Primary Information | |
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BoMiProt ID | Bomi4041 |
Protein Name | Aryl hydrocarbon receptor nuclear translocator/ARNT protein |
Organism | Bos taurus |
Uniprot ID | Q9BE97 |
Milk Fraction | whey |
Ref Sequence ID | NP_776418.1 |
Aminoacid Length | 790 |
Molecular Weight | 86663 |
FASTA Sequence | Download |
Gene Name | ARNT |
Gene ID | 281010 |
Protein Existence Status | reviewed |
Secondary Information | |
Protein Function | ARNT (aryl hydrocarbon receptor nuclear translocator) is a key component of various pathways which induce the transcription of cytochrome P450 and hypoxia response genes.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. The heterodimer with HIF1A or EPAS1/HIF2A functions as a transcriptional regulator of the adaptive response to hypoxia |
Biochemical Properties | a type of basic helix-loop-helix/PER-ARNT-SIM homology (bHLH/PAS) transcription factor.ARNT can be alternatively spliced to express Alt ARNT, containing an additional 15 amino acids immediately N-terminal to the DNA-binding basic region. |
PTMs | Acetylation and Phosphorylation |
Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | >sp|Q9BE97|ARNT_BOVIN Aryl hydrocarbon receptor nuclear translocator OS=Bos taurus OX=9913 GN=ARNT PE=1 SV=1 MAATTANPEMTSDVPPLGPAIASGNPGPGIQGGGAIVQRAIKRRPGLDFDDDGEGNSKFL RCDDDQMSNDKERFARS*77DDEQSSADKERLARENHSEIERRRRNKMTAYITELSDMVPTCS ALARKPDKLTILRMAVSHMKSLRGTGNTSTDGTYKPSFLTDQELKHLILEAADGFLFIVS CETGRVVYVSDSVTPVLNQPQSEWFGSTLYDQVHPDDVDKLREQLSTSENALTGRILDLK TGTVKKEGQQSSMRMCMGSRRSFICRMRCGNSSVDSVSMNRLSFVRNRCRNGLGSAKDGE PHFVVVHCTGYIKAWPPAGVSLPDDDPEAGQGSKFCLVAIGRLQVTSSPNCTDMSNVCQP TEFISRHNIEGIFTFVDHRCVATVGYQPQELLGKNIVEFCHPEDQQLLRDSFQQVVKLKG QVLSVMFRFRSKNREWLWVRTSSFTFQNPYSDEIEYIICTNTNVKNSSQEPRPSLSNTIQ RPQLGPTANLSLEMGSGQLAPRQQQQQTELDVVPGRDGLTSCNHSQVSVQPVTTTGPEHS KPLEKSESLFAQDRDPRFSEIYSNISTDQSKGISSSTVPATQQLFSQGNTFPPTPRPAEN FRNSGLAPPVTIVQPSTSAGQMLAQISRHSNPTQGAAPAWTPSTRPGFSAQQVVTEATAK TRSSQFGVGSFQTPSSFSPMSLPGASTASPGAAAYPSLTNRGSNFAPETGQTAGQFQTRT AEGVGVWPQWQGQQSHHRSSSNEQHVQQPSAQQPGQPEVFQEMLSMLGDQSNSYNNEEFP DLTMFPSFSE |
CATH | Matched CATH superfamily n/a |
Predicted Disorder Regions | 23-29, 49-93, 149-155, 244-253, 483-521, 550-553, 637-643, 669-689, 703-788 |
DisProt Annotation | |
TM Helix Prediction | No TM helices |
Significance of PTMs | ARNT is predominantly phosphorylated on serine residues and that serine 348 (S348) in the PAS domain.phosphorylation of ARNT is also required for this heterodimerization.Phosphorylation of this PAS-region serine residue may be important in other ARNT-mediated gene expression systems. ARNT and Alt ARNT proteins are differentially phosphorylated by protein kinase CKII in vitro.CKII phosphorylation inhibits DNA-binding to an E-box probe by Alt ARNT, but not ARNT. The major site of phosphorylation is Ser77, found exclusively in Alt ARNT. |
PDB ID | 5Y7Y, |
Bibliography | 1.Levine SL, Perdew GH. Aryl hydrocarbon receptor (AhR)/AhR nuclear translocator (ARNT) activity is unaltered by phosphorylation of a periodicity/ARNT/single-minded (PAS)-region serine residue. Mol Pharmacol. 2001 Mar;59(3):557-66. doi: 10.1124/mol.59.3.557. PMID: 11179451. 2.Sakurai, S., Shimizu, T., & Ohto, U. (2017). The crystal structure of the AhRR-ARNT heterodimer reveals the structural basis of the repression of AhR-mediated transcription. The Journal of biological chemistry, 292(43), 17609–17616. https://doi.org/10.1074/jbc.M117.812974 3.Kewley RJ, Whitelaw ML. Phosphorylation inhibits DNA-binding of alternatively spliced aryl hydrocarbon receptor nuclear translocator. Biochem Biophys Res Commun. 2005 Dec 9;338(1):660-7. doi: 10.1016/j.bbrc.2005.08.073. Epub 2005 Aug 19. PMID: 16129408. |