379727.8; ENSP00000369050.3; ENSG00000140465.15. [P04798-1] DR Ensembl; ENST00000395048.6; ENSP00000378488.2; ENSG00000140465.15. [P04798-1] DR Ensembl; ENST00000562201.5; ENSP00000455340.1; ENSG00000140465.15. [P04798-2] DR Ensembl; ENST00000564596.5; ENSP00000457668.1; ENSG00000140465.15. [P04798-3] DR Ensembl; ENST00000567032.5; ENSP00000456585.1; ENSG00000140465.15. [P04798-1] DR Ensembl; ENST00000569630.5; ENSP00000455051.1; ENSG00000140465.15. [P04798-2] DR GeneID; 1543; -. DR KEGG; hsa:1543; -. DR MANE-Select; ENST00000379727.8; ENSP00000369050.3; NM_001319217.2; NP_001306146.1. DR UCSC; uc002ayp.4; human. [P04798-1] DR AGR; HGNC:2595; -. DR CTD; 1543; -. DR DisGeNET; 1543; -. DR GeneCards; CYP1A1; -. DR HGNC; HGNC:2595; CYP1A1. DR HPA; ENSG00000140465; Tissue enhanced (liver, 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; DPRAYWQ; -. DR OrthoDB; 2900138at2759; -. 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 SignaLink; P04798; -. DR SIGNOR; P04798; -. DR UniPathway; UPA00199; -. DR UniPathway; UPA00912; -. DR BioGRID-ORCS; 1543; 9 hits in 1148 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 male germ line stem cell (sensu Vertebrata) in testis and 116 other cell types or tissues. DR ExpressionAtlas; P04798; baseline and differential. 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:0120319; F:long-chain fatty acid omega-1 hydroxylase activity; IDA:UniProtKB. DR GO; GO:0102033; F:long-chain fatty acid omega-hydroxylase activity; IDA:UniProtKB. 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:0009308; P:amine metabolic process; IEA:Ensembl. DR GO; GO:0043010; P:camera-type eye development; 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: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:0001676; P:long-chain fatty acid metabolic process; IDA:UniProtKB. DR GO; GO:0060137; P:maternal process involved in parturition; IEA:Ensembl. DR GO; GO:0046209; P:nitric oxide metabolic process; 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:1904681; P:response to 3-methylcholanthrene; IEA:Ensembl. DR GO; GO:0046685; P:response to arsenic-containing substance; 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:0033189; P:response to vitamin A; 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:0048771; P:tissue remodeling; IEA:Ensembl. DR GO; GO:0042359; P:vitamin D metabolic process; IC:BHF-UCL. DR GO; GO:0006805; P:xenobiotic metabolic process; IDA:BHF-UCL. 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; P04798; HS. 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 BINDING 224 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:23508959" FT BINDING 457 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO: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, FT 17beta-estradiol and estrone respectively.; FT 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 //