ARNT_RABIT
ID ARNT_RABIT Reviewed; 790 AA.
AC O02748;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 134.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white; TISSUE=Liver;
RX PubMed=9022676; DOI=10.1111/j.1432-1033.1996.0512r.x;
RA Takahashi Y., Nakayama K., Shimojima T., Itoh S., Kamataki T.;
RT "Expression of aryl hydrocarbon receptor (AhR) and aryl hydrocarbon
RT receptor nuclear translocator (Arnt) in adult rabbits known to be non-
RT responsive to cytochrome P-450 1A1 (CYP1A1) inducers.";
RL Eur. J. Biochem. 242:512-518(1996).
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|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 -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Was expressed at almost the same level in all
CC tissues except for the heart, liver, and small intestine.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D45239; BAA19931.1; -; mRNA.
DR RefSeq; NP_001075675.1; NM_001082206.1.
DR AlphaFoldDB; O02748; -.
DR BMRB; O02748; -.
DR SMR; O02748; -.
DR STRING; 9986.ENSOCUP00000011684; -.
DR PRIDE; O02748; -.
DR GeneID; 100008996; -.
DR KEGG; ocu:100008996; -.
DR CTD; 405; -.
DR eggNOG; KOG3561; Eukaryota.
DR InParanoid; O02748; -.
DR OrthoDB; 331262at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005667; C:transcription regulator complex; IEA:InterPro.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISS:UniProtKB.
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 2: Evidence at transcript 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..790
FT /note="Aryl hydrocarbon receptor nuclear translocator"
FT /id="PRO_0000127120"
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..98
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..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..790
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 790 AA; 86905 MW; 202D3D88415F90D8 CRC64;
MAATTANPEM TSDVPSLGPN ITSGNPGPAI QGGGTIVQRA VKRRPGLDFD DDGEGNSKFL
RCDEDQMSND KERFARSDDE QSSADKERLA RENHSEIERR RRNKMTAYIT ELSDIVPTCS
ALARKPDKLT ILRMAVSHMK SLRGTGNTST DGSYKPSFLT DQELKHLILE AADGFLFIVS
CETGRVVYVS DSVTPVLNQP QSEWFGSTLY DQVHPDDVDK LREQLSTSEN ALTGRILDLK
TGTVKKEGQQ SSMRMCMGSR RSFICRMRCG NSSVDPVSMN RLSFVRNRCR NGLGSVKDGE
PHFVVVHCTG YIKAWPPAGV SLPDDDPEAG QGSKFCLVAI GRLQVTSSPN CTDMSNVCQP
TEFISRHNIE GIFTFVDHRC VATVGYQPQE LLGKNIVEFC HPEDQQLLRD SFQQVVKLKG
QVLSVMFRFR SKNREWLWTR TSSFTFQNPY SDEIEYIICT NTNVKNSSQE PRPTLSNPIQ
RPQLGPTANL PLEVGSGQLA PRQQQQQTEL DMVPGRDGLT NYNHSQISVQ PVATTGPEHG
KPLEKSDSLF AQDRDPRFSE MYSNINADQS KGISSSTVPA TQQLFSQGNT FPPNPRPAEN
FRNSGLAPPV TIVQASASAG EMLAQISRHS NPTQGTAPTW TPSTRPGFSA QQVASQATTK
SRSSQFGVGN FQSPSSFSSM SLSSTSTASS GAAAYPSLTS RGSNFAPETG QTAGQFQTRT
AEGVGVWPQW QGQQPHHRST SSEQHVQQPS TQQPNQPEVF QEMLSMLGDQ SSSYNNEEFP
DLTMFPSFSE
