ID CP1A2_HUMAN Reviewed; 516 AA. AC P05177; Q16754; Q6NWU3; Q6NWU5; Q9BXX7; Q9UK49; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 12-SEP-2018, sequence version 4. DT 27-MAR-2024, entry version 228. DE RecName: Full=Cytochrome P450 1A2 {ECO:0000303|PubMed:14725854}; DE EC=1.14.14.1 {ECO:0000269|PubMed:11555828, ECO:0000269|PubMed:12865317, ECO:0000269|PubMed:9435160}; DE AltName: Full=CYPIA2; DE AltName: Full=Cholesterol 25-hydroxylase {ECO:0000305|PubMed:21576599}; DE AltName: Full=Cytochrome P(3)450; DE AltName: Full=Cytochrome P450 4; DE AltName: Full=Cytochrome P450-P3; DE AltName: Full=Hydroperoxy icosatetraenoate dehydratase {ECO:0000305|PubMed:21068195}; DE EC=4.2.1.152 {ECO:0000269|PubMed:21068195}; GN Name=CYP1A2 {ECO:0000303|PubMed:2575218, ECO:0000312|HGNC:HGNC:2596}; 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 [MRNA]. RX PubMed=3755823; DOI=10.1093/nar/14.16.6773; RA Jaiswal A.K., Nebert D.W., Gonzalez F.J.; RT "Human P3(450): cDNA and complete amino acid sequence."; RL Nucleic Acids Res. 14:6773-6774(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RX PubMed=3462722; DOI=10.1073/pnas.83.18.6731; RA Quattrochi L.C., Pendurthi U.R., Okino S.T., Potenza C., Tukey R.H.; RT "Human cytochrome P-450 4 mRNA and gene: part of a multigene family that RT contains Alu sequences in its mRNA."; RL Proc. Natl. Acad. Sci. U.S.A. 83:6731-6735(1986). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2575218; DOI=10.1210/mend-3-9-1399; RA Ikeya K., Jaiswal A.K., Owens R.A., Jones J.E., Nebert D.W., Kimura S.; RT "Human CYP1A2: sequence, gene structure, comparison with the mouse and rat RT orthologous gene, and differences in liver 1A2 mRNA expression."; RL Mol. Endocrinol. 3:1399-1408(1989). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX PubMed=3681487; RA Jaiswal A.K., Nebert D.W., McBride O.W., Gonzalez F.J.; RT "Human P(3)450: cDNA and complete protein sequence, repetitive Alu RT sequences in the 3' nontranslated region, and localization of gene to RT chromosome 15."; RL J. Exp. Pathol. 3:1-17(1987). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-314. RC TISSUE=Liver; RA Zhuge J., Qian Y., Xie H., Yu Y.; RT "Sequence of a new human cytochrome P450-1A2 cDNA."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [6] 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 [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-73; ASN-104; PHE-111; RP VAL-205; TRP-281 AND ILE-438. RG NIEHS SNPs program; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 PROTEIN SEQUENCE OF 2-19. RX PubMed=3517618; RA Wrighton S.A., Campanile C., Thomas P.E., Maines S.L., Watkins P.B., RA Parker G., Mendez-Picon G., Haniu M., Shively J.E., Levin W., RA Guzelian P.S.; RT "Identification of a human liver cytochrome P-450 homologous to the major RT isosafrole-inducible cytochrome P-450 in the rat."; RL Mol. Pharmacol. 29:405-410(1986). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 295-485. RC TISSUE=Liver; 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, AND PATHWAY. RX PubMed=9435160; RA Bylund J., Kunz T., Valmsen K., Oliw E.H.; RT "Cytochromes P450 with bisallylic hydroxylation activity on arachidonic and RT linoleic acids studied with human recombinant enzymes and with human and RT rat liver microsomes."; RL J. Pharmacol. Exp. Ther. 284:51-60(1998). RN [12] 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 [13] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. 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 [14] RP FUNCTION, AND CATALYTIC ACTIVITY. 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, BIOPHYSICOCHEMICAL PROPERTIES, AND CHARACTERIZATION OF VARIANTS RP ASN-348; PHE-386; TYR-406 AND TRP-431. RX PubMed=14725854; DOI=10.1016/j.abb.2003.11.019; RA Zhou H., Josephy P.D., Kim D., Guengerich F.P.; RT "Functional characterization of four allelic variants of human cytochrome RT P450 1A2."; RL Arch. Biochem. Biophys. 422:23-30(2004). RN [16] 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 [17] 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 [18] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND PATHWAY. RX PubMed=21576599; DOI=10.1194/jlr.m014084; RA Honda A., Miyazaki T., Ikegami T., Iwamoto J., Maeda T., Hirayama T., RA Saito Y., Teramoto T., Matsuzaki Y.; RT "Cholesterol 25-hydroxylation activity of CYP3A."; RL J. Lipid Res. 52:1509-1516(2011). RN [19] 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 [20] RP INTERACTION WITH PGRMC1. RX PubMed=26988023; DOI=10.1038/ncomms11030; RA Kabe Y., Nakane T., Koike I., Yamamoto T., Sugiura Y., Harada E., RA Sugase K., Shimamura T., Ohmura M., Muraoka K., Yamamoto A., Uchida T., RA Iwata S., Yamaguchi Y., Krayukhina E., Noda M., Handa H., Ishimori K., RA Uchiyama S., Kobayashi T., Suematsu M.; RT "Haem-dependent dimerization of PGRMC1/Sigma-2 receptor facilitates cancer RT proliferation and chemoresistance."; RL Nat. Commun. 7:11030-11030(2016). RN [21] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 27-515 IN COMPLEX WITH THE RP INHIBITOR ALPHA-NAPHTHOFLAVONE AND HEME. RX PubMed=17311915; DOI=10.1074/jbc.m611692200; RA Sansen S., Yano J.K., Reynald R.L., Schoch G.A., Griffin K.J., Stout C.D., RA Johnson E.F.; RT "Adaptations for the oxidation of polycyclic aromatic hydrocarbons RT exhibited by the structure of human P450 1A2."; RL J. Biol. Chem. 282:14348-14355(2007). RN [22] RP VARIANT LEU-21. RX PubMed=9884316; RA Huang J.D., Guo W.C., Lai M.D., Guo Y.L., Lambert G.H.; RT "Detection of a novel cytochrome P-450 1A2 polymorphism (F21L) in RT Chinese."; RL Drug Metab. Dispos. 27:98-101(1999). RN [23] RP VARIANTS ASN-348; PHE-386; TYR-406 AND TRP-431. RX PubMed=11295848; RA Chevalier D., Cauffiez C., Allorge D., Lo-Guidice J.-M., Lhermitte M., RA Lafitte J.-J., Broly F.; RT "Five novel natural allelic variants-951A->C, 1042G->A (D348N), 1156A->T RT (I386F), 1217G->A (C406Y) and 1291C->T (C431Y)-of the human CYP1A2 gene in RT a French Caucasian population."; RL Hum. Mutat. 17:355-356(2001). RN [24] RP VARIANTS MET-83; GLN-168; LEU-186; CYS-212; SER-299 AND ILE-438. RX PubMed=14563787; DOI=10.1124/jpet.103.055798; RA Murayama N., Soyama A., Saito Y., Nakajima Y., Komamura K., Ueno K., RA Kamakura S., Kitakaze M., Kimura H., Goto Y., Saitoh O., Katoh M., RA Ohnuma T., Kawai M., Sugai K., Ohtsuki T., Suzuki C., Minami N., Ozawa S., RA Sawada J.; RT "Six novel nonsynonymous CYP1A2 gene polymorphisms: catalytic activities of RT the naturally occurring variant enzymes."; RL J. Pharmacol. Exp. Ther. 308:300-306(2004). RN [25] RP VARIANTS CYS-18; ARG-298; VAL-314 AND TRP-431. 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 [26] RP VARIANTS ARG-42; GLN-377 AND HIS-456. RX PubMed=15770072; DOI=10.2133/dmpk.20.24; RA Soyama A., Saito Y., Hanioka N., Maekawa K., Komamura K., Kamakura S., RA Kitakaze M., Tomoike H., Ueno K., Goto Y., Kimura H., Katoh M., Sugai K., RA Saitoh O., Kawai M., Ohnuma T., Ohtsuki T., Suzuki C., Minami N., RA Kamatani N., Ozawa S., Sawada J.; RT "Single nucleotide polymorphisms and haplotypes of CYP1A2 in a Japanese RT population."; RL Drug Metab. Pharmacokinet. 20:24-33(2005). RN [27] RP VARIANT CYS-18. 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 [28] RP EFFECT OF CAFFEINE METABOLISM ON RISKS OF MYOCARDIAL INFARCTION, RP POLYMORPHISM, AND FUNCTION. RX PubMed=16522833; DOI=10.1001/jama.295.10.1135; RA Cornelis M.C., El-Sohemy A., Kabagambe E.K., Campos H.; RT "Coffee, CYP1A2 genotype, and risk of myocardial infarction."; RL JAMA 295:1135-1141(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:9435160, PubMed:10681376, PubMed:11555828, CC PubMed:12865317, PubMed:19965576). 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:9435160, PubMed:10681376, PubMed:11555828, PubMed:12865317, CC PubMed:19965576). Catalyzes the hydroxylation of carbon-hydrogen bonds CC (PubMed:11555828, PubMed:12865317). Exhibits high catalytic activity CC for the formation of hydroxyestrogens from estrone (E1) and 17beta- CC estradiol (E2), namely 2-hydroxy E1 and E2 (PubMed:11555828, CC PubMed:12865317). Metabolizes cholesterol toward 25-hydroxycholesterol, CC a physiological regulator of cellular cholesterol homeostasis CC (PubMed:21576599). May act as a major enzyme for all-trans retinoic CC acid biosynthesis in the liver. Catalyzes two successive oxidative CC transformation of all-trans retinol to all-trans retinal and then to CC the active form all-trans retinoic acid (PubMed:10681376). Primarily CC catalyzes stereoselective epoxidation of the last double bond of CC polyunsaturated fatty acids (PUFA), displaying a strong preference for CC the (R,S) stereoisomer (PubMed:19965576). Catalyzes bisallylic CC hydroxylation and omega-1 hydroxylation of PUFA (PubMed:9435160). May CC also participate in eicosanoids metabolism by converting hydroperoxide CC species into oxo metabolites (lipoxygenase-like reaction, NADPH- CC independent) (PubMed:21068195). Plays a role in the oxidative CC metabolism of xenobiotics. Catalyzes the N-hydroxylation of CC heterocyclic amines and the O-deethylation of phenacetin CC (PubMed:14725854). Metabolizes caffeine via N3-demethylation CC (Probable). {ECO:0000269|PubMed:10681376, ECO:0000269|PubMed:11555828, CC ECO:0000269|PubMed:12865317, ECO:0000269|PubMed:14725854, CC ECO:0000269|PubMed:19965576, ECO:0000269|PubMed:21068195, CC ECO:0000269|PubMed:21576599, ECO:0000269|PubMed:9435160, CC ECO:0000305|PubMed:16522833}. 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:11555828, ECO:0000269|PubMed:12865317, CC ECO:0000269|PubMed:9435160}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17150; CC Evidence={ECO:0000305|PubMed:11555828, ECO:0000305|PubMed:12865317, CC ECO:0000305|PubMed:9435160}; 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47213; CC Evidence={ECO:0000305|PubMed:11555828, ECO:0000305|PubMed:12865317}; 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:11555828, ECO:0000269|PubMed:12865317}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47281; CC Evidence={ECO:0000305|PubMed:11555828, ECO:0000305|PubMed:12865317}; 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47209; CC Evidence={ECO:0000305|PubMed:12865317}; 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47293; CC Evidence={ECO:0000305|PubMed:12865317}; CC -!- CATALYTIC ACTIVITY: CC Reaction=cholesterol + O2 + reduced [NADPH--hemoprotein reductase] = CC 25-hydroxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein CC reductase]; Xref=Rhea:RHEA:50256, Rhea:RHEA-COMP:11964, Rhea:RHEA- CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16113, ChEBI:CHEBI:42977, ChEBI:CHEBI:57618, CC ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:21576599}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50257; CC Evidence={ECO:0000305|PubMed:21576599}; 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=(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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49861; CC Evidence={ECO:0000305|PubMed:19965576}; 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,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:19965576}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39780; 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=(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 -!- 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=(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=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced CC [NADPH--hemoprotein reductase] = 13-hydroxy-(5Z,8Z,11Z,14Z)- CC eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein CC reductase]; Xref=Rhea:RHEA:52292, Rhea:RHEA-COMP:11964, Rhea:RHEA- CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, CC ChEBI:CHEBI:136524; Evidence={ECO:0000269|PubMed:9435160}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52293; CC Evidence={ECO:0000305|PubMed:9435160}; 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:9435160}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39760; CC Evidence={ECO:0000305|PubMed:9435160}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(9Z,12Z)-octadecadienoate + O2 + reduced [NADPH--hemoprotein CC reductase] = 11-hydroxy-(9Z,12Z)-octadecadienoate + H(+) + H2O + CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:52284, CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:136522; CC Evidence={ECO:0000269|PubMed:9435160}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52285; CC Evidence={ECO:0000305|PubMed:9435160}; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=19 uM for 17beta-estradiol (2-hydroxylation) CC {ECO:0000269|PubMed:11555828}; CC KM=9 uM for all-trans retinol {ECO:0000269|PubMed:10681376}; CC KM=4 uM for 2-amino-6-methyldipyrido[1,2-a:3',2'-d]imidazole CC {ECO:0000269|PubMed:14725854}; CC KM=21 uM for 2-amino-3-methylimidazo[4,5-f]quinoline CC {ECO:0000269|PubMed:14725854}; CC KM=26 uM for 2-amino-2,4-dimethylimidazo[4,5-f]quinoline CC {ECO:0000269|PubMed:14725854}; CC KM=27 uM for 2-amino-3,8-dimethylimidazo[4,5-f]quinoxaline CC {ECO:0000269|PubMed:14725854}; CC KM=71 uM for 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine CC {ECO:0000269|PubMed:14725854}; CC KM=25 uM for phenacetin {ECO:0000269|PubMed:14725854}; CC Vmax=9.2 nmol/min/nmol enzyme toward 17beta-estradiol CC (2-hydroxylation) {ECO:0000269|PubMed:11555828}; CC Vmax=491 pmol/min/nmol enzyme toward all-trans retinol CC {ECO:0000269|PubMed:10681376}; CC -!- PATHWAY: Cofactor metabolism; retinol metabolism. CC {ECO:0000269|PubMed:10681376}. CC -!- PATHWAY: Steroid metabolism; cholesterol metabolism. CC {ECO:0000269|PubMed:21576599}. CC -!- PATHWAY: Lipid metabolism; arachidonate metabolism. CC {ECO:0000269|PubMed:19965576, ECO:0000269|PubMed:21068195, CC ECO:0000269|PubMed:9435160}. CC -!- SUBUNIT: Interacts with PGRMC1; the interaction requires PGRMC1 CC homodimerization. {ECO:0000269|PubMed:26988023}. CC -!- INTERACTION: CC P05177; O95870: ABHD16A; NbExp=3; IntAct=EBI-17183330, EBI-348517; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral CC membrane protein. Microsome membrane {ECO:0000269|PubMed:21576599}; CC Peripheral membrane protein. CC -!- TISSUE SPECIFICITY: Liver. CC -!- INDUCTION: By nicotine, omeprazole, phenobarbital, primidone and CC rifampicin. CC -!- POLYMORPHISM: The CYP1A2*1F allele which is quite common (40 to 50%) is CC due to a substitution of a base in the non-coding region of the CYP1A2 CC gene and has the effect of decreasing the enzyme inducibility. CC Individuals who are homozygous for the CYP1A2*1F allele are 'slow' CC caffeine metabolizers. Thus for these individual increased intake of CC caffeine seems to be associated with a concomitant increase in the risk CC of non-fatal myocardial infraction (MI). {ECO:0000305|PubMed:16522833}. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=PharmVar Pharmacogen Variation Consortium; CC Note=CYP1A2 alleles; CC URL="https://www.pharmvar.org/gene/CYP1A2"; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/cyp1a2/"; 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; Z00036; CAA77335.1; -; mRNA. DR EMBL; M55053; AAA52146.1; -; mRNA. DR EMBL; M12078; AAA52154.1; -; mRNA. DR EMBL; L00389; AAA35738.1; -; Genomic_DNA. DR EMBL; L00384; AAA35738.1; JOINED; Genomic_DNA. DR EMBL; L00385; AAA35738.1; JOINED; Genomic_DNA. DR EMBL; L00386; AAA35738.1; JOINED; Genomic_DNA. DR EMBL; L00388; AAA35738.1; JOINED; Genomic_DNA. DR EMBL; L00387; AAA35738.1; JOINED; Genomic_DNA. DR EMBL; M31667; AAA52163.1; -; Genomic_DNA. DR EMBL; M31664; AAA52163.1; JOINED; Genomic_DNA. DR EMBL; M31665; AAA52163.1; JOINED; Genomic_DNA. DR EMBL; M31666; AAA52163.1; JOINED; Genomic_DNA. DR EMBL; AF182274; AAF13599.1; -; mRNA. DR EMBL; AF253322; AAK25728.1; -; Genomic_DNA. DR EMBL; DQ022432; AAY26399.1; -; Genomic_DNA. DR EMBL; BC067424; AAH67424.1; -; mRNA. DR EMBL; BC067425; AAH67425.1; -; mRNA. DR EMBL; BC067426; AAH67426.1; -; mRNA. DR EMBL; BC067427; AAH67427.1; -; mRNA. DR EMBL; BC067428; AAH67428.1; -; mRNA. DR EMBL; BC067429; AAH67429.1; -; mRNA. DR CCDS; CCDS32293.1; -. DR PIR; S16718; O4HU4. DR RefSeq; NP_000752.2; NM_000761.4. DR PDB; 2HI4; X-ray; 1.95 A; A=27-516. DR PDBsum; 2HI4; -. DR AlphaFoldDB; P05177; -. DR SMR; P05177; -. DR BioGRID; 107924; 11. DR IntAct; P05177; 7. DR STRING; 9606.ENSP00000342007; -. DR BindingDB; P05177; -. DR ChEMBL; CHEMBL3356; -. DR DrugBank; DB08496; (R)-warfarin. DR DrugBank; DB01667; 8-azaguanine. DR DrugBank; DB14132; 8-chlorotheophylline. DR DrugBank; DB04356; 9-Deazaguanine. DR DrugBank; DB02489; 9-Methylguanine. DR DrugBank; DB11932; Abametapir. DR DrugBank; DB12001; Abemaciclib. DR DrugBank; DB05812; Abiraterone. DR DrugBank; DB13573; Acefylline. DR DrugBank; DB01418; Acenocoumarol. DR DrugBank; DB00316; Acetaminophen. DR DrugBank; DB15568; Adagrasib. DR DrugBank; DB06594; Agomelatine. DR DrugBank; DB00518; Albendazole. DR DrugBank; DB05396; Albinterferon Alfa-2B. DR DrugBank; DB00969; Alosetron. DR DrugBank; DB07453; alpha-Naphthoflavone. DR DrugBank; DB01424; Aminophenazone. DR DrugBank; DB01223; Aminophylline. DR DrugBank; DB01118; Amiodarone. DR DrugBank; DB00321; Amitriptyline. DR DrugBank; DB00261; Anagrelide. DR DrugBank; DB01217; Anastrozole. DR DrugBank; DB01435; Antipyrine. DR DrugBank; DB06605; Apixaban. DR DrugBank; DB05676; Apremilast. DR DrugBank; DB06413; Armodafinil. DR DrugBank; DB06216; Asenapine. DR DrugBank; DB01072; Atazanavir. DR DrugBank; DB15011; Avacopan. DR DrugBank; DB06442; Avasimibe. DR DrugBank; DB06626; Axitinib. DR DrugBank; DB00993; Azathioprine. DR DrugBank; DB00972; Azelastine. DR DrugBank; DB13203; Bamifylline. DR DrugBank; DB05015; Belinostat. DR DrugBank; DB16703; Belumosudil. DR DrugBank; DB06769; Bendamustine. DR DrugBank; DB01086; Benzocaine. DR DrugBank; DB06770; Benzyl alcohol. DR DrugBank; DB06771; Besifloxacin. DR DrugBank; DB06732; beta-Naphthoflavone. DR DrugBank; DB00195; Betaxolol. DR DrugBank; DB04889; Bicifadine. DR DrugBank; DB11967; Binimetinib. DR DrugBank; DB13975; Black cohosh. DR DrugBank; DB00188; Bortezomib. DR DrugBank; DB12151; Brincidofovir. DR DrugBank; DB01558; Bromazepam. DR DrugBank; DB14018; Bromotheophylline. DR DrugBank; DB13812; Bufylline. DR DrugBank; DB00201; Caffeine. DR DrugBank; DB09061; Cannabidiol. DR DrugBank; DB14737; Cannabinol. DR DrugBank; DB11791; Capmatinib. DR DrugBank; DB06774; Capsaicin. DR DrugBank; DB00564; Carbamazepine. DR DrugBank; DB06016; Cariprazine. DR DrugBank; DB01136; Carvedilol. DR DrugBank; DB12814; Cepeginterferon alfa-2B. DR DrugBank; DB00477; Chlorpromazine. DR DrugBank; DB00356; Chlorzoxazone. DR DrugBank; DB01166; Cilostazol. DR DrugBank; DB00501; Cimetidine. DR DrugBank; DB01012; Cinacalcet. DR DrugBank; DB00568; Cinnarizine. DR DrugBank; DB00827; Cinoxacin. DR DrugBank; DB00537; Ciprofloxacin. DR DrugBank; DB00215; Citalopram. DR DrugBank; DB12499; Clascoterone. DR DrugBank; DB14025; Clinafloxacin. DR DrugBank; DB01242; Clomipramine. DR DrugBank; DB00575; Clonidine. DR DrugBank; DB00758; Clopidogrel. DR DrugBank; DB00363; Clozapine. DR DrugBank; DB00286; Conjugated estrogens. DR DrugBank; DB11672; Curcumin. DR DrugBank; DB14635; Curcumin sulfate. DR DrugBank; DB00924; Cyclobenzaprine. DR DrugBank; DB08912; Dabrafenib. DR DrugBank; DB00851; Dacarbazine. DR DrugBank; DB06292; Dapagliflozin. DR DrugBank; DB01254; Dasatinib. DR DrugBank; DB01609; Deferasirox. DR DrugBank; DB01151; Desipramine. DR DrugBank; DB16650; Deucravacitinib. DR DrugBank; DB12161; Deutetrabenazine. DR DrugBank; DB01191; Dexfenfluramine. DR DrugBank; DB00633; Dexmedetomidine. DR DrugBank; DB11994; Diacerein. DR DrugBank; DB00586; Diclofenac. DR DrugBank; DB11511; Difloxacin. DR DrugBank; DB12945; Dihydralazine. DR DrugBank; DB00280; Disopyramide. DR DrugBank; DB01184; Domperidone. DR DrugBank; DB09167; Dosulepin. DR DrugBank; DB05928; Dovitinib. DR DrugBank; DB01142; Doxepin. DR DrugBank; DB09273; Doxofylline. DR DrugBank; DB00470; Dronabinol. DR DrugBank; DB00476; Duloxetine. DR DrugBank; DB00625; Efavirenz. DR DrugBank; DB15444; Elexacaftor. DR DrugBank; DB06210; Eltrombopag. DR DrugBank; DB13874; Enasidenib. DR DrugBank; DB00467; Enoxacin. DR DrugBank; DB11404; Enrofloxacin. 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; DB04574; Estrone sulfate. DR DrugBank; DB13592; Etamiphylline. DR DrugBank; DB00330; Ethambutol. DR DrugBank; DB00898; Ethanol. DR DrugBank; DB00977; Ethinylestradiol. DR DrugBank; DB00773; Etoposide. DR DrugBank; DB01628; Etoricoxib. DR DrugBank; DB00927; Famotidine. DR DrugBank; DB04854; Febuxostat. DR DrugBank; DB01482; Fenethylline. DR DrugBank; DB00574; Fenfluramine. DR DrugBank; DB12265; Fexinidazole. DR DrugBank; DB01195; Flecainide. DR DrugBank; DB08972; Flumequine. DR DrugBank; DB04841; Flunarizine. DR DrugBank; DB00544; Fluorouracil. DR DrugBank; DB00472; Fluoxetine. DR DrugBank; DB00499; Flutamide. DR DrugBank; DB00176; Fluvoxamine. DR DrugBank; DB01320; Fosphenytoin. DR DrugBank; DB00998; Frovatriptan. DR DrugBank; DB14029; Furafylline. DR DrugBank; DB06160; Garenoxacin. DR DrugBank; DB01044; Gatifloxacin. DR DrugBank; DB01241; Gemfibrozil. DR DrugBank; DB01155; Gemifloxacin. DR DrugBank; DB01645; Genistein. DR DrugBank; DB01381; Ginkgo biloba. DR DrugBank; DB00986; Glycopyrronium. DR DrugBank; DB00365; Grepafloxacin. DR DrugBank; DB00400; Griseofulvin. DR DrugBank; DB05708; GTS-21. DR DrugBank; DB00629; Guanabenz. DR DrugBank; DB00502; Haloperidol. DR DrugBank; DB01094; Hesperetin. DR DrugBank; DB14999; Human interferon beta. DR DrugBank; DB04076; Hypoxanthine. DR DrugBank; DB11737; Icotinib. DR DrugBank; DB00619; Imatinib. DR DrugBank; DB00458; Imipramine. DR DrugBank; DB11564; Insulin argine. DR DrugBank; DB01306; Insulin aspart. DR DrugBank; DB09456; Insulin beef. DR DrugBank; DB09564; Insulin degludec. DR DrugBank; DB01307; Insulin detemir. DR DrugBank; DB00047; Insulin glargine. DR DrugBank; DB01309; Insulin glulisine. DR DrugBank; DB00030; Insulin human. DR DrugBank; DB00046; Insulin lispro. DR DrugBank; DB11567; Insulin peglispro. DR DrugBank; DB00071; Insulin pork. DR DrugBank; DB11568; Insulin tregopil. DR DrugBank; DB05258; Interferon alfa. DR DrugBank; DB00034; Interferon alfa-2a. DR DrugBank; DB00105; Interferon alfa-2b. DR DrugBank; DB15131; Interferon alfa-2c. DR DrugBank; DB00011; Interferon alfa-n1. DR DrugBank; DB00018; Interferon alfa-n3. DR DrugBank; DB00069; Interferon alfacon-1. DR DrugBank; DB00060; Interferon beta-1a. DR DrugBank; DB00068; Interferon beta-1b. DR DrugBank; DB00033; Interferon gamma-1b. DR DrugBank; DB00951; Isoniazid. DR DrugBank; DB11757; Istradefylline. DR DrugBank; DB09570; Ixazomib. DR DrugBank; DB01026; Ketoconazole. DR DrugBank; DB01097; Leflunomide. DR DrugBank; DB09078; Lenvatinib. DR DrugBank; DB01002; Levobupivacaine. DR DrugBank; DB05667; Levoketoconazole. DR DrugBank; DB00281; Lidocaine. DR DrugBank; DB12406; Lisofylline. DR DrugBank; DB09198; Lobeglitazone. DR DrugBank; DB04948; Lofexidine. DR DrugBank; DB00978; Lomefloxacin. DR DrugBank; DB06448; Lonafarnib. DR DrugBank; DB16220; Lonapegsomatropin. DR DrugBank; DB01601; Lopinavir. DR DrugBank; DB00455; Loratadine. DR DrugBank; DB04871; Lorcaserin. DR DrugBank; DB06077; Lumateperone. DR DrugBank; DB01283; Lumiracoxib. DR DrugBank; DB00772; Malathion. DR DrugBank; DB00934; Maprotiline. DR DrugBank; DB06234; Maribavir. DR DrugBank; DB14009; Medical Cannabis. DR DrugBank; DB00784; Mefenamic acid. DR DrugBank; DB01065; Melatonin. DR DrugBank; DB00170; Menadione. DR DrugBank; DB00454; Meperidine. DR DrugBank; DB00532; Mephenytoin. DR DrugBank; DB00333; Methadone. DR DrugBank; DB00763; Methimazole. DR DrugBank; DB00553; Methoxsalen. DR DrugBank; DB01028; Methoxyflurane. DR DrugBank; DB09241; Methylene blue. DR DrugBank; DB01233; Metoclopramide. DR DrugBank; DB00379; Mexiletine. DR DrugBank; DB06148; Mianserin. DR DrugBank; DB01388; Mibefradil. DR DrugBank; DB06595; Midostaurin. DR DrugBank; DB00370; Mirtazapine. DR DrugBank; DB16236; Mitapivat. DR DrugBank; DB00745; Modafinil. DR DrugBank; DB00218; Moxifloxacin. DR DrugBank; DB06510; Muraglitazar. DR DrugBank; DB14011; Nabiximols. DR DrugBank; DB00461; Nabumetone. DR DrugBank; DB00607; Nafcillin. DR DrugBank; DB00779; Nalidixic acid. DR DrugBank; DB00788; Naproxen. DR DrugBank; DB06600; Nemonoxacin. DR DrugBank; DB00238; Nevirapine. DR DrugBank; DB06803; Niclosamide. DR DrugBank; DB00184; Nicotine. DR DrugBank; DB01115; Nifedipine. DR DrugBank; DB11793; Niraparib. DR DrugBank; DB00435; Nitric Oxide. DR DrugBank; DB05115; NN344. DR DrugBank; DB00717; Norethisterone. DR DrugBank; DB01059; Norfloxacin. DR DrugBank; DB00540; Nortriptyline. DR DrugBank; DB05990; Obeticholic acid. DR DrugBank; DB01165; Ofloxacin. DR DrugBank; DB00334; Olanzapine. DR DrugBank; DB16267; Olutasidenib. DR DrugBank; DB00338; Omeprazole. DR DrugBank; DB00904; Ondansetron. DR DrugBank; DB11632; Opicapone. DR DrugBank; DB11443; Orbifloxacin. DR DrugBank; DB01173; Orphenadrine. DR DrugBank; DB11837; Osilodrostat. DR DrugBank; DB09330; Osimertinib. DR DrugBank; DB01303; Oxtriphylline. DR DrugBank; DB11697; Pacritinib. DR DrugBank; DB00377; Palonosetron. DR DrugBank; DB00715; Paroxetine. DR DrugBank; DB06589; Pazopanib. DR DrugBank; DB11774; Pazufloxacin. DR DrugBank; DB00487; Pefloxacin. DR DrugBank; DB00008; Peginterferon alfa-2a. DR DrugBank; DB00022; Peginterferon alfa-2b. DR DrugBank; DB09122; Peginterferon beta-1a. DR DrugBank; DB13634; Pentifylline. DR DrugBank; DB00806; Pentoxifylline. DR DrugBank; DB11198; Peppermint oil. DR DrugBank; DB08883; Perampanel. DR DrugBank; DB00850; Perphenazine. DR DrugBank; DB03783; Phenacetin. DR DrugBank; DB01174; Phenobarbital. DR DrugBank; DB00388; Phenylephrine. DR DrugBank; DB00252; Phenytoin. DR DrugBank; DB11450; Pimobendan. DR DrugBank; DB01100; Pimozide. DR DrugBank; DB13823; Pipemidic acid. DR DrugBank; DB04951; Pirfenidone. DR DrugBank; DB11642; Pitolisant. DR DrugBank; DB08910; Pomalidomide. DR DrugBank; DB15822; Pralsetinib. DR DrugBank; DB01058; Praziquantel. DR DrugBank; DB01087; Primaquine. DR DrugBank; DB00794; Primidone. DR DrugBank; DB00420; Promazine. DR DrugBank; DB09288; Propacetamol. DR DrugBank; DB01182; Propafenone. DR DrugBank; DB06479; Propentofylline. DR DrugBank; DB00818; Propofol. DR DrugBank; DB00571; Propranolol. DR DrugBank; DB13449; Proxyphylline. DR DrugBank; DB11892; Prulifloxacin. DR DrugBank; DB04216; Quercetin. DR DrugBank; DB00908; Quinidine. DR DrugBank; DB00468; Quinine. DR DrugBank; DB01129; Rabeprazole. DR DrugBank; DB00980; Ramelteon. DR DrugBank; DB09290; Ramosetron. DR DrugBank; DB00863; Ranitidine. DR DrugBank; DB01367; Rasagiline. DR DrugBank; DB00409; Remoxipride. DR DrugBank; DB02709; Resveratrol. DR DrugBank; DB13174; Rhein. DR DrugBank; DB01045; Rifampicin. DR DrugBank; DB11753; Rifamycin. DR DrugBank; DB00740; Riluzole. DR DrugBank; DB00503; Ritonavir. DR DrugBank; DB00533; Rofecoxib. DR DrugBank; DB01656; Roflumilast. DR DrugBank; DB15119; Ropeginterferon alfa-2b. DR DrugBank; DB00268; Ropinirole. DR DrugBank; DB00296; Ropivacaine. DR DrugBank; DB00412; Rosiglitazone. DR DrugBank; DB00817; Rosoxacin. DR DrugBank; DB12332; Rucaparib. DR DrugBank; DB13772; Rufloxacin. DR DrugBank; DB06654; Safinamide. DR DrugBank; DB11491; Sarafloxacin. DR DrugBank; DB00418; Secobarbital. DR DrugBank; DB01037; Selegiline. DR DrugBank; DB11689; Selumetinib. DR DrugBank; DB06290; Simeprevir. DR DrugBank; DB13261; Sitafloxacin. DR DrugBank; DB15093; Somapacitan. DR DrugBank; DB00052; Somatotropin. DR DrugBank; DB00398; Sorafenib. DR DrugBank; DB01208; Sparfloxacin. DR DrugBank; DB09118; Stiripentol. DR DrugBank; DB00428; Streptozocin. DR DrugBank; DB06820; Sulconazole. DR DrugBank; DB00382; Tacrine. DR DrugBank; DB00675; Tamoxifen. DR DrugBank; DB06083; Tapinarof. DR DrugBank; DB09071; Tasimelteon. DR DrugBank; DB05488; Technetium Tc-99m ciprofloxacin. DR DrugBank; DB09256; Tegafur. DR DrugBank; DB01079; Tegaserod. DR DrugBank; DB01405; Temafloxacin. DR DrugBank; DB00857; Terbinafine. DR DrugBank; DB08880; Teriflunomide. DR DrugBank; DB01412; Theobromine. DR DrugBank; DB00277; Theophylline. DR DrugBank; DB00730; Thiabendazole. DR DrugBank; DB01623; Thiothixene. DR DrugBank; DB00208; Ticlopidine. DR DrugBank; DB06137; Tirbanibulin. DR DrugBank; DB00697; Tizanidine. DR DrugBank; DB01056; Tocainide. DR DrugBank; DB06264; Tolperisone. DR DrugBank; DB00752; Tranylcypromine. DR DrugBank; DB00384; Triamterene. DR DrugBank; DB12245; Triclabendazole. DR DrugBank; DB00831; Trifluoperazine. DR DrugBank; DB15442; Trilaciclib. DR DrugBank; DB00440; Trimethoprim. DR DrugBank; DB00685; Trovafloxacin. DR DrugBank; DB08867; Ulipristal. DR DrugBank; DB14989; Umbralisib. DR DrugBank; DB13609; Umifenovir. DR DrugBank; DB06235; Vadimezan. DR DrugBank; DB00313; Valproic acid. DR DrugBank; DB08881; Vemurafenib. DR DrugBank; DB00661; Verapamil. DR DrugBank; DB09185; Viloxazine. DR DrugBank; DB12026; Voxilaprevir. DR DrugBank; DB00682; Warfarin. DR DrugBank; DB02134; Xanthine. DR DrugBank; DB00549; Zafirlukast. DR DrugBank; DB00744; Zileuton. DR DrugBank; DB00315; Zolmitriptan. DR DrugBank; DB00425; Zolpidem. DR DrugBank; DB09225; Zotepine. DR DrugBank; DB09120; Zucapsaicin. DR DrugCentral; P05177; -. DR GuidetoPHARMACOLOGY; 1319; -. DR SwissLipids; SLP:000001202; -. DR GlyCosmos; P05177; 1 site, No reported glycans. DR GlyGen; P05177; 1 site. DR iPTMnet; P05177; -. DR PhosphoSitePlus; P05177; -. DR BioMuta; CYP1A2; -. DR DMDM; 117144; -. DR MassIVE; P05177; -. DR MaxQB; P05177; -. DR PaxDb; 9606-ENSP00000342007; -. DR PeptideAtlas; P05177; -. DR Antibodypedia; 4221; 873 antibodies from 38 providers. DR DNASU; 1544; -. DR Ensembl; ENST00000343932.5; ENSP00000342007.4; ENSG00000140505.7. DR GeneID; 1544; -. DR KEGG; hsa:1544; -. DR MANE-Select; ENST00000343932.5; ENSP00000342007.4; NM_000761.5; NP_000752.2. DR UCSC; uc002ayr.2; human. DR AGR; HGNC:2596; -. DR CTD; 1544; -. DR DisGeNET; 1544; -. DR GeneCards; CYP1A2; -. DR HGNC; HGNC:2596; CYP1A2. DR HPA; ENSG00000140505; Tissue enriched (liver). DR MIM; 108330; gene. DR MIM; 124060; gene+phenotype. DR neXtProt; NX_P05177; -. DR OpenTargets; ENSG00000140505; -. DR PharmGKB; PA27093; -. DR VEuPathDB; HostDB:ENSG00000140505; -. DR eggNOG; KOG0156; Eukaryota. DR GeneTree; ENSGT00950000183037; -. DR HOGENOM; CLU_001570_22_0_1; -. DR InParanoid; P05177; -. DR OMA; AKWEIFL; -. DR OrthoDB; 2900138at2759; -. DR PhylomeDB; P05177; -. DR TreeFam; TF105095; -. DR BioCyc; MetaCyc:HS06728-MONOMER; -. DR BRENDA; 1.14.14.1; 2681. DR BRENDA; 1.14.99.38; 2681. DR PathwayCommons; P05177; -. DR Reactome; R-HSA-156581; Methylation. DR Reactome; R-HSA-211957; Aromatic amines can be N-hydroxylated or N-dealkylated by CYP1A2. 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-5423646; Aflatoxin activation and detoxification. DR Reactome; R-HSA-9018681; Biosynthesis of protectins. DR Reactome; R-HSA-9027307; Biosynthesis of maresin-like SPMs. DR SABIO-RK; P05177; -. DR SignaLink; P05177; -. DR UniPathway; UPA00296; -. DR UniPathway; UPA00383; -. DR UniPathway; UPA00912; -. DR BioGRID-ORCS; 1544; 14 hits in 1148 CRISPR screens. DR EvolutionaryTrace; P05177; -. DR GeneWiki; CYP1A2; -. DR GenomeRNAi; 1544; -. DR Pharos; P05177; Tchem. DR PRO; PR:P05177; -. DR Proteomes; UP000005640; Chromosome 15. DR RNAct; P05177; Protein. DR Bgee; ENSG00000140505; Expressed in buccal mucosa cell and 97 other cell types or tissues. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0034875; F:caffeine oxidase activity; IDA:BHF-UCL. DR GO; GO:0032451; F:demethylase activity; IDA:UniProtKB. DR GO; GO:0009055; F:electron transfer activity; TAS:UniProtKB. DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL. 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:0020037; F:heme binding; IDA:UniProtKB. DR GO; GO:0106256; F:hydroperoxy icosatetraenoate dehydratase activity; IEA:UniProtKB-EC. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0004497; F:monooxygenase activity; IDA:BHF-UCL. DR GO; GO:0016491; F:oxidoreductase activity; IDA:BHF-UCL. DR GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IMP:UniProtKB. DR GO; GO:0046222; P:aflatoxin metabolic process; TAS:Reactome. DR GO; GO:0009820; P:alkaloid metabolic process; IDA:BHF-UCL. DR GO; GO:0045333; P:cellular respiration; IEA:Ensembl. DR GO; GO:0071276; P:cellular response to cadmium ion; IEA:Ensembl. DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0018894; P:dibenzo-p-dioxin metabolic process; 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:0046483; P:heterocycle metabolic process; IDA:BHF-UCL. DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IEA:Ensembl. DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; TAS:Reactome. DR GO; GO:0030324; P:lung development; IEA:Ensembl. DR GO; GO:0032259; P:methylation; TAS:Reactome. DR GO; GO:0032787; P:monocarboxylic acid metabolic process; IDA:BHF-UCL. DR GO; GO:0016098; P:monoterpenoid metabolic process; IDA:BHF-UCL. DR GO; GO:0097267; P:omega-hydroxylase P450 pathway; TAS:Reactome. DR GO; GO:0070989; P:oxidative demethylation; IDA:BHF-UCL. DR GO; GO:0006778; P:porphyrin-containing compound metabolic process; IEA:Ensembl. DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl. DR GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl. DR GO; GO:0042572; P:retinol metabolic process; IDA:UniProtKB. DR GO; GO:0006706; P:steroid catabolic process; IMP:BHF-UCL. DR GO; GO:0009403; P:toxin biosynthetic process; IDA:BHF-UCL. DR GO; GO:0042178; P:xenobiotic catabolic process; IDA: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; P05177; HS. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Endoplasmic reticulum; KW Fatty acid metabolism; Glycoprotein; Heme; Iron; Lipid metabolism; Lyase; KW Membrane; Metal-binding; Microsome; Monooxygenase; Oxidoreductase; KW Reference proteome; Steroid metabolism; Sterol metabolism. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:3517618" FT CHAIN 2..516 FT /note="Cytochrome P450 1A2" FT /id="PRO_0000051651" FT BINDING 226 FT /ligand="substrate" FT /evidence="ECO:0000305" FT BINDING 458 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT CARBOHYD 69 FT /note="O-linked (GlcNAc) serine" FT /evidence="ECO:0000250" FT VARIANT 18 FT /note="S -> C (in dbSNP:rs17861152)" FT /evidence="ECO:0000269|PubMed:15469410, FT ECO:0000269|PubMed:15643613" FT /id="VAR_023196" FT VARIANT 21 FT /note="F -> L (in allele CYP1A2*2; dbSNP:rs56160784)" FT /evidence="ECO:0000269|PubMed:9884316" FT /id="VAR_008349" FT VARIANT 42 FT /note="P -> R (in allele CYP1A2*15; dbSNP:rs72547511)" FT /evidence="ECO:0000269|PubMed:15770072" FT /id="VAR_025182" FT VARIANT 73 FT /note="G -> R (in dbSNP:rs45565238)" FT /evidence="ECO:0000269|Ref.7" FT /id="VAR_025183" FT VARIANT 83 FT /note="T -> M (in allele CYP1A2*9; dbSNP:rs138652540)" FT /evidence="ECO:0000269|PubMed:14563787" FT /id="VAR_020848" FT VARIANT 104 FT /note="D -> N (in dbSNP:rs34067076)" FT /evidence="ECO:0000269|Ref.7" FT /id="VAR_025184" FT VARIANT 111 FT /note="L -> F (in dbSNP:rs45442197)" FT /evidence="ECO:0000269|Ref.7" FT /id="VAR_025185" FT VARIANT 168 FT /note="E -> Q (in allele CYP1A2*10; dbSNP:rs72547512)" FT /evidence="ECO:0000269|PubMed:14563787" FT /id="VAR_020849" FT VARIANT 186 FT /note="F -> L (in allele CYP1A2*11; drastic reduction in FT O-deethylation of phenacetin and 7-ethoxyresorufin; has a FT Vmax of approximately 5% of that of the wild-type and FT 5-fold lower Km value; dbSNP:rs72547513)" FT /evidence="ECO:0000269|PubMed:14563787" FT /id="VAR_020850" FT VARIANT 205 FT /note="F -> V (in dbSNP:rs45540640)" FT /evidence="ECO:0000269|Ref.7" FT /id="VAR_025186" FT VARIANT 212 FT /note="S -> C (in allele CYP1A2*12; dbSNP:rs758748797)" FT /evidence="ECO:0000269|PubMed:14563787" FT /id="VAR_020851" FT VARIANT 281 FT /note="R -> W (in dbSNP:rs45468096)" FT /evidence="ECO:0000269|Ref.7" FT /id="VAR_025187" FT VARIANT 298 FT /note="S -> R (in dbSNP:rs17861157)" FT /evidence="ECO:0000269|PubMed:15469410" FT /id="VAR_024709" FT VARIANT 299 FT /note="G -> S (in allele CYP1A2*13; dbSNP:rs35796837)" FT /evidence="ECO:0000269|PubMed:14563787" FT /id="VAR_020852" FT VARIANT 314 FT /note="I -> V (in dbSNP:rs28399418)" FT /evidence="ECO:0000269|PubMed:15469410, ECO:0000269|Ref.5" FT /id="VAR_024710" FT VARIANT 348 FT /note="D -> N (in allele CYP1A2*3; increases FT N-hydroxylation activity of heterocyclic amines; reduces FT phenacetin O-deethylation activity; dbSNP:rs56276455)" FT /evidence="ECO:0000269|PubMed:11295848, FT ECO:0000269|PubMed:14725854" FT /id="VAR_020793" FT VARIANT 377 FT /note="R -> Q (in allele CYP1A2*16; dbSNP:rs72547515)" FT /evidence="ECO:0000269|PubMed:15770072" FT /id="VAR_025188" FT VARIANT 386 FT /note="I -> F (in allele CYP1A2*4; increases catalytic FT efficiency of N-hydroxylation towards some heterocyclic FT amines and reduces towards others; reduces catalytic FT efficiency of phenacetin O-deethylation due to a high FT decrease in the affinity for phenacetin; dbSNP:rs72547516)" FT /evidence="ECO:0000269|PubMed:11295848, FT ECO:0000269|PubMed:14725854" FT /id="VAR_020794" FT VARIANT 406 FT /note="C -> Y (in allele CYP1A2*5; increases FT N-hydroxylation activity of heterocyclic amines; reduces FT catalytic efficiency of phenacetin O-deethylation; FT dbSNP:rs55889066)" FT /evidence="ECO:0000269|PubMed:11295848, FT ECO:0000269|PubMed:14725854" FT /id="VAR_020795" FT VARIANT 431 FT /note="R -> W (in allele CYP1A2*6; not detected when FT expressed in heterologous system as it may be critical for FT maintenance of protein tertiary structure; FT dbSNP:rs28399424)" FT /evidence="ECO:0000269|PubMed:11295848, FT ECO:0000269|PubMed:14725854, ECO:0000269|PubMed:15469410" FT /id="VAR_020796" FT VARIANT 438 FT /note="T -> I (in allele CYP1A2*14; dbSNP:rs45486893)" FT /evidence="ECO:0000269|PubMed:14563787, ECO:0000269|Ref.7" FT /id="VAR_020853" FT VARIANT 456 FT /note="R -> H (in allele CYP1A2*8; dbSNP:rs72547517)" FT /evidence="ECO:0000269|PubMed:15770072" FT /id="VAR_025189" FT VARIANT 457 FT /note="R -> W (in dbSNP:rs34151816)" FT /id="VAR_055563" FT CONFLICT 79 FT /note="R -> S (in Ref. 2; AAA35738)" FT /evidence="ECO:0000305" FT CONFLICT 81 FT /note="G -> D (in Ref. 8; AAH67427)" FT /evidence="ECO:0000305" FT CONFLICT 170 FT /note="K -> M (in Ref. 5; AAF13599)" FT /evidence="ECO:0000305" FT CONFLICT 311 FT /note="V -> L (in Ref. 2; AAA52154)" FT /evidence="ECO:0000305" FT CONFLICT 380 FT /note="S -> P (in Ref. 8; AAH67429)" FT /evidence="ECO:0000305" FT CONFLICT 450..451 FT /note="LF -> MLV (in Ref. 2; AAA52154)" FT /evidence="ECO:0000305" FT CONFLICT 492 FT /note="T -> I (in Ref. 5; AAF13599)" FT /evidence="ECO:0000305" FT CONFLICT 511 FT /note="Missing (in Ref. 1; CAA77335 and 3; FT AAA52146/AAA52163)" FT /evidence="ECO:0000305" FT CONFLICT 512 FT /note="R -> P (in Ref. 2; AAA35738)" FT /evidence="ECO:0000305" FT TURN 49..51 FT /evidence="ECO:0007829|PDB:2HI4" FT HELIX 54..57 FT /evidence="ECO:0007829|PDB:2HI4" FT HELIX 61..72 FT /evidence="ECO:0007829|PDB:2HI4" FT STRAND 74..80 FT /evidence="ECO:0007829|PDB:2HI4" FT STRAND 83..88 FT /evidence="ECO:0007829|PDB:2HI4" FT HELIX 91..98 FT /evidence="ECO:0007829|PDB:2HI4" FT TURN 99..101 FT /evidence="ECO:0007829|PDB:2HI4" FT HELIX 102..104 FT /evidence="ECO:0007829|PDB:2HI4" FT HELIX 112..115 FT /evidence="ECO:0007829|PDB:2HI4" FT TURN 123..125 FT /evidence="ECO:0007829|PDB:2HI4" FT HELIX 131..146 FT /evidence="ECO:0007829|PDB:2HI4" FT TURN 147..149 FT /evidence="ECO:0007829|PDB:2HI4" FT HELIX 160..181 FT /evidence="ECO:0007829|PDB:2HI4" FT HELIX 188..205 FT /evidence="ECO:0007829|PDB:2HI4" FT HELIX 206..208 FT /evidence="ECO:0007829|PDB:2HI4" FT HELIX 214..220 FT /evidence="ECO:0007829|PDB:2HI4" FT HELIX 221..223 FT /evidence="ECO:0007829|PDB:2HI4" FT HELIX 224..227 FT /evidence="ECO:0007829|PDB:2HI4" FT HELIX 235..237 FT /evidence="ECO:0007829|PDB:2HI4" FT HELIX 240..244 FT /evidence="ECO:0007829|PDB:2HI4" FT HELIX 248..273 FT /evidence="ECO:0007829|PDB:2HI4" FT HELIX 283..293 FT /evidence="ECO:0007829|PDB:2HI4" FT HELIX 305..308 FT /evidence="ECO:0007829|PDB:2HI4" FT HELIX 310..335 FT /evidence="ECO:0007829|PDB:2HI4" FT HELIX 337..350 FT /evidence="ECO:0007829|PDB:2HI4" FT TURN 351..353 FT /evidence="ECO:0007829|PDB:2HI4" FT HELIX 359..361 FT /evidence="ECO:0007829|PDB:2HI4" FT HELIX 366..379 FT /evidence="ECO:0007829|PDB:2HI4" FT STRAND 394..396 FT /evidence="ECO:0007829|PDB:2HI4" FT STRAND 399..401 FT /evidence="ECO:0007829|PDB:2HI4" FT STRAND 406..410 FT /evidence="ECO:0007829|PDB:2HI4" FT HELIX 411..416 FT /evidence="ECO:0007829|PDB:2HI4" FT TURN 418..420 FT /evidence="ECO:0007829|PDB:2HI4" FT HELIX 429..432 FT /evidence="ECO:0007829|PDB:2HI4" FT STRAND 437..440 FT /evidence="ECO:0007829|PDB:2HI4" FT HELIX 442..445 FT /evidence="ECO:0007829|PDB:2HI4" FT HELIX 454..456 FT /evidence="ECO:0007829|PDB:2HI4" FT HELIX 461..478 FT /evidence="ECO:0007829|PDB:2HI4" FT STRAND 480..482 FT /evidence="ECO:0007829|PDB:2HI4" FT STRAND 496..498 FT /evidence="ECO:0007829|PDB:2HI4" FT STRAND 507..510 FT /evidence="ECO:0007829|PDB:2HI4" SQ SEQUENCE 516 AA; 58407 MW; 8557AB02860C4806 CRC64; MALSQSVPFS ATELLLASAI FCLVFWVLKG LRPRVPKGLK SPPEPWGWPL LGHVLTLGKN PHLALSRMSQ RYGDVLQIRI GSTPVLVLSR LDTIRQALVR QGDDFKGRPD LYTSTLITDG QSLTFSTDSG PVWAARRRLA QNALNTFSIA SDPASSSSCY LEEHVSKEAK ALISRLQELM AGPGHFDPYN QVVVSVANVI GAMCFGQHFP ESSDEMLSLV KNTHEFVETA SSGNPLDFFP ILRYLPNPAL QRFKAFNQRF LWFLQKTVQE HYQDFDKNSV RDITGALFKH SKKGPRASGN LIPQEKIVNL VNDIFGAGFD TVTTAISWSL MYLVTKPEIQ RKIQKELDTV IGRERRPRLS DRPQLPYLEA FILETFRHSS FLPFTIPHST TRDTTLNGFY IPKKCCVFVN QWQVNHDPEL WEDPSEFRPE RFLTADGTAI NKPLSEKMML FGMGKRRCIG EVLAKWEIFL FLAILLQQLE FSVPPGVKVD LTPIYGLTMK HARCEHVQAR LRFSIN //