AHRR_RAT
ID AHRR_RAT Reviewed; 701 AA.
AC Q75NT5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Aryl hydrocarbon receptor repressor;
DE Short=AhR repressor;
DE Short=AhRR;
GN Name=Ahrr;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=Long Evans;
RX PubMed=15013435; DOI=10.1016/j.bbrc.2004.01.028;
RA Korkalainen M., Tuomisto J., Pohjanvirta R.;
RT "Primary structure and inducibility by 2,3,7,8-tetrachlorodibenzo-p-dioxin
RT (TCDD) of aryl hydrocarbon receptor repressor in a TCDD-sensitive and a
RT TCDD-resistant rat strain.";
RL Biochem. Biophys. Res. Commun. 315:123-131(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=Wistar; TISSUE=Heart;
RX PubMed=16595894; DOI=10.1248/bpb.29.640;
RA Nishihashi H., Kanno Y., Tomuro K., Nakahama T., Inouye Y.;
RT "Primary structure and organ-specific expression of the rat aryl
RT hydrocarbon receptor repressor gene.";
RL Biol. Pharm. Bull. 29:640-647(2006).
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:16595894}.
CC -!- SUBUNIT: Interacts with ARNT, ANKRA2, HDAC4 and HDAC5. Interacts with
CC ARNT; forms a heterodimer with ARNT (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:A9YTQ3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly in the
CC nuclear compartment. First cytoplasmic, translocates into the nuclear
CC compartment upon interaction with ARNT in the cytoplasmic compartment
CC (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis and weakly expressed in
CC heart and liver. Highly expressed in small intestine and cecum in a
CC male-dominant sexual dimorphic fashion. {ECO:0000269|PubMed:15013435,
CC ECO:0000269|PubMed:16595894}.
CC -!- INDUCTION: Increased after TCDD exposure in liver. Highly increased
CC after TCDD exposure in kidney, spleen and heart. Up-regulated by 3-MC
CC in small intestine. {ECO:0000269|PubMed:15013435,
CC ECO:0000269|PubMed:16595894}.
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DR EMBL; AY367561; AAR15509.1; -; mRNA.
DR EMBL; AB174900; BAD13341.1; -; mRNA.
DR RefSeq; NP_001019456.1; NM_001024285.1.
DR AlphaFoldDB; Q75NT5; -.
DR SMR; Q75NT5; -.
DR STRING; 10116.ENSRNOP00000019806; -.
DR iPTMnet; Q75NT5; -.
DR PhosphoSitePlus; Q75NT5; -.
DR PaxDb; Q75NT5; -.
DR PRIDE; Q75NT5; -.
DR Ensembl; ENSRNOT00000019806; ENSRNOP00000019806; ENSRNOG00000014721.
DR GeneID; 498999; -.
DR KEGG; rno:498999; -.
DR UCSC; RGD:1559857; rat.
DR CTD; 57491; -.
DR RGD; 1559857; Ahrr.
DR eggNOG; KOG3560; Eukaryota.
DR GeneTree; ENSGT00940000154486; -.
DR HOGENOM; CLU_023661_0_0_1; -.
DR InParanoid; Q75NT5; -.
DR OMA; LGCDCRA; -.
DR OrthoDB; 325707at2759; -.
DR PhylomeDB; Q75NT5; -.
DR TreeFam; TF352074; -.
DR Reactome; R-RNO-211945; Phase I - Functionalization of compounds.
DR Reactome; R-RNO-211976; Endogenous sterols.
DR Reactome; R-RNO-211981; Xenobiotics.
DR Reactome; R-RNO-8937144; Aryl hydrocarbon receptor signalling.
DR PRO; PR:Q75NT5; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000014721; Expressed in jejunum and 6 other tissues.
DR Genevisible; Q75NT5; RN.
DR GO; GO:0034751; C:aryl hydrocarbon receptor complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0033235; P:positive regulation of protein sumoylation; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006805; P:xenobiotic metabolic process; IEA:InterPro.
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 2: Evidence at transcript level;
KW Cytoplasm; DNA-binding; Isopeptide bond; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..701
FT /note="Aryl hydrocarbon receptor repressor"
FT /id="PRO_0000333859"
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 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..701
FT /note="Needed for transcriptional repression"
FT /evidence="ECO:0000250"
FT COMPBIAS 22..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ SEQUENCE 701 AA; 77799 MW; D80419445C87494E CRC64;
MMIPSGECTY AGRKRRKPIQ KRRLTMGTEK SNPSKRHRDR LNTELDHLAS LLPFSPDIIS
KLDKLSVLRL SVSYLRVKSF FQALQETCVW SAPALSPEDH SSRGFPVQEG RLLLESLNGF
ALVVSAEGMI FYASATIVDY LGFHQTDVMH QNIYDYIHVD DRQDFCRQLH WAMDPPQVVF
GQSPHADTDN TVLGKLLRAQ EGGKGLPSEY SAFLTRCFIC RVRCLLDSTS GFLTMQFQGK
LKFLFGQKKK TPSGTALPPR LSLFCIVAPV LPSVTEMKMK SAFLKAKHRA DIVVTMDSRA
KAVTSLCESE LHPKLNYLAG RSNGENVISL FRGQTDRSHW TRALARSSCL CLRGGPDLLD
PKGTSGDREE DDQKHILRRS PGARGQREMH KYSYGLETPV HLRHLDWSTE QRSQEGTTKL
TRQPSKSEPS TCLVPHGSCV PYPGSQGMFS ASNMASFRES LDHPTGTYCS QMNRPLPDIH
QGQVDPSTCH IPQGSLGSRI PLSGMQCFTA RGFSTEDAKL PSLPVNIGTP CNPVLSLEVP
IKMENESGSQ DIVEASTTSC VWLGTGDMTR RHLVGFPARM HLKTEPDYRQ QVCTPHRGHG
ILGTNPHSRD TVGSCREHAP LYSAHCTCLS PEPPHHLFMC SHSESQHPSL DQDCRAPIVK
REPLDSPSWA APGHVTVPRM FPKNASITVI PSKGSDGIFL P
