AHRR_MOUSE
ID AHRR_MOUSE Reviewed; 701 AA.
AC Q3U1U7; Q147Z5; Q3U3H6; Q69ZN4; Q9Z312;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Aryl hydrocarbon receptor repressor;
DE Short=AhR repressor;
DE Short=AhRR;
GN Name=Ahrr; Synonyms=Kiaa1234;
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] (ISOFORM 1), FUNCTION, INTERACTION WITH ARNT,
RP SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=C57BL/6J; TISSUE=Intestine;
RX PubMed=9887096; DOI=10.1101/gad.13.1.20;
RA Mimura J., Ema M., Sogawa K., Fujii-Kuriyama Y.;
RT "Identification of a novel mechanism of regulation of Ah (dioxin) receptor
RT function.";
RL Genes Dev. 13:20-25(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 92-701 (ISOFORM 3).
RC TISSUE=Fetal brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [6]
RP INDUCTION.
RX PubMed=12520768; DOI=10.1016/s0161-813x(02)00040-2;
RA Huang P., Ceccatelli S., Haakansson H., Grandison L., Rannug A.;
RT "Constitutive and TCDD-induced expression of Ah receptor-responsive genes
RT in the pituitary.";
RL NeuroToxicology 23:783-793(2002).
RN [7]
RP FUNCTION, AND INTERACTION WITH ANKRA2; HDAC4 AND HDAC5.
RX PubMed=17949687; DOI=10.1016/j.bbrc.2007.09.131;
RA Oshima M., Mimura J., Yamamoto M., Fujii-Kuriyama Y.;
RT "Molecular mechanism of transcriptional repression of AhR repressor
RT involving ANKRA2, HDAC4, and HDAC5.";
RL Biochem. Biophys. Res. Commun. 364:276-282(2007).
CC -!- FUNCTION: Mediates dioxin toxicity and is involved in regulation of
CC cell growth and differentiation. Represses the transcription activity
CC of AHR by competing with this transcription factor for heterodimer
CC formation with the ARNT and subsequently binding to the xenobiotic
CC response element (XRE) sequence present in the promoter regulatory
CC region of variety of genes. Represses CYP1A1 by binding the XRE
CC sequence and recruiting ANKRA2, HDAC4 and/or HDAC5. Autoregulates its
CC expression by associating with its own XRE site.
CC {ECO:0000269|PubMed:17949687, ECO:0000269|PubMed:9887096}.
CC -!- SUBUNIT: Interacts with ARNT, ANKRA2, HDAC4 and HDAC5. Interacts with
CC ARNT; forms a heterodimer with ARNT (By similarity).
CC {ECO:0000250|UniProtKB:A9YTQ3, ECO:0000269|PubMed:17949687,
CC ECO:0000269|PubMed:9887096}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9887096}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:9887096}.
CC Note=Predominantly in the nuclear compartment. First cytoplasmic,
CC translocates into the nuclear compartment upon interaction with ARNT in
CC the cytoplasmic compartment.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3U1U7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3U1U7-2; Sequence=VSP_033565;
CC Name=3;
CC IsoId=Q3U1U7-3; Sequence=VSP_033566;
CC -!- INDUCTION: By 3MC. Up-regulated by 2,3,7,8-tetrachlorodibenzo-p-dioxin
CC (TCDD) and beta-naphthoflavone in pituitary.
CC {ECO:0000269|PubMed:12520768, ECO:0000269|PubMed:9887096}.
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DR EMBL; AB015140; BAA37132.1; -; mRNA.
DR EMBL; AK154152; BAE32410.1; -; mRNA.
DR EMBL; AK154761; BAE32810.1; -; mRNA.
DR EMBL; AK155711; BAE33396.1; -; mRNA.
DR EMBL; AC123833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT009486; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC118534; AAI18535.1; -; mRNA.
DR EMBL; AK173134; BAD32412.1; -; mRNA.
DR CCDS; CCDS26641.1; -. [Q3U1U7-1]
DR CCDS; CCDS84037.1; -. [Q3U1U7-2]
DR RefSeq; NP_001304280.1; NM_001317351.1.
DR RefSeq; NP_033774.1; NM_009644.3.
DR RefSeq; XP_006517111.1; XM_006517048.1.
DR RefSeq; XP_006517112.1; XM_006517049.3.
DR RefSeq; XP_006517113.1; XM_006517050.2.
DR AlphaFoldDB; Q3U1U7; -.
DR SMR; Q3U1U7; -.
DR BioGRID; 198038; 4.
DR CORUM; Q3U1U7; -.
DR STRING; 10090.ENSMUSP00000022059; -.
DR iPTMnet; Q3U1U7; -.
DR PhosphoSitePlus; Q3U1U7; -.
DR MaxQB; Q3U1U7; -.
DR PaxDb; Q3U1U7; -.
DR PRIDE; Q3U1U7; -.
DR ProteomicsDB; 281958; -. [Q3U1U7-1]
DR ProteomicsDB; 281959; -. [Q3U1U7-2]
DR ProteomicsDB; 281960; -. [Q3U1U7-3]
DR DNASU; 11624; -.
DR GeneID; 11624; -.
DR KEGG; mmu:11624; -.
DR UCSC; uc007rev.1; mouse. [Q3U1U7-1]
DR UCSC; uc007rex.1; mouse. [Q3U1U7-3]
DR CTD; 57491; -.
DR MGI; MGI:1333776; Ahrr.
DR eggNOG; KOG3560; Eukaryota.
DR InParanoid; Q3U1U7; -.
DR OrthoDB; 325707at2759; -.
DR PhylomeDB; Q3U1U7; -.
DR TreeFam; TF352074; -.
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; 11624; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Cyp1a1; mouse.
DR PRO; PR:Q3U1U7; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q3U1U7; protein.
DR GO; GO:0034751; C:aryl hydrocarbon receptor complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR GO; GO:0033235; P:positive regulation of protein sumoylation; IDA:BHF-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IC:BHF-UCL.
DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:MGI.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR039091; AHR/AHRR.
DR InterPro; IPR039092; AHRR.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR PANTHER; PTHR10649; PTHR10649; 1.
DR PANTHER; PTHR10649:SF3; PTHR10649:SF3; 1.
DR Pfam; PF00010; HLH; 1.
DR Pfam; PF00989; PAS; 1.
DR SMART; SM00353; HLH; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR PROSITE; PS50888; BHLH; 1.
DR PROSITE; PS50112; PAS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; DNA-binding; Isopeptide bond; Nucleus;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..701
FT /note="Aryl hydrocarbon receptor repressor"
FT /id="PRO_0000333858"
FT DOMAIN 25..78
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT DOMAIN 106..176
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT REGION 409..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..701
FT /note="Needed for transcriptional repression"
FT CROSSLNK 583
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:A9YTQ3"
FT CROSSLNK 660
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:A9YTQ3"
FT VAR_SEQ 1..128
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033565"
FT VAR_SEQ 300..701
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_033566"
FT CONFLICT 3
FT /note="I -> V (in Ref. 2; BAE32810)"
FT /evidence="ECO:0000305"
FT CONFLICT 637
FT /note="L -> F (in Ref. 1; BAA37132, 2; BAE32410/BAE32810
FT and 4; AAI18535)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 701 AA; 77726 MW; A440A214C2AEF6E6 CRC64;
MMIPSGECTY AGRKRRKPIQ KRRLTMGAEK SNPSKRHRDR LNTELDHLAS LLPFSPDIIS
KLDKLSVLRL SVSYLRVKSF FQALQETCVW SAPALSPEEH SYRGFPVQEG RLLLESLNGF
ALVVSAEGMI FYASATIVDY LGFHQTDVMH QNIYDYIHVD DRQDFCRQLH WAMDPPQVVF
GQSPHADTDN TVLGKLLRAQ EGGKGLPSEY SAFLTRCFIC RVRCLLDSTS GFLTMQFQGK
LKFLFGQKKK TPSGTALPPR LSLFCIVAPV LPSVTEMKMK STFLKAKHRA DIVVTMDSRA
KAVTSLCESE LHPKLNYLAG KSNGENGISL FRGQTDRSHW ARALARSSCL CLRGGPDLLD
PKGTSGDREE EDQKHILRRS PGAWGQREMH KYSYGLETPV HLRHLNWSTE QRSQESTTKL
TRQPSKNEPS TCLVPHGSCV PYPGSQGMLS ASNMASFRDS LDHPTGAYCS QMNRPLSDIH
QGQVDPSTCH ISQGSLGSRI PLTGMQRFTA RGFSTEDAKL PSLPVTIGTP CNPVLSLDVP
IKMENESGSQ DIVEASTTSC LWLGTSDMAR GHLVGFPARM HLKTEPDYRQ QACTPHLGHG
MLGTNPYSRD TVGSCREHAP LYSAHCTCLD PEPPHHLFMC SHSESQHPSL DQDCRAPIVK
REPLDSPSWA APGQVTVPRM FPKSASKTVI PSKGSDGIFL P
