AHR_MOUSE
ID AHR_MOUSE Reviewed; 848 AA.
AC P30561; Q8QZX6; Q8R4S3; Q99P79; Q9QVY1;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 25-MAR-2003, sequence version 3.
DT 25-MAY-2022, entry version 202.
DE RecName: Full=Aryl hydrocarbon receptor;
DE Short=Ah receptor;
DE Short=AhR;
DE Flags: Precursor;
GN Name=Ahr;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND VARIANTS ILE-324; LEU-348;
RP LEU-471; SER-533; LEU-589 AND ALA-758.
RC STRAIN=C57L; TISSUE=Hepatoma;
RX PubMed=1314586; DOI=10.1016/0006-291x(92)91185-s;
RA Ema M., Sogawa K., Watanabe N., Chujoh Y., Matsushita N., Gotoh O.,
RA Funae Y., Fujii-Kuriyama Y.;
RT "cDNA cloning and structure of mouse putative Ah receptor.";
RL Biochem. Biophys. Res. Commun. 184:246-253(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 10-36; 232-261; 335-350 AND
RP 636-646, AND VARIANTS ILE-324; LEU-348; LEU-471; SER-533; LEU-589 AND
RP ALA-758.
RC STRAIN=C57BL/6J, and C57L; TISSUE=Liver;
RX PubMed=1325649; DOI=10.1073/pnas.89.17.8185;
RA Burbach K.M., Poland A., Bradfield C.A.;
RT "Cloning of the Ah-receptor cDNA reveals a distinctive ligand-activated
RT transcription factor.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:8185-8189(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE, AND VARIANTS ILE-324; LEU-348; VAL-375; LEU-471;
RP SER-533; LEU-589 AND ALA-758.
RC STRAIN=C57BL/6J, and DBA/2J;
RX PubMed=8148872; DOI=10.1097/00008571-199312000-00005;
RA Chang C.-Y., Smith D.R., Prasad V.S., Sidman C.L., Nebert D.W., Puga A.;
RT "Ten nucleotide differences, five of which cause amino acid changes, are
RT associated with the Ah receptor locus polymorphism of C57BL/6 and DBA/2
RT mice.";
RL Pharmacogenetics 3:312-321(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=8408082; DOI=10.1016/s0021-9258(20)80668-1;
RA Schmidt J.V., Carver L.A., Bradfield C.A.;
RT "Molecular characterization of the murine Ahr gene. Organization, promoter
RT analysis, and chromosomal assignment.";
RL J. Biol. Chem. 268:22203-22209(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, VARIANTS ILE-324; LEU-348; VAL-375;
RP LEU-471; SER-533; LEU-589 AND ALA-758, AND CHARACTERIZATION OF VARIANTS
RP ILE-324; VAL-375; LEU-471; SER-533 AND LEU-589.
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Liver;
RX PubMed=7961644; DOI=10.1016/s0021-9258(18)46990-6;
RA Ema M., Ohe N., Suzuki M., Mimura J., Sogawa K., Ikawa S.,
RA Fujii-Kuriyama Y.;
RT "Dioxin binding activities of polymorphic forms of mouse and human
RT arylhydrocarbon receptors.";
RL J. Biol. Chem. 269:27337-27343(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE, FUNCTION, VARIANTS ILE-324; LEU-348; VAL-375; LEU-471;
RP SER-533; LEU-589; ALA-758; VAL-808; ASP-821 AND VAL-824, AND
RP CHARACTERIZATION OF VARIANTS LEU-348 AND VAL-375.
RC STRAIN=C57BL/6J;
RX PubMed=7969080;
RA Poland A., Palen D., Glover E.;
RT "Analysis of the four alleles of the murine aryl hydrocarbon receptor.";
RL Mol. Pharmacol. 46:915-921(1994).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-348; VAL-375; ILE-589
RP AND ALA-758.
RC STRAIN=129/SvJ;
RA Hadd A.G., Nguyen L.P., Garrigues C.S., Thomas R.S., Rank D.R., Penn S.G.,
RA LaPres J.J., Roach D., Blaga I., Schneider J., Shilova K., Bradfield C.A.,
RA Jovanovich S.B.;
RT "Mouse aryl-hydrocarbon receptor (AhR) genomic region.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ILE-324; LEU-348; VAL-375;
RP LEU-471; SER-533; ILE-589 AND ALA-758.
RC STRAIN=A/J, BALB/cBY, C3H/HeJ, C57BL/6J, CBA/J, DBA/2J, and SJL/J;
RX PubMed=11875369; DOI=10.1097/00008571-200203000-00009;
RA Thomas R.S., Penn S.G., Holden K., Bradfield C.A., Rank D.R.;
RT "Sequence variation and phylogenetic history of the mouse Ahr gene.";
RL Pharmacogenetics 12:151-163(2002).
RN [9]
RP PROTEIN SEQUENCE OF 10-36.
RX PubMed=1846217;
RA Bradfield C.A., Glover E., Poland A.;
RT "Purification and N-terminal amino acid sequence of the Ah receptor from
RT the C57BL/6J mouse.";
RL Mol. Pharmacol. 39:13-19(1991).
RN [10]
RP INDUCTION.
RX PubMed=8806768; DOI=10.1006/abbi.1996.0378;
RA FitzGerald C.T., Fernandez-Salguero P., Gonzalez F.J., Nebert D.W.,
RA Puga A.;
RT "Differential regulation of mouse Ah receptor gene expression in cell lines
RT of different tissue origins.";
RL Arch. Biochem. Biophys. 333:170-178(1996).
RN [11]
RP FUNCTION.
RX PubMed=8806883; DOI=10.1006/taap.1996.0210;
RA Fernandez-Salguero P.M., Hilbert D.M., Rudikoff S., Ward J.M.,
RA Gonzalez F.J.;
RT "Aryl-hydrocarbon receptor-deficient mice are resistant to 2,3,7,8-
RT tetrachlorodibenzo-p-dioxin-induced toxicity.";
RL Toxicol. Appl. Pharmacol. 140:173-179(1996).
RN [12]
RP FUNCTION.
RX PubMed=9427285; DOI=10.1046/j.1365-2443.1997.1490345.x;
RA Mimura J., Yamashita K., Nakamura K., Morita M., Takagi T.N., Nakao K.,
RA Ema M., Sogawa K., Yasuda M., Katsuki M., Fujii-Kuriyama Y.;
RT "Loss of teratogenic response to 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD)
RT in mice lacking the Ah (dioxin) receptor.";
RL Genes Cells 2:645-654(1997).
RN [13]
RP FUNCTION.
RX PubMed=10973493; DOI=10.1073/pnas.190256997;
RA Lahvis G.P., Lindell S.L., Thomas R.S., McCuskey R.S., Murphy C.,
RA Glover E., Bentz M., Southard J., Bradfield C.A.;
RT "Portosystemic shunting and persistent fetal vascular structures in aryl
RT hydrocarbon receptor-deficient mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:10442-10447(2000).
RN [14]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=10639156; DOI=10.1073/pnas.97.2.779;
RA Shimizu Y., Nakatsuru Y., Ichinose M., Takahashi Y., Kume H., Mimura J.,
RA Fujii-Kuriyama Y., Ishikawa T.;
RT "Benzoapyrene carcinogenicity is lost in mice lacking the aryl hydrocarbon
RT receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:779-782(2000).
RN [15]
RP INTERACTION WITH MYBBP1A.
RX PubMed=11956195; DOI=10.1074/jbc.m200740200;
RA Jones L.C., Okino S.T., Gonda T.J., Whitlock J.P. Jr.;
RT "Myb-binding protein 1a augments AhR-dependent gene expression.";
RL J. Biol. Chem. 277:22515-22519(2002).
RN [16]
RP REVIEW ON ROLE IN CELL CYCLE.
RX PubMed=12213388; DOI=10.1016/s0009-2797(02)00069-8;
RA Puga A., Xia Y., Elferink C.;
RT "Role of the aryl hydrocarbon receptor in cell cycle regulation.";
RL Chem. Biol. Interact. 141:117-130(2002).
RN [17]
RP INTERACTION WITH NEDD8, LACK OF NEDDYLATION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=12215427; DOI=10.1074/jbc.m202413200;
RA Antenos M., Casper R.F., Brown T.J.;
RT "Interaction with Nedd8, a ubiquitin-like protein, enhances the
RT transcriptional activity of the aryl hydrocarbon receptor.";
RL J. Biol. Chem. 277:44028-44034(2002).
RN [18]
RP INTERACTION WITH HSP90AB1.
RX PubMed=15581363; DOI=10.1021/bi048736m;
RA Ogiso H., Kagi N., Matsumoto E., Nishimoto M., Arai R., Shirouzu M.,
RA Mimura J., Fujii-Kuriyama Y., Yokoyama S.;
RT "Phosphorylation analysis of 90 kDa heat shock protein within the cytosolic
RT arylhydrocarbon receptor complex.";
RL Biochemistry 43:15510-15519(2004).
RN [19]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ARNTL.
RX PubMed=20106950; DOI=10.1093/toxsci/kfq022;
RA Xu C.X., Krager S.L., Liao D.F., Tischkau S.A.;
RT "Disruption of CLOCK-BMAL1 transcriptional activity is responsible for aryl
RT hydrocarbon receptor-mediated regulation of Period1 gene.";
RL Toxicol. Sci. 115:98-108(2010).
RN [20]
RP DISRUPTION PHENOTYPE.
RX PubMed=29726989; DOI=10.1093/hmg/ddy165;
RA Zhou Y., Li S., Huang L., Yang Y., Zhang L., Yang M., Liu W., Ramasamy K.,
RA Jiang Z., Sundaresan P., Zhu X., Yang Z.;
RT "A splicing mutation in aryl hydrocarbon receptor associated with retinitis
RT pigmentosa.";
RL Hum. Mol. Genet. 27:2563-2572(2018).
RN [21] {ECO:0007744|PDB:4M4X}
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 110-267 OF HOMODIMER, MUTAGENESIS
RP OF GLU-112; PHE-115; LEU-116; ALA-119; LEU-120; VAL-124; PHE-260 AND
RP ILE-262, DOMAIN, REGION, SUBUNIT, AND INTERACTION WITH ARNT.
RX PubMed=24001774; DOI=10.1128/mcb.00698-13;
RA Wu D., Potluri N., Kim Y., Rastinejad F.;
RT "Structure and dimerization properties of the aryl hydrocarbon receptor
RT PAS-A domain.";
RL Mol. Cell. Biol. 33:4346-4356(2013).
RN [22] {ECO:0007744|PDB:5V0L}
RP X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS) OF 29-267 IN COMPLEXES WITH ARNT AND
RP DNA, MUTAGENESIS OF ARG-39; LEU-42; ASN-43; LEU-49; LYS-65; ARG-70;
RP PHE-115; LEU-120; PHE-134; ILE-152; LYS-238 AND LEU-240, SUBCELLULAR
RP LOCATION, FUNCTION, AND INTERACTION WITH ARNT.
RX PubMed=28396409; DOI=10.1073/pnas.1617035114;
RA Seok S.H., Lee W., Jiang L., Molugu K., Zheng A., Li Y., Park S.,
RA Bradfield C.A., Xing Y.;
RT "Structural hierarchy controlling dimerization and target DNA recognition
RT in the AHR transcriptional complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:5431-5436(2017).
CC -!- FUNCTION: Ligand-activated transcription factor that enables cells to
CC adapt to changing conditions by sensing compounds from the environment,
CC diet, microbiome and cellular metabolism, and which plays important
CC roles in development, immunity and cancer (PubMed:10639156,
CC PubMed:10973493, PubMed:1314586, PubMed:7961644, PubMed:7969080,
CC PubMed:8806883, PubMed:9427285). Upon ligand binding, translocates into
CC the nucleus, where it heterodimerizes with ARNT and induces
CC transcription by binding to xenobiotic response elements (XRE) (By
CC similarity). Regulates a variety of biological processes, including
CC angiogenesis, hematopoiesis, drug and lipid metabolism, cell motility
CC and immune modulation (PubMed:20106950, PubMed:28396409). Xenobiotics
CC can act as ligands: upon xenobiotic-binding, activates the expression
CC of multiple phase I and II xenobiotic chemical metabolizing enzyme
CC genes (such as the CYP1A1 gene) (PubMed:10639156, PubMed:10973493,
CC PubMed:1314586, PubMed:7961644, PubMed:7969080, PubMed:8806883,
CC PubMed:9427285). Mediates biochemical and toxic effects of halogenated
CC aromatic hydrocarbons (By similarity). Next to xenobiotics, natural
CC ligands derived from plants, microbiota, and endogenous metabolism are
CC potent AHR agonists (By similarity). Tryptophan (Trp) derivatives
CC constitute an important class of endogenous AHR ligands (By
CC similarity). Acts as a negative regulator of anti-tumor immunity:
CC indoles and kynurenic acid generated by Trp catabolism act as ligand
CC and activate AHR, thereby promoting AHR-driven cancer cell motility and
CC suppressing adaptive immunity (By similarity). Regulates the circadian
CC clock by inhibiting the basal and circadian expression of the core
CC circadian component PER1 (By similarity). Inhibits PER1 by repressing
CC the CLOCK-ARNTL/BMAL1 heterodimer mediated transcriptional activation
CC of PER1 (PubMed:20106950). The heterodimer ARNT:AHR binds to core DNA
CC sequence 5'-TGCGTG-3' within the dioxin response element (DRE) of
CC target gene promoters and activates their transcription
CC (PubMed:28396409). {ECO:0000250|UniProtKB:P35869,
CC ECO:0000269|PubMed:10639156, ECO:0000269|PubMed:10973493,
CC ECO:0000269|PubMed:1314586, ECO:0000269|PubMed:20106950,
CC ECO:0000269|PubMed:28396409, ECO:0000269|PubMed:7961644,
CC ECO:0000269|PubMed:7969080, ECO:0000269|PubMed:8806883,
CC ECO:0000269|PubMed:9427285}.
CC -!- SUBUNIT: Homodimer (PubMed:24001774). Heterodimer; efficient DNA
CC binding requires dimerization with another bHLH protein (By
CC similarity). Interacts with ARNT; the heterodimer ARNT:AHR binds to
CC core DNA sequence 5'-TGCGTG-3' within the dioxin response element (DRE)
CC of target gene promoters and activates their transcription
CC (PubMed:24001774, PubMed:28396409). Binds MYBBP1A (PubMed:11956195).
CC Interacts with coactivators including SRC-1, RIP140 and NOCA7, and with
CC the corepressor SMRT. Interacts with NEDD8 and IVNS1ABP
CC (PubMed:12215427). Interacts with ARNTL/BMAL1 (PubMed:20106950).
CC Interacts with HSP90AB1 (PubMed:15581363). Interacts with TIPARP;
CC leading to mono-ADP-ribosylation of AHR and subsequent inhibition of
CC AHR (By similarity). {ECO:0000250|UniProtKB:P35869,
CC ECO:0000269|PubMed:11956195, ECO:0000269|PubMed:12215427,
CC ECO:0000269|PubMed:15581363, ECO:0000269|PubMed:20106950,
CC ECO:0000269|PubMed:24001774, ECO:0000269|PubMed:28396409}.
CC -!- INTERACTION:
CC P30561; P79832: arnt; Xeno; NbExp=2; IntAct=EBI-78863, EBI-958635;
CC P30561; O94763: URI1; Xeno; NbExp=2; IntAct=EBI-78863, EBI-357067;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12215427,
CC ECO:0000269|PubMed:28396409}. Nucleus {ECO:0000269|PubMed:12215427,
CC ECO:0000269|PubMed:20106950, ECO:0000269|PubMed:28396409}.
CC Note=Initially cytoplasmic; upon binding with ligand and interaction
CC with a HSP90, it translocates to the nucleus.
CC {ECO:0000269|PubMed:20106950, ECO:0000269|PubMed:28396409}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested including brain,
CC heart, kidney, liver, lung, muscle, ovary, skin, spleen and thymus.
CC {ECO:0000269|PubMed:10639156}.
CC -!- DEVELOPMENTAL STAGE: Between 10 dpc and 12 dpc, abundantly expressed in
CC neuroepithelium, branchial arches, cranial nerves, liver, heart and
CC spinal ganglia. {ECO:0000269|PubMed:12215427}.
CC -!- INDUCTION: Induced or repressed by TGF-beta and dioxin in a cell-type
CC specific fashion. Repressed by cAMP, retinoic acid, and TPA.
CC {ECO:0000269|PubMed:8806768}.
CC -!- DOMAIN: The PAS 1 domain is essential for dimerization and also
CC required for AHR:ARNT heterodimerization.
CC {ECO:0000269|PubMed:24001774}.
CC -!- PTM: Mono-ADP-ribosylated, leading to inhibit transcription activator
CC activity of AHR. {ECO:0000250|UniProtKB:P35869}.
CC -!- POLYMORPHISM: There are four common alleles; AHRB1; AHRB2; AHRB3 and
CC AHRD. The sequence of AHRB2 is shown here.
CC -!- DISRUPTION PHENOTYPE: AHR knockdown in the retina results in reduced
CC electroretinogram responses, thinning of the outer segment, and
CC degeneration of photoreceptors. {ECO:0000269|PubMed:29726989}.
CC -!- MISCELLANEOUS: Although it interacts with NEDD8, it does not seem to be
CC neddylated. {ECO:0000269|PubMed:12215427}.
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DR EMBL; D38417; BAA07469.1; -; mRNA.
DR EMBL; M94623; AAA02896.1; -; Unassigned_DNA.
DR EMBL; L19749; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR EMBL; L19750; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR EMBL; L19751; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR EMBL; L19752; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR EMBL; L19753; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR EMBL; L19754; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR EMBL; L19755; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR EMBL; L19756; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR EMBL; L19757; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR EMBL; L19758; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR EMBL; L19759; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR EMBL; D38416; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF325111; AAK13443.1; -; Genomic_DNA.
DR EMBL; AF405560; AAL89725.1; -; mRNA.
DR EMBL; AF405561; AAL89726.1; -; mRNA.
DR EMBL; AF405562; AAL89727.1; -; mRNA.
DR EMBL; AF405563; AAL89728.1; -; mRNA.
DR EMBL; AF405566; AAL89731.1; -; mRNA.
DR EMBL; AF405567; AAL89732.1; -; mRNA.
DR EMBL; AF405570; AAL89735.1; -; mRNA.
DR PIR; A46266; A46266.
DR RefSeq; NP_038492.1; NM_013464.4.
DR PDB; 4M4X; X-ray; 2.55 A; A/B=110-267.
DR PDB; 5V0L; X-ray; 4.00 A; B=29-267.
DR PDBsum; 4M4X; -.
DR PDBsum; 5V0L; -.
DR AlphaFoldDB; P30561; -.
DR SMR; P30561; -.
DR BioGRID; 198037; 8.
DR CORUM; P30561; -.
DR DIP; DIP-222N; -.
DR IntAct; P30561; 8.
DR STRING; 10090.ENSMUSP00000112137; -.
DR BindingDB; P30561; -.
DR ChEMBL; CHEMBL6099; -.
DR GuidetoPHARMACOLOGY; 2951; -.
DR iPTMnet; P30561; -.
DR PhosphoSitePlus; P30561; -.
DR MaxQB; P30561; -.
DR PaxDb; P30561; -.
DR PRIDE; P30561; -.
DR ProteomicsDB; 281961; -.
DR DNASU; 11622; -.
DR GeneID; 11622; -.
DR KEGG; mmu:11622; -.
DR CTD; 196; -.
DR MGI; MGI:105043; Ahr.
DR eggNOG; KOG3560; Eukaryota.
DR InParanoid; P30561; -.
DR OrthoDB; 174264at2759; -.
DR PhylomeDB; P30561; -.
DR Reactome; R-MMU-211945; Phase I - Functionalization of compounds.
DR Reactome; R-MMU-211976; Endogenous sterols.
DR Reactome; R-MMU-211981; Xenobiotics.
DR Reactome; R-MMU-8937144; Aryl hydrocarbon receptor signalling.
DR BioGRID-ORCS; 11622; 2 hits in 77 CRISPR screens.
DR ChiTaRS; Ahr; mouse.
DR PRO; PR:P30561; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P30561; protein.
DR GO; GO:0034751; C:aryl hydrocarbon receptor complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:DFLAT.
DR GO; GO:0034752; C:cytosolic aryl hydrocarbon receptor complex; TAS:DFLAT.
DR GO; GO:0034753; C:nuclear aryl hydrocarbon receptor complex; TAS:DFLAT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005667; C:transcription regulator complex; TAS:MGI.
DR GO; GO:0017162; F:aryl hydrocarbon receptor binding; IPI:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; IPI:UniProtKB.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:MGI.
DR GO; GO:0070888; F:E-box binding; IDA:UniProtKB.
DR GO; GO:0051879; F:Hsp90 protein binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0004879; F:nuclear receptor activity; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0017025; F:TBP-class protein binding; ISO:MGI.
DR GO; GO:0001094; F:TFIID-class transcription factor complex binding; ISO:MGI.
DR GO; GO:0015643; F:toxic substance binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0001223; F:transcription coactivator binding; ISO:MGI.
DR GO; GO:0030183; P:B cell differentiation; TAS:DFLAT.
DR GO; GO:0001782; P:B cell homeostasis; IMP:DFLAT.
DR GO; GO:0001922; P:B-1 B cell homeostasis; TAS:DFLAT.
DR GO; GO:0008015; P:blood circulation; IMP:DFLAT.
DR GO; GO:0001568; P:blood vessel development; IMP:DFLAT.
DR GO; GO:0097746; P:blood vessel diameter maintenance; IMP:DFLAT.
DR GO; GO:0048514; P:blood vessel morphogenesis; IMP:DFLAT.
DR GO; GO:0001974; P:blood vessel remodeling; IMP:DFLAT.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IMP:DFLAT.
DR GO; GO:0043010; P:camera-type eye development; IMP:DFLAT.
DR GO; GO:0019933; P:cAMP-mediated signaling; ISO:MGI.
DR GO; GO:0003214; P:cardiac left ventricle morphogenesis; IMP:DFLAT.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000902; P:cell morphogenesis; IMP:DFLAT.
DR GO; GO:1904613; P:cellular response to 2,3,7,8-tetrachlorodibenzodioxine; ISO:MGI.
DR GO; GO:1904682; P:cellular response to 3-methylcholanthrene; IDA:UniProtKB.
DR GO; GO:0071320; P:cellular response to cAMP; ISO:MGI.
DR GO; GO:1904322; P:cellular response to forskolin; ISO:MGI.
DR GO; GO:0032922; P:circadian regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0003243; P:circumferential growth involved in left ventricle morphogenesis; IMP:DFLAT.
DR GO; GO:0061009; P:common bile duct development; IMP:DFLAT.
DR GO; GO:0035162; P:embryonic hemopoiesis; IMP:DFLAT.
DR GO; GO:0048732; P:gland development; IMP:MGI.
DR GO; GO:0072102; P:glomerulus morphogenesis; IMP:DFLAT.
DR GO; GO:0002376; P:immune system process; IMP:DFLAT.
DR GO; GO:0060993; P:kidney morphogenesis; IMP:DFLAT.
DR GO; GO:0001889; P:liver development; IMP:DFLAT.
DR GO; GO:0002260; P:lymphocyte homeostasis; IMP:DFLAT.
DR GO; GO:0010693; P:negative regulation of alkaline phosphatase activity; ISO:MGI.
DR GO; GO:1903170; P:negative regulation of calcium ion transmembrane transport; ISO:MGI.
DR GO; GO:2000279; P:negative regulation of DNA biosynthetic process; ISO:MGI.
DR GO; GO:0060547; P:negative regulation of necrotic cell death; IMP:DFLAT.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISO:MGI.
DR GO; GO:0033689; P:negative regulation of osteoblast proliferation; ISO:MGI.
DR GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; IMP:DFLAT.
DR GO; GO:0002841; P:negative regulation of T cell mediated immune response to tumor cell; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045906; P:negative regulation of vasoconstriction; IMP:DFLAT.
DR GO; GO:0001541; P:ovarian follicle development; ISO:MGI.
DR GO; GO:0045793; P:positive regulation of cell size; IMP:DFLAT.
DR GO; GO:0040010; P:positive regulation of growth rate; IMP:DFLAT.
DR GO; GO:0045899; P:positive regulation of RNA polymerase II transcription preinitiation complex assembly; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0035166; P:post-embryonic hemopoiesis; IMP:DFLAT.
DR GO; GO:0030850; P:prostate gland development; IMP:MGI.
DR GO; GO:0002819; P:regulation of adaptive immune response; ISS:UniProtKB.
DR GO; GO:0030888; P:regulation of B cell proliferation; ISO:MGI.
DR GO; GO:0008217; P:regulation of blood pressure; TAS:DFLAT.
DR GO; GO:0010468; P:regulation of gene expression; ISO:MGI.
DR GO; GO:0060420; P:regulation of heart growth; TAS:DFLAT.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0048608; P:reproductive structure development; IMP:MGI.
DR GO; GO:0014070; P:response to organic cyclic compound; ISO:MGI.
DR GO; GO:0009636; P:response to toxic substance; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:UniProtKB.
DR GO; GO:0048745; P:smooth muscle tissue development; IMP:DFLAT.
DR GO; GO:0048536; P:spleen development; IMP:DFLAT.
DR GO; GO:0043029; P:T cell homeostasis; IMP:DFLAT.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0060841; P:venous blood vessel development; IMP:DFLAT.
DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:MGI.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR033348; AHR.
DR InterPro; IPR039091; AHR/AHRR.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR PANTHER; PTHR10649; PTHR10649; 1.
DR PANTHER; PTHR10649:SF9; PTHR10649:SF9; 1.
DR Pfam; PF00010; HLH; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 1.
DR SMART; SM00353; HLH; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF47459; SSF47459; 1.
DR SUPFAM; SSF55785; SSF55785; 2.
DR PROSITE; PS50888; BHLH; 1.
DR PROSITE; PS50112; PAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; ADP-ribosylation; Biological rhythms; Cell cycle;
KW Cytoplasm; Direct protein sequencing; DNA-binding; Nucleus; Receptor;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation.
FT PROPEP 1..9
FT /evidence="ECO:0000269|PubMed:1325649,
FT ECO:0000269|PubMed:1846217"
FT /id="PRO_0000013452"
FT CHAIN 10..848
FT /note="Aryl hydrocarbon receptor"
FT /id="PRO_0000013453"
FT DOMAIN 26..79
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT DOMAIN 116..179
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 269..336
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 342..380
FT /note="PAC"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 37..65
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P35869"
FT REGION 116..124
FT /note="Required for maintaining the overall integrity of
FT the AHR:ARNT heterodimer and its transcriptional activity"
FT /evidence="ECO:0000269|PubMed:24001774"
FT REGION 260..262
FT /note="Required for maintaining the overall integrity of
FT the AHR:ARNT heterodimer and its transcriptional activity"
FT /evidence="ECO:0000269|PubMed:24001774"
FT REGION 421..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 324
FT /note="M -> I (in allele AHRB1; no increase in specific
FT ligand binding)"
FT /evidence="ECO:0000269|PubMed:11875369,
FT ECO:0000269|PubMed:1314586, ECO:0000269|PubMed:1325649,
FT ECO:0000269|PubMed:7961644, ECO:0000269|PubMed:7969080,
FT ECO:0000269|PubMed:8148872"
FT VARIANT 348
FT /note="F -> L (in allele AHRB1 and allele AHRD; no
FT reduction in specific ligand binding)"
FT /evidence="ECO:0000269|PubMed:11875369,
FT ECO:0000269|PubMed:1314586, ECO:0000269|PubMed:1325649,
FT ECO:0000269|PubMed:7961644, ECO:0000269|PubMed:7969080,
FT ECO:0000269|PubMed:8148872, ECO:0000269|Ref.7"
FT VARIANT 375
FT /note="A -> V (in allele AHRD; reduced specific ligand
FT binding)"
FT /evidence="ECO:0000269|PubMed:11875369,
FT ECO:0000269|PubMed:7961644, ECO:0000269|PubMed:7969080,
FT ECO:0000269|PubMed:8148872, ECO:0000269|Ref.7"
FT VARIANT 471
FT /note="P -> L (in allele AHRB1; no increase in specific
FT ligand binding)"
FT /evidence="ECO:0000269|PubMed:11875369,
FT ECO:0000269|PubMed:1314586, ECO:0000269|PubMed:1325649,
FT ECO:0000269|PubMed:7961644, ECO:0000269|PubMed:7969080,
FT ECO:0000269|PubMed:8148872"
FT VARIANT 533
FT /note="N -> S (in allele AHRB1; no increase in specific
FT ligand binding)"
FT /evidence="ECO:0000269|PubMed:11875369,
FT ECO:0000269|PubMed:1314586, ECO:0000269|PubMed:1325649,
FT ECO:0000269|PubMed:7961644, ECO:0000269|PubMed:7969080,
FT ECO:0000269|PubMed:8148872"
FT VARIANT 589
FT /note="M -> I (in allele AHRD)"
FT /evidence="ECO:0000269|PubMed:11875369, ECO:0000269|Ref.7"
FT VARIANT 589
FT /note="M -> L (in allele AHRB1; no increase in specific
FT ligand binding)"
FT /evidence="ECO:0000269|PubMed:1314586,
FT ECO:0000269|PubMed:1325649, ECO:0000269|PubMed:7961644,
FT ECO:0000269|PubMed:7969080, ECO:0000269|PubMed:8148872"
FT VARIANT 758
FT /note="T -> A (in allele AHRB1 and allele AHRD)"
FT /evidence="ECO:0000269|PubMed:11875369,
FT ECO:0000269|PubMed:1314586, ECO:0000269|PubMed:1325649,
FT ECO:0000269|PubMed:7961644, ECO:0000269|PubMed:7969080,
FT ECO:0000269|PubMed:8148872, ECO:0000269|Ref.7"
FT VARIANT 806..848
FT /note="Missing (in allele AHRB1)"
FT VARIANT 808
FT /note="I -> V (in allele AHRB3)"
FT /evidence="ECO:0000269|PubMed:7969080"
FT VARIANT 821
FT /note="G -> D (in allele AHRB3)"
FT /evidence="ECO:0000269|PubMed:7969080"
FT VARIANT 824
FT /note="A -> V (in allele AHRB3)"
FT /evidence="ECO:0000269|PubMed:7969080"
FT VARIANT 843..848
FT /note="TPGGFL -> SHLVGSCSSHARMKFIQEQDTGTVRVGHQYYFSKTFDSCI
FT (in allele AHRB3)"
FT MUTAGEN 39
FT /note="R->D: Drastically reduces the binding affinity of
FT AHR?ARNT to dioxin response element (DRE). Impairs ligand-
FT induced nuclear translocation of AHR."
FT /evidence="ECO:0000269|PubMed:28396409"
FT MUTAGEN 42
FT /note="L->E: Significantly reduces binding affinities of
FT the AHR?ARNT heterodimer to DRE."
FT /evidence="ECO:0000269|PubMed:28396409"
FT MUTAGEN 43
FT /note="N->A: Reduces the binding affinity of AHR?ARNT to
FT the DRE by more than 10-fold."
FT /evidence="ECO:0000269|PubMed:28396409"
FT MUTAGEN 49
FT /note="L->E: Reduces the AHR induction transcription
FT activity by 50%. Increases ligand-induced nuclear
FT translocation of AHR."
FT /evidence="ECO:0000269|PubMed:28396409"
FT MUTAGEN 65
FT /note="K->E: Reduces the binding affinity of AHR?ARNT to
FT the DRE by more than 10-fold."
FT /evidence="ECO:0000269|PubMed:28396409"
FT MUTAGEN 70
FT /note="R->D: Drastically reduces the AHR transcription
FT activity inductiona. Increases constitutive AHR nuclear
FT translocation in the absence of ligands. Reduces binding
FT affinity for the DRE by more than 30-fold in vitro."
FT /evidence="ECO:0000269|PubMed:28396409"
FT MUTAGEN 112
FT /note="E->A: Reduces transcription activity. Decreases
FT interaction with ARNT."
FT /evidence="ECO:0000269|PubMed:24001774"
FT MUTAGEN 115
FT /note="F->A: Highly disrupts the dimerization ability of
FT AHR."
FT /evidence="ECO:0000269|PubMed:24001774"
FT MUTAGEN 115
FT /note="F->D: Highly disrupts the dimerization ability of
FT AHR. Reduces the AHR transcription factor activity
FT induction by 50%."
FT /evidence="ECO:0000269|PubMed:24001774,
FT ECO:0000269|PubMed:28396409"
FT MUTAGEN 116
FT /note="L->E: Highly disrupts the dimerization ability of
FT AHR. Reduces transcription activity. Decreases interaction
FT with ARNT."
FT /evidence="ECO:0000269|PubMed:24001774"
FT MUTAGEN 119
FT /note="A->D: Highly disrupts the dimerization ability of
FT AHR. Reduces transcription activity. Impairs interaction
FT with ARNT."
FT /evidence="ECO:0000269|PubMed:24001774"
FT MUTAGEN 120
FT /note="L->D: Significantly reduces binding affinities of
FT the AHR?ARNT heterodimer to DRE."
FT /evidence="ECO:0000269|PubMed:28396409"
FT MUTAGEN 120
FT /note="L->E: Highly disrupts the dimerization ability of
FT AHR. Reduces transcription activity. Impairs interaction
FT with ARNT."
FT /evidence="ECO:0000269|PubMed:24001774"
FT MUTAGEN 124
FT /note="V->D: Highly disrupts the dimerization ability of
FT AHR. Reduces transcription activity. Impairs interaction
FT with ARNT."
FT /evidence="ECO:0000269|PubMed:24001774"
FT MUTAGEN 134
FT /note="F->D: Reduces the AHR induction activity by ?50%.
FT Translocate to thee nucleus at a high level."
FT /evidence="ECO:0000269|PubMed:28396409"
FT MUTAGEN 152
FT /note="I->D: Completely abolished the AHR induction
FT activity, the ligand-induced nuclear translocation of AHR,
FT and drastically reduced DRE-binding in vitro."
FT /evidence="ECO:0000269|PubMed:28396409"
FT MUTAGEN 238
FT /note="K->D: Significantly reduces binding affinities of
FT the AHR?ARNT heterodimer to DRE."
FT /evidence="ECO:0000269|PubMed:28396409"
FT MUTAGEN 240
FT /note="L->D: Significantly reduces binding affinities of
FT the AHR?ARNT heterodimer to DRE."
FT /evidence="ECO:0000269|PubMed:28396409"
FT MUTAGEN 260
FT /note="F->D: Reduces transcription activity. Impairs
FT interaction with ARNT."
FT /evidence="ECO:0000269|PubMed:24001774"
FT MUTAGEN 262
FT /note="I->D: Reduces transcription activity. Decreases
FT interaction with ARNT."
FT /evidence="ECO:0000269|PubMed:24001774"
FT CONFLICT 74
FT /note="S -> T (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 132..133
FT /note="LV -> FL (in Ref. 1 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 171..172
FT /note="QL -> HV (in Ref. 1 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="H -> N (in Ref. 5; D38416)"
FT /evidence="ECO:0000305"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:4M4X"
FT HELIX 114..119
FT /evidence="ECO:0007829|PDB:4M4X"
FT STRAND 120..128
FT /evidence="ECO:0007829|PDB:4M4X"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:4M4X"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:4M4X"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:4M4X"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:4M4X"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:4M4X"
FT HELIX 165..172
FT /evidence="ECO:0007829|PDB:4M4X"
FT STRAND 211..219
FT /evidence="ECO:0007829|PDB:4M4X"
FT STRAND 225..240
FT /evidence="ECO:0007829|PDB:4M4X"
FT STRAND 256..265
FT /evidence="ECO:0007829|PDB:4M4X"
SQ SEQUENCE 848 AA; 95017 MW; AA1560FA83DDD03C CRC64;
MSSGANITYA SRKRRKPVQK TVKPIPAEGI KSNPSKRHRD RLNTELDRLA SLLPFPQDVI
NKLDKLSVLR LSVSYLRAKS FFDVALKSTP ADRNGGQDQC RAQIRDWQDL QEGEFLLQAL
NGFVLVVTAD ALVFYASSTI QDYLGFQQSD VIHQSVYELI HTEDRAEFQR QLHWALNPDS
AQGVDEAHGP PQAAVYYTPD QLPPENASFM ERCFRCRLRC LLDNSSGFLA MNFQGRLKYL
HGQNKKGKDG ALLPPQLALF AIATPLQPPS ILEIRTKNFI FRTKHKLDFT PIGCDAKGQL
ILGYTEVELC TRGSGYQFIH AADMLHCAES HIRMIKTGES GMTVFRLFAK HSRWRWVQSN
ARLIYRNGRP DYIIATQRPL TDEEGREHLQ KRSTSLPFMF ATGEAVLYEI SSPFSPIMDP
LPIRTKSNTS RKDWAPQSTP SKDSFHPSSL MSALIQQDES IYLCPPSSPA PLDSHFLMGS
VSKCGSWQDS FAAAGSEAAL KHEQIGHAQD VNLALSGGPS ELFPDNKNND LYNIMRNLGI
DFEDIRSMQN EEFFRTDSTA AGEVDFKDID ITDEILTYVQ DSLNNSTLMN SACQQQPVTQ
HLSCMLQERL QLEQQQQLQQ PPPQALEPQQ QLCQMVCPQQ DLGPKHTQIN GTFASWNPTP
PVSFNCPQQE LKHYQLFSSL QGTAQEFPYK PEVDSVPYTQ NFAPCNQPLL PEHSKSVQLD
FPGRDFEPSL HPTTSNLDFV SCLQVPENQS HGINSQSTMV SPQAYYAGAM SMYQCQPGPQ
RTPVDQTQYS SEIPGSQAFL SKVQSRGIFN ETYSSDLSSI GHAAQTTGHL HHLAEARPLP
DITPGGFL
