ARNT_BOVIN
ID ARNT_BOVIN Reviewed; 790 AA.
AC Q9BE97;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Aryl hydrocarbon receptor nuclear translocator;
DE Short=ARNT protein;
GN Name=ARNT;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hara S., Takahashi R., Kobayashi C., Imura N.;
RT "Characterization of bovine endothelial aryl hydrocarbon receptor nuclear
RT translocator.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:5Y7Y}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 82-464 IN COMPLEX WITH AHRR, AND
RP INTERACTION WITH AHRR.
RX PubMed=28904176; DOI=10.1074/jbc.m117.812974;
RA Sakurai S., Shimizu T., Ohto U.;
RT "The crystal structure of the AhRR-ARNT heterodimer reveals the structural
RT basis of the repression of AhR-mediated transcription.";
RL J. Biol. Chem. 292:17609-17616(2017).
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 (PubMed:28904176). Interacts with NOCA7 (By
CC similarity). Interacts with TACC3 (By similarity). Interacts with AHR;
CC the heterodimer ARNT:AHR binds to core DNA sequence 5'-TGCGTG-3' within
CC the dioxin response element (DRE) of target gene promoters and
CC activates their transcription (By similarity). Interacts with SIM1 and
CC NPAS4 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P27540,
CC ECO:0000250|UniProtKB:P53762, ECO:0000269|PubMed:28904176}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
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DR EMBL; AB053954; BAB40668.1; -; mRNA.
DR RefSeq; NP_776418.1; NM_173993.1.
DR PDB; 5Y7Y; X-ray; 2.40 A; B=82-464.
DR PDBsum; 5Y7Y; -.
DR AlphaFoldDB; Q9BE97; -.
DR BMRB; Q9BE97; -.
DR SMR; Q9BE97; -.
DR BioGRID; 158383; 1.
DR STRING; 9913.ENSBTAP00000028023; -.
DR PaxDb; Q9BE97; -.
DR PRIDE; Q9BE97; -.
DR GeneID; 281010; -.
DR KEGG; bta:281010; -.
DR CTD; 405; -.
DR eggNOG; KOG3561; Eukaryota.
DR InParanoid; Q9BE97; -.
DR OrthoDB; 331262at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0034751; C:aryl hydrocarbon receptor complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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: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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
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 GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 3D-structure; Acetylation; Activator; DNA-binding; Isopeptide bond;
KW Nucleus; 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_0000274192"
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..96
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..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..716
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"
FT HELIX 99..115
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT HELIX 128..143
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT HELIX 161..171
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT HELIX 193..196
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT TURN 202..206
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT HELIX 220..224
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT STRAND 306..312
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT STRAND 337..342
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT STRAND 362..367
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT STRAND 372..376
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT HELIX 380..384
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT HELIX 388..391
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT HELIX 396..399
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT HELIX 402..404
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT HELIX 405..418
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT STRAND 423..430
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT STRAND 436..447
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT TURN 449..451
FT /evidence="ECO:0007829|PDB:5Y7Y"
FT STRAND 454..463
FT /evidence="ECO:0007829|PDB:5Y7Y"
SQ SEQUENCE 790 AA; 86663 MW; A480FE6F100B0381 CRC64;
MAATTANPEM TSDVPPLGPA IASGNPGPGI QGGGAIVQRA IKRRPGLDFD DDGEGNSKFL
RCDDDQMSND KERFARSDDE QSSADKERLA RENHSEIERR RRNKMTAYIT ELSDMVPTCS
ALARKPDKLT ILRMAVSHMK SLRGTGNTST DGTYKPSFLT DQELKHLILE AADGFLFIVS
CETGRVVYVS DSVTPVLNQP QSEWFGSTLY DQVHPDDVDK LREQLSTSEN ALTGRILDLK
TGTVKKEGQQ SSMRMCMGSR RSFICRMRCG NSSVDSVSMN RLSFVRNRCR NGLGSAKDGE
PHFVVVHCTG YIKAWPPAGV SLPDDDPEAG QGSKFCLVAI GRLQVTSSPN CTDMSNVCQP
TEFISRHNIE GIFTFVDHRC VATVGYQPQE LLGKNIVEFC HPEDQQLLRD SFQQVVKLKG
QVLSVMFRFR SKNREWLWVR TSSFTFQNPY SDEIEYIICT NTNVKNSSQE PRPSLSNTIQ
RPQLGPTANL SLEMGSGQLA PRQQQQQTEL DVVPGRDGLT SCNHSQVSVQ PVTTTGPEHS
KPLEKSESLF AQDRDPRFSE IYSNISTDQS KGISSSTVPA TQQLFSQGNT FPPTPRPAEN
FRNSGLAPPV TIVQPSTSAG QMLAQISRHS NPTQGAAPAW TPSTRPGFSA QQVVTEATAK
TRSSQFGVGS FQTPSSFSPM SLPGASTASP GAAAYPSLTN RGSNFAPETG QTAGQFQTRT
AEGVGVWPQW QGQQSHHRSS SNEQHVQQPS AQQPGQPEVF QEMLSMLGDQ SNSYNNEEFP
DLTMFPSFSE
