ID   ARNT_RAT                Reviewed;         800 AA.
AC   P41739;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   27-MAR-2024, entry version 167.
DE   RecName: Full=Aryl hydrocarbon receptor nuclear translocator;
DE            Short=ARNT protein;
DE   AltName: Full=Dioxin receptor, nuclear translocator;
DE   AltName: Full=Hypoxia-inducible factor 1-beta;
DE            Short=HIF-1-beta;
DE            Short=HIF1-beta;
GN   Name=Arnt;
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].
RC   STRAIN=Wistar;
RA   Drutel G., Kathmann M., Heron A., Schwartz J.C., Arrang J.-M.;
RL   Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 96-453.
RC   STRAIN=Sprague-Dawley;
RX   PubMed=8065918; DOI=10.1093/nar/22.15.3038;
RA   Carver L.A., Hogenesch J.B., Bradfield C.A.;
RT   "Tissue specific expression of the rat Ah-receptor and ARNT mRNAs.";
RL   Nucleic Acids Res. 22:3038-3044(1994).
CC   -!- FUNCTION: Required for activity of the AHR. Upon ligand binding, AHR
CC       translocates into the nucleus, where it heterodimerizes with ARNT and
CC       induces transcription by binding to xenobiotic response elements (XRE).
CC       Not required for the ligand-binding subunit to translocate from the
CC       cytosol to the nucleus after ligand binding. The complex initiates
CC       transcription of genes involved in the regulation of a variety of
CC       biological processes, including angiogenesis, hematopoiesis, drug and
CC       lipid metabolism, cell motility and immune modulation (By similarity).
CC       The heterodimer binds to core DNA sequence 5'-TACGTG-3' within the
CC       hypoxia response element (HRE) of target gene promoters and functions
CC       as a transcriptional regulator of the adaptive response to hypoxia (By
CC       similarity). The heterodimer ARNT:AHR binds to core DNA sequence 5'-
CC       TGCGTG-3' within the dioxin response element (DRE) of target gene
CC       promoters and activates their transcription (By similarity).
CC       {ECO:0000250|UniProtKB:P27540, ECO:0000250|UniProtKB:P53762}.
CC   -!- SUBUNIT: Monomer. Homodimer only upon binding to a DNA (By similarity).
CC       Efficient DNA binding requires dimerization with another bHLH protein.
CC       Interacts with TACC3 (By similarity). Interacts with HIF1A, EPAS1,
CC       NPAS1 and NPAS3; forms a heterodimer that binds core DNA sequence 5'-
CC       TACGTG-3' within the hypoxia response element (HRE) of target gene
CC       promoters (By similarity). Forms a heterodimer with AHRR, as well as
CC       with other bHLH proteins. Interacts with NOCA7 (By similarity).
CC       Interacts with TACC3 (By similarity). Interacts with AHR; the
CC       heterodimer ARNT:AHR binds to core DNA sequence 5'-TGCGTG-3' within the
CC       dioxin response element (DRE) of target gene promoters and activates
CC       their transcription (By similarity). Interacts with SIM1 and NPAS4 (By
CC       similarity). {ECO:0000250, ECO:0000250|UniProtKB:P27540,
CC       ECO:0000250|UniProtKB:P53762}.
CC   -!- INTERACTION:
CC       P41739; P41738: Ahr; NbExp=2; IntAct=EBI-1162920, EBI-1162880;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P27540}.
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DR   EMBL; U61184; AAB03811.1; -; mRNA.
DR   EMBL; U08986; AAA56896.1; -; mRNA.
DR   PIR; S58376; S58376.
DR   RefSeq; NP_036912.1; NM_012780.1.
DR   AlphaFoldDB; P41739; -.
DR   SMR; P41739; -.
DR   BioGRID; 247282; 1.
DR   IntAct; P41739; 1.
DR   STRING; 10116.ENSRNOP00000060764; -.
DR   iPTMnet; P41739; -.
DR   PhosphoSitePlus; P41739; -.
DR   PaxDb; 10116-ENSRNOP00000060764; -.
DR   DNASU; 25242; -.
DR   GeneID; 25242; -.
DR   KEGG; rno:25242; -.
DR   UCSC; RGD:2153; rat.
DR   AGR; RGD:2153; -.
DR   CTD; 405; -.
DR   RGD; 2153; Arnt.
DR   eggNOG; KOG3561; Eukaryota.
DR   InParanoid; P41739; -.
DR   OrthoDB; 2872674at2759; -.
DR   PhylomeDB; P41739; -.
DR   Reactome; R-RNO-1234158; Regulation of gene expression by Hypoxia-inducible Factor.
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   Reactome; R-RNO-9768919; NPAS4 regulates expression of target genes.
DR   PRO; PR:P41739; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0034751; C:aryl hydrocarbon receptor complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0034753; C:nuclear aryl hydrocarbon receptor complex; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR   GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR   GO; GO:0017162; F:aryl hydrocarbon receptor binding; ISO:RGD.
DR   GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISO:RGD.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; ISO:RGD.
DR   GO; GO:0001892; P:embryonic placenta development; ISO:RGD.
DR   GO; GO:0030522; P:intracellular receptor signaling pathway; IEA:GOC.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; ISO:RGD.
DR   GO; GO:0046209; P:nitric oxide metabolic process; IEP:RGD.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:RGD.
DR   GO; GO:0046886; P:positive regulation of hormone biosynthetic process; ISO:RGD.
DR   GO; GO:0033235; P:positive regulation of protein sumoylation; ISO:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; ISO:RGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0071548; P:response to dexamethasone; IEP:RGD.
DR   GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR   GO; GO:0009636; P:response to toxic substance; NAS:RGD.
DR   CDD; cd18947; bHLH-PAS_ARNT; 1.
DR   CDD; cd00130; PAS; 2.
DR   Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   InterPro; IPR001067; Nuc_translocat.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR23042:SF50; ARYL HYDROCARBON RECEPTOR NUCLEAR TRANSLOCATOR; 1.
DR   PANTHER; PTHR23042; CIRCADIAN PROTEIN CLOCK/ARNT/BMAL/PAS; 1.
DR   Pfam; PF00010; HLH; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF14598; PAS_11; 1.
DR   PRINTS; PR00785; NCTRNSLOCATR.
DR   SMART; SM00353; HLH; 1.
DR   SMART; SM00086; PAC; 1.
DR   SMART; SM00091; PAS; 2.
DR   SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR   SUPFAM; SSF88633; Positive stranded ssRNA viruses; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50888; BHLH; 1.
DR   PROSITE; PS50112; PAS; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; DNA-binding; Isopeptide bond; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P27540"
FT   CHAIN           2..800
FT                   /note="Aryl hydrocarbon receptor nuclear translocator"
FT                   /id="PRO_0000127121"
FT   DOMAIN          89..142
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   DOMAIN          161..235
FT                   /note="PAS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          349..419
FT                   /note="PAS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          424..467
FT                   /note="PAC"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          73..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          88..128
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P53762"
FT   REGION          112..264
FT                   /note="Required for heterodimer formation with EPAS1"
FT                   /evidence="ECO:0000250|UniProtKB:P53762"
FT   REGION          112..168
FT                   /note="Required for heterodimer formation with HIF1A"
FT                   /evidence="ECO:0000250|UniProtKB:P53762"
FT   REGION          167..171
FT                   /note="Mediates the transcription activity and dimerization
FT                   of the AHR:ARNT complex"
FT                   /evidence="ECO:0000250|UniProtKB:P53762"
FT   REGION          465..487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          499..520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          536..566
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          644..676
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          690..726
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          739..800
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        551..565
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        742..789
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P27540"
FT   MOD_RES         77
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P27540"
FT   CROSSLNK        58
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P27540"
SQ   SEQUENCE   800 AA;  88221 MW;  CD71FCDF2C23BF34 CRC64;
     MAATTANPEM TSDVPSLGPT IASGNPGPGI QGGGAVVQRA IKRRSGLDFD DEGEVNSKFL
     RCDDEQMCND KERFARSDDE QSSADKERLA RENHSEIERR RRNKMTAYIT ELSDMVPTCS
     ALARKPDKLT ILRMAVSHMK SLRGTGNTST DGSYKPSFLT DQELKHLILE AADGFLFIVS
     CETGRVVYVS DSVTPVLNQP QSEWFGSTLY DQVHPDDVDK LREQLSTSEN ALTGRILDLK
     TGTVKKEGQQ SSMRMCMGSR RSFICRMRCG TSSVDPVSMN RLSFLRNRCR NGLGSVKEGE
     PHFVVVHCTG YIKAWPPAGV SLPDDDPEAG QGSKFCLVAI GRLQVTSSPN CTDMSNICQP
     TEFISRHNIE GIFTFVDHRC VATVGYQPQE LLGKNIVEFC HPEDQQLLRD SFQQVVKLKG
     QVLSVMFRFR AKNREWLWMR TSSFTFQNPY SDEMSIFICT NTNVKNSSQE PRPTLSNTIQ
     RSQLGPTTNL SLEMGTGVLA SRQQQQQQQQ QQQQQQQQTE LDMVPGRDGL ASYSHSQVSV
     QPVATAGSEH SKPLEKSEGL FVQDRDPRFS EIYPNISADQ SKGLSSSTVP ATQQLFSQGS
     SFPPNPRPAE NFRNSGLTPP VTIVQPSSSA GQILAQISRH SNLTQGSAPT WTSSTRPGFS
     AQLPTQATAK TRSSQFGVNN FQTSSSFSAM SLPGAPTASP STAAYPTLPN RGSNFPPETG
     QTTGQFQTRT AEGVGVWPQW QGQQPHHRSS SNEQHVQPTS AQPSSQPEVF QEMLSMLGDQ
     SNTYNNEEFP DLTMFPPFSE
//