CP1A2_HUMAN
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 03-AUG-2022, entry version 219.
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 [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:47212, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16469, ChEBI:CHEBI:28744,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:11555828, ECO:0000269|PubMed:12865317};
CC 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 [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:47280, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16469, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:62845;
CC Evidence={ECO:0000269|PubMed: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 [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:42092, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17336, ChEBI:CHEBI:17898,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:10681376};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42093;
CC Evidence={ECO:0000305|PubMed:10681376};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinal + O2 + reduced [NADPH--hemoprotein
CC reductase] = all-trans-retinoate + 2 H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:42088, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17898, ChEBI:CHEBI:35291,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:10681376};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42089;
CC Evidence={ECO:0000305|PubMed:10681376};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = (14R,15S)-epoxy-(5Z,8Z,11Z)-eicosatrienoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:49860, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:131965; Evidence={ECO:0000269|PubMed:19965576};
CC 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 [NADPH--
CC hemoprotein reductase] = (14S,15R)-epoxy-(5Z,8Z,11Z)-eicosatrienoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:49856, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:131964; Evidence={ECO:0000269|PubMed:19965576};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49857;
CC Evidence={ECO:0000305|PubMed:19965576};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = (17R,18S)-epoxy-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:39779, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:58562,
CC ChEBI:CHEBI:76634; Evidence={ECO:0000269|PubMed: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 [NADPH--
CC hemoprotein reductase] = 13-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:52292, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI: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 [NADPH--
CC hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:39759, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:76627; Evidence={ECO:0000269|PubMed: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 (2-
CC 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 ---------------------------------------------------------------------------
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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; 10.
DR IntAct; P05177; 6.
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; 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; DB11791; Capmatinib.
DR DrugBank; DB06774; Capsaicin.
DR DrugBank; DB00564; Carbamazepine.
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; 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; 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; 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; 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; 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; 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; 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; 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; 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 GlyGen; P05177; 1 site.
DR iPTMnet; P05177; -.
DR PhosphoSitePlus; P05177; -.
DR BioMuta; CYP1A2; -.
DR DMDM; 117144; -.
DR MassIVE; P05177; -.
DR MaxQB; P05177; -.
DR PaxDb; P05177; -.
DR PeptideAtlas; P05177; -.
DR PRIDE; P05177; -.
DR Antibodypedia; 4221; 768 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 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 Orphanet; 284121; Prediction of toxicity or absent response to clozapine.
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; 702827at2759; -.
DR PhylomeDB; P05177; -.
DR TreeFam; TF105095; -.
DR BioCyc; MetaCyc:HS06728-MON; -.
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; 13 hits in 1068 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 tissues.
DR Genevisible; P05177; HS.
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 Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR008066; Cyt_P450_E_grp-I_CYP1.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR01683; EP450ICYP1A.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 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 O-
FT deethylation of phenacetin and 7-ethoxyresorufin; has a
FT Vmax of approximately 5% of that of the wild-type and 5-
FT 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 N-
FT 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 N-
FT 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; AAA52146/
FT 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
