Nuclear receptor subfamily 1 group B member 1 ; NR1B1
Categories
Elisa
Function
Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RXR/RAR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone acetylation, chromatin condensation and transcriptional suppression. On ligand binding, the corepressors dissociate from the receptors and associate with the coactivators leading to transcriptional activation. Regulates expression of target genes in a ligand-dependent manner by recruiting chromatin complexes containing MLL5. Mediates retinoic acid-induced granulopoiesis. RARA plays an essential role in the regulation of retinoic acid-induced germ cell development during spermatogenesis. Has a role in the survival of early spermatocytes at the beginning prophase of meiosis. In Sertoli cells, may promote the survival and development of early meiotic prophase spermatocytes.
Specificity
Natural and recombinant Dog Retinoic acid receptor alpha
Subcellular Location
Nucleus Cytoplasm Nuclear localization depends on ligand binding, phosphorylation and sumoylation. Transloaction to the nucleus is dependent on activation of PKC and the downstream MAPK phosphorylation.
Interacts with NCOA7 in a ligand-inducible manner. Interacts with MLL5. Interacts (via the ligand-binding domain) with PRAME; interaction is direct and ligand (retinoic acid)-dependent. Interacts with NCOR1 and NCOR2; the interaction occurs in the absence of ligand and represses transciptional activity. Interacts with NCOA3 and NCOA6 coactivators, leading to a strong increase of transcription of target genes. Interacts with CDK7; the interaction is enhanced by interaction with GTF2H3. Interacts with GTF2H3; the interaction requires prior phosphorylation on Ser-369 which then enhances interaction with CDK7. Interacts with PRKAR1A; the interaction negatively regulates RARA transcriptional activity. Interacts with PRMT2. Interacts with LRIF1.
"Molecular cloning of canine highly similar retinoic acid receptor alpha." Miyajima N., Watanabe M., Sugano S., Sasaki N. Submitted (2004-05) to the EMBL/GenBank/DDBJ databases
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