ARNT_RAT
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 25-MAY-2022, entry version 159.
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 Ah (dioxin) receptor. This
CC protein is required for the ligand-binding subunit to translocate from
CC the cytosol to the nucleus after ligand binding. The complex then
CC initiates transcription of genes involved in the activation of PAH
CC procarcinogens. The heterodimer with HIF1A or EPAS1/HIF2A functions as
CC a transcriptional regulator of the adaptive response to hypoxia (By
CC similarity). The heterodimer binds to core DNA sequence 5'-TACGTG-3'
CC within the hypoxia response element (HRE) of target gene promoters and
CC functions as a transcriptional regulator of the adaptive response to
CC hypoxia (By similarity). 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 (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:P27540,
CC 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.
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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; P41739; -.
DR DNASU; 25242; -.
DR GeneID; 25242; -.
DR KEGG; rno:25242; -.
DR UCSC; RGD:2153; rat.
DR CTD; 405; -.
DR RGD; 2153; Arnt.
DR eggNOG; KOG3561; Eukaryota.
DR InParanoid; P41739; -.
DR OrthoDB; 331262at2759; -.
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 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:0005634; C:nucleus; IDA: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; ISO:RGD.
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: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; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
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:0043619; P:regulation of transcription from RNA polymerase II promoter in response to oxidative stress; ISO:RGD.
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; cd00130; PAS; 2.
DR Gene3D; 4.10.280.10; -; 1.
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 Pfam; PF00010; HLH; 1.
DR Pfam; PF00989; PAS; 1.
DR PRINTS; PR00785; NCTRNSLOCATR.
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 TIGRFAMs; TIGR00229; sensory_box; 1.
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
