P41739 · ARNT_RAT
- ProteinAryl hydrocarbon receptor nuclear translocator
- GeneArnt
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids800 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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 (By similarity).
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 (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 (By similarity).
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 (By similarity).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAryl hydrocarbon receptor nuclear translocator
- Short namesARNT protein
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionP41739
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000127121 | 2-800 | Aryl hydrocarbon receptor nuclear translocator | |||
Sequence: AATTANPEMTSDVPSLGPTIASGNPGPGIQGGGAVVQRAIKRRSGLDFDDEGEVNSKFLRCDDEQMCNDKERFARSDDEQSSADKERLARENHSEIERRRRNKMTAYITELSDMVPTCSALARKPDKLTILRMAVSHMKSLRGTGNTSTDGSYKPSFLTDQELKHLILEAADGFLFIVSCETGRVVYVSDSVTPVLNQPQSEWFGSTLYDQVHPDDVDKLREQLSTSENALTGRILDLKTGTVKKEGQQSSMRMCMGSRRSFICRMRCGTSSVDPVSMNRLSFLRNRCRNGLGSVKEGEPHFVVVHCTGYIKAWPPAGVSLPDDDPEAGQGSKFCLVAIGRLQVTSSPNCTDMSNICQPTEFISRHNIEGIFTFVDHRCVATVGYQPQELLGKNIVEFCHPEDQQLLRDSFQQVVKLKGQVLSVMFRFRAKNREWLWMRTSSFTFQNPYSDEMSIFICTNTNVKNSSQEPRPTLSNTIQRSQLGPTTNLSLEMGTGVLASRQQQQQQQQQQQQQQQQTELDMVPGRDGLASYSHSQVSVQPVATAGSEHSKPLEKSEGLFVQDRDPRFSEIYPNISADQSKGLSSSTVPATQQLFSQGSSFPPNPRPAENFRNSGLTPPVTIVQPSSSAGQILAQISRHSNLTQGSAPTWTSSTRPGFSAQLPTQATAKTRSSQFGVNNFQTSSSFSAMSLPGAPTASPSTAAYPTLPNRGSNFPPETGQTTGQFQTRTAEGVGVWPQWQGQQPHHRSSSNEQHVQPTSAQPSSQPEVFQEMLSMLGDQSNTYNNEEFPDLTMFPPFSE | ||||||
Cross-link | 58 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 77 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Monomer. Homodimer only upon binding to a DNA (By similarity).
Efficient DNA binding requires dimerization with another bHLH protein. Interacts with TACC3 (By similarity).
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 (By similarity).
Forms a heterodimer with AHRR, as well as with other bHLH proteins. Interacts with NOCA7 (By similarity).
Interacts with TACC3 (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 (By similarity).
Interacts with SIM1 and NPAS4 (By similarity).
Efficient DNA binding requires dimerization with another bHLH protein. Interacts with TACC3 (By similarity).
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 (By similarity).
Forms a heterodimer with AHRR, as well as with other bHLH proteins. Interacts with NOCA7 (By similarity).
Interacts with TACC3 (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 (By similarity).
Interacts with SIM1 and NPAS4 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P41739 | Ahr P41738 | 2 | EBI-1162920, EBI-1162880 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-19 | Polar residues | ||||
Sequence: MAATTANPEMTSDVPSLGP | ||||||
Region | 1-33 | Disordered | ||||
Sequence: MAATTANPEMTSDVPSLGPTIASGNPGPGIQGG | ||||||
Region | 73-95 | Disordered | ||||
Sequence: RFARSDDEQSSADKERLARENHS | ||||||
Region | 88-128 | DNA-binding | ||||
Sequence: RLARENHSEIERRRRNKMTAYITELSDMVPTCSALARKPDK | ||||||
Domain | 89-142 | bHLH | ||||
Sequence: LARENHSEIERRRRNKMTAYITELSDMVPTCSALARKPDKLTILRMAVSHMKSL | ||||||
Region | 112-168 | Required for heterodimer formation with HIF1A | ||||
Sequence: LSDMVPTCSALARKPDKLTILRMAVSHMKSLRGTGNTSTDGSYKPSFLTDQELKHLI | ||||||
Region | 112-264 | Required for heterodimer formation with EPAS1 | ||||
Sequence: LSDMVPTCSALARKPDKLTILRMAVSHMKSLRGTGNTSTDGSYKPSFLTDQELKHLILEAADGFLFIVSCETGRVVYVSDSVTPVLNQPQSEWFGSTLYDQVHPDDVDKLREQLSTSENALTGRILDLKTGTVKKEGQQSSMRMCMGSRRSFI | ||||||
Domain | 161-235 | PAS 1 | ||||
Sequence: DQELKHLILEAADGFLFIVSCETGRVVYVSDSVTPVLNQPQSEWFGSTLYDQVHPDDVDKLREQLSTSENALTGR | ||||||
Region | 167-171 | Mediates the transcription activity and dimerization of the AHR:ARNT complex | ||||
Sequence: LILEA | ||||||
Domain | 349-419 | PAS 2 | ||||
Sequence: PNCTDMSNICQPTEFISRHNIEGIFTFVDHRCVATVGYQPQELLGKNIVEFCHPEDQQLLRDSFQQVVKLK | ||||||
Domain | 424-467 | PAC | ||||
Sequence: SVMFRFRAKNREWLWMRTSSFTFQNPYSDEMSIFICTNTNVKNS | ||||||
Region | 465-487 | Disordered | ||||
Sequence: KNSSQEPRPTLSNTIQRSQLGPT | ||||||
Region | 499-520 | Disordered | ||||
Sequence: LASRQQQQQQQQQQQQQQQQTE | ||||||
Region | 536-566 | Disordered | ||||
Sequence: SQVSVQPVATAGSEHSKPLEKSEGLFVQDRD | ||||||
Compositional bias | 551-565 | Basic and acidic residues | ||||
Sequence: SKPLEKSEGLFVQDR | ||||||
Region | 644-676 | Disordered | ||||
Sequence: TQGSAPTWTSSTRPGFSAQLPTQATAKTRSSQF | ||||||
Region | 690-726 | Disordered | ||||
Sequence: MSLPGAPTASPSTAAYPTLPNRGSNFPPETGQTTGQF | ||||||
Region | 739-800 | Disordered | ||||
Sequence: QWQGQQPHHRSSSNEQHVQPTSAQPSSQPEVFQEMLSMLGDQSNTYNNEEFPDLTMFPPFSE | ||||||
Compositional bias | 742-789 | Polar residues | ||||
Sequence: GQQPHHRSSSNEQHVQPTSAQPSSQPEVFQEMLSMLGDQSNTYNNEEF |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length800
- Mass (Da)88,221
- Last updated1997-11-01 v2
- ChecksumCD71FCDF2C23BF34
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F1LMF9 | F1LMF9_RAT | Arnt | 810 | ||
E9PTS2 | E9PTS2_RAT | Arnt | 777 | ||
A0A0G2K804 | A0A0G2K804_RAT | Arnt | 795 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-19 | Polar residues | ||||
Sequence: MAATTANPEMTSDVPSLGP | ||||||
Compositional bias | 551-565 | Basic and acidic residues | ||||
Sequence: SKPLEKSEGLFVQDR | ||||||
Compositional bias | 742-789 | Polar residues | ||||
Sequence: GQQPHHRSSSNEQHVQPTSAQPSSQPEVFQEMLSMLGDQSNTYNNEEF |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U61184 EMBL· GenBank· DDBJ | AAB03811.1 EMBL· GenBank· DDBJ | mRNA | ||
U08986 EMBL· GenBank· DDBJ | AAA56896.1 EMBL· GenBank· DDBJ | mRNA |