P53762 · ARNT_MOUSE

  • Protein
    Aryl hydrocarbon receptor nuclear translocator
  • Gene
    Arnt
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Required for activity of the Ah (dioxin) receptor. This protein is required for the ligand-binding subunit to translocate from the cytosol to the nucleus after ligand binding. The complex then initiates transcription of genes involved in the activation of PAH procarcinogens (By similarity).
The heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters and functions as a transcriptional regulator of the adaptive response to hypoxia (PubMed:26245371, PubMed:27782878).
The heterodimer ARNT:AHR binds to core DNA sequence 5'-TGCGTG-3' within the dioxin response element (DRE) of target gene promoters and activates their transcription (PubMed:28602820).
Required for activity of the AHR. Upon ligand binding, AHR translocates into the nucleus, where it heterodimerizes with ARNT and induces transcription by binding to xenobiotic response elements (XRE). Not required for the ligand-binding subunit to translocate from the cytosol to the nucleus after ligand binding. The complex initiates transcription of genes involved in the regulation of a variety of biological processes, including angiogenesis, hematopoiesis, drug and lipid metabolism, cell motility and immune modulation (By similarity).
The heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters and functions as a transcriptional regulator of the adaptive response to hypoxia (PubMed:26245371, PubMed:27782878).
The heterodimer ARNT:AHR binds to core DNA sequence 5'-TGCGTG-3' within the dioxin response element (DRE) of target gene promoters and activates their transcription (PubMed:26245371, PubMed:27782878, PubMed:28602820).

GO annotations

AspectTerm
Cellular Componentaryl hydrocarbon receptor complex
Cellular Componentcytoplasm
Cellular Componentnuclear aryl hydrocarbon receptor complex
Cellular Componentnuclear body
Cellular Componentnucleus
Cellular ComponentRNA polymerase II transcription regulator complex
Cellular Componenttranscription regulator complex
Molecular Functionaryl hydrocarbon receptor binding
Molecular Functioncis-regulatory region sequence-specific DNA binding
Molecular FunctionDNA-binding transcription factor activity
Molecular FunctionDNA-binding transcription factor activity, RNA polymerase II-specific
Molecular Functionnuclear receptor activity
Molecular Functionprotein heterodimerization activity
Molecular Functionprotein homodimerization activity
Molecular Functionprotein-containing complex binding
Molecular FunctionRNA polymerase II cis-regulatory region sequence-specific DNA binding
Molecular Functionsequence-specific DNA binding
Molecular Functionsequence-specific double-stranded DNA binding
Biological Processcell differentiation
Biological Processcellular response to oxidative stress
Biological Processembryonic placenta development
Biological Processnegative regulation of inflammatory response
Biological Processpositive regulation of DNA-templated transcription
Biological Processpositive regulation of hormone biosynthetic process
Biological Processpositive regulation of protein sumoylation
Biological Processpositive regulation of transcription by RNA polymerase II
Biological Processpositive regulation of vascular endothelial growth factor production
Biological Processregulation of transcription by RNA polymerase II
Biological Processresponse to hypoxia
Biological Processresponse to toxic substance

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Aryl hydrocarbon receptor nuclear translocator
  • Short names
    ARNT protein
  • Alternative names
    • Dioxin receptor, nuclear translocator
    • Hypoxia-inducible factor 1-beta (HIF-1-beta; HIF1-beta)

Gene names

    • Name
      Arnt

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • FVB/N
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    P53762
  • Secondary accessions
    • Q60661
    • Q921F3

Proteomes

Organism-specific databases

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis94Reduces DNA binding.
Mutagenesis98Reduces DNA binding.
Mutagenesis102Reduces DNA binding. Decreases transcription factor activity.
Mutagenesis112Interferes with transcription factor activity.
Mutagenesis112Impairs heterodimer formation with EPAS1. Impairs heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Compromise NPAS4:ARNT heterodimer stability. Compromise AHR:ARNT heterodimer stability.
Mutagenesis132Impairs heterodimer formation with EPAS1. Impairs heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Compromise NPAS4:ARNT heterodimer stability. Compromise AHR:ARNT heterodimer stability.
Mutagenesis136Impairs heterodimer formation with EPAS1. Impairs heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Compromise NPAS4:ARNT heterodimer stability. Compromise AHR:ARNT heterodimer stability.
Mutagenesis139Interferes with transcription factor activity.
Mutagenesis164Does not affect transcription factor activity.
Mutagenesis167Highly reduces transcription activity. Impairs interaction with AHR. Impairs heterodimer formation with EPAS1. Impairs heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Compromise NPAS4:ARNT heterodimer stability. Compromise AHR:ARNT heterodimer stability.
Mutagenesis168Highly reduces transcription activity. Impairs interaction with AHR. Impairs heterodimer formation with EPAS1. Impairs heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Compromise NPAS4:ARNT heterodimer stability. Compromise AHR:ARNT heterodimer stability.
Mutagenesis171Reduces transcription activity. Markedly reduces interaction with AHR. Impairs heterodimer formation with EPAS1. Markedly decreases heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Compromise NPAS4:ARNT heterodimer stability. Compromise AHR:ARNT heterodimer stability.
Mutagenesis264Impairs heterodimer formation with EPAS1. Markedly decreases heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Does not compromise NPAS4:ARNT heterodimer stability. Does not compromise AHR:ARNT heterodimer stability.
Mutagenesis266Markedly decreases heterodimer formation with EPAS1. Decreases heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Does not compromise NPAS4:ARNT heterodimer stability. Does not compromise AHR:ARNT heterodimer stability.
Mutagenesis305Markedly decreases heterodimer formation with EPAS1. Markedly decreases heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Does not compromise NPAS4:ARNT heterodimer stability. Does not compromise AHR:ARNT heterodimer stability.
Mutagenesis307Decreases heterodimer formation with EPAS1. Decreases heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Does not compromise NPAS4:ARNT heterodimer stability. Does not compromise AHR:ARNT heterodimer stability.
Mutagenesis366Markedly decreases heterodimer formation with EPAS1. Markedly decreases heterodimer formation with HIF1A. Impairs heterodimer formation with EPAS1; when associated with N-448. Impairs heterodimer formation with HIF1A; when associated with N-448. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Does not compromise NPAS4:ARNT heterodimer stability. Does not compromise AHR:ARNT heterodimer stability.
Mutagenesis448Decreases heterodimer formation with EPAS1. Decreases heterodimer formation with HIF1A. Impairs heterodimer formation with EPAS1; when associated with A-366. Impairs heterodimer formation with HIF1A; when associated with A-366. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Does not compromise NPAS4:ARNT heterodimer stability. Does not compromise AHR:ARNT heterodimer stability.
Mutagenesis456Decreases heterodimer formation with EPAS1. Decreases heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Does not compromise NPAS4:ARNT heterodimer stability. Does not compromise AHR:ARNT heterodimer stability.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 23 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain, cross-link.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylalanine
ChainPRO_00001271192-791Aryl hydrocarbon receptor nuclear translocator
Cross-link58Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue77Phosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Ubiquitous.

Gene expression databases

Interaction

Subunit

Monomer (PubMed:28602820).
Homodimer only upon binding to a DNA (PubMed:26245371, PubMed:28602820).
Efficient DNA binding requires dimerization with another bHLH protein (By similarity).
Interacts with TACC3 (PubMed:11025203).
Interacts with HIF1A, EPAS1, NPAS1 and NPAS3; forms a heterodimer that binds core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters (PubMed:26245371, PubMed:27782878).
Forms a heterodimer with AHRR, as well as with other bHLH proteins (PubMed:9887096).
Interacts with NOCA7 (By similarity).
Interacts with AHR; the heterodimer ARNT:AHR binds to core DNA sequence 5'-TGCGTG-3' within the dioxin response element (DRE) of target gene promoters and activates their transcription (PubMed:24001774, PubMed:27782878, PubMed:28602820).
Interacts with SIM1 and NPAS4 (PubMed:27782878).

Binary interactions

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for compositional bias, region, domain.

TypeIDPosition(s)Description
Compositional bias1-19Polar residues
Region1-33Disordered
Region73-97Disordered
Region88-128DNA-binding
Domain89-142bHLH
Region112-168Required for heterodimer formation with HIF1A
Region112-264Required for heterodimer formation with EPAS1
Domain161-235PAS 1
Region167-171Mediates the transcription activity and dimerization of the AHR:ARNT complex
Domain349-419PAS 2
Domain424-467PAC
Region465-508Disordered
Region530-554Disordered
Region631-667Disordered
Compositional bias682-698Polar residues
Region682-715Disordered
Region730-791Disordered
Compositional bias733-780Polar residues

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

P53762-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Name
    Long
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    791
  • Mass (Da)
    86,963
  • Last updated
    2011-07-27 v3
  • Checksum
    BDEC0991CD57D402
MAATTANPEMTSDVPSLGPTIASGNPGPGIQGGGAVVQRAIKRRSGLDFDDEVEVNTKFLRCDDDQMCNDKERFARSDDEQSSADKERLARENHSEIERRRRNKMTAYITELSDMVPTCSALARKPDKLTILRMAVSHMKSLRGTGNTSTDGSYKPSFLTDQELKHLILEAADGFLFIVSCETGRVVYVSDSVTPVLNQPQSEWFGSTLYDQVHPDDVDKLREQLSTSENALTGRVLDLKTGTVKKEGQQSSMRMCMGSRRSFICRMRCGTSSVDPVSMNRLSFLRNRCRNGLGSVKEGEPHFVVVHCTGYIKAWPPAGVSLPDDDPEAGQGSKFCLVAIGRLQVTSSPNCTDMSNICQPTEFISRHNIEGIFTFVDHRCVATVGYQPQELLGKNIVEFCHPEDQQLLRDSFQQVVKLKGQVLSVMFRFRSKTREWLWMRTSSFTFQNPYSDEIEYIICTNTNVKNSSQEPRPTLSNTIPRSQLGPTANLSLEMGTGQLPSRQQQQQHTELDMVPGRDGLASYNHSQVSVQPVASAGSEHSKPLEKSEGLFAQDRDPRFPEIYPSITADQSKGISSSTVPATQQLFSQGSSFPPNPRPAENFRNSGLTPPVTIVQPSSSAGQILAQISRHSNPAQGSAPTWTSSSRPGFAAQQVPTQATAKTRSSQFGVNNFQTSSSFSAMSLPGAPTASSGTAAYPALPNRGSNFPPETGQTTGQFQARTAEGVGVWPQWQGQQPHHRSSSSEQHVQQTQAQAPSQPEVFQEMLSMLGDQSNTYNNEEFPDLTMFPPFSE

P53762-2

  • Name
    Short
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 77-100: SDDEQSSADKERLARENHSEIERR → TKFL

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
D3YV20D3YV20_MOUSEArnt76
Q3ULM2Q3ULM2_MOUSEArnt776
Q8CEC2Q8CEC2_MOUSEArnt760
F7C9F6F7C9F6_MOUSEArnt126

Features

Showing features for compositional bias, alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Compositional bias1-19Polar residues
Alternative sequenceVSP_00209377-100in isoform Short
Sequence conflict411in Ref. 2; AAA61732
Sequence conflict534in Ref. 2; AAA61732
Sequence conflict644in Ref. 1; AAA56717
Sequence conflict650in Ref. 2; AAA61732
Compositional bias682-698Polar residues
Compositional bias733-780Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U10325
EMBL· GenBank· DDBJ
AAA56717.1
EMBL· GenBank· DDBJ
mRNA
U14333
EMBL· GenBank· DDBJ
AAA61732.1
EMBL· GenBank· DDBJ
mRNA
AK153355
EMBL· GenBank· DDBJ
BAE31928.1
EMBL· GenBank· DDBJ
mRNA
CH466620
EMBL· GenBank· DDBJ
EDL38816.1
EMBL· GenBank· DDBJ
Genomic DNA
BC012870
EMBL· GenBank· DDBJ
AAH12870.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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