Recombinant Human Retinoid X Receptor alpha/RXRA protein (Tag Free)

Specifications

Form

Liquid

Additional notes

The Retinoid X Receptor alpha/RXRA protein (111-228aa) was over expressed in E.coli and purified by using conventional column chromatography techniques.

General info

Function

Receptor for retinoic acid that acts as a transcription factor (PubMed : 10874028, PubMed : 11162439, PubMed : 11915042, PubMed : 37478846). Forms homo- or heterodimers with retinoic acid receptors (RARs) and binds to target response elements in response to their ligands, all-trans or 9-cis retinoic acid, to regulate gene expression in various biological processes (PubMed : 10195690, PubMed : 11162439, PubMed : 11915042, PubMed : 16107141, PubMed : 17761950, PubMed : 18800767, PubMed : 19167885, PubMed : 28167758, PubMed : 37478846). The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 to regulate transcription (PubMed : 10195690, PubMed : 11162439, PubMed : 11915042, PubMed : 17761950, PubMed : 28167758). The high affinity ligand for retinoid X receptors (RXRs) is 9-cis retinoic acid (PubMed : 1310260). In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone deacetylation, chromatin condensation and transcriptional suppression (PubMed : 20215566). On ligand binding, the corepressors dissociate from the receptors and coactivators are recruited leading to transcriptional activation (PubMed : 20215566, PubMed : 37478846, PubMed : 9267036). Serves as a common heterodimeric partner for a number of nuclear receptors, such as RARA, RARB and PPARA (PubMed : 10195690, PubMed : 11915042, PubMed : 28167758, PubMed : 29021580). The RXRA/RARB heterodimer can act as a transcriptional repressor or transcriptional activator, depending on the RARE DNA element context (PubMed : 29021580). The RXRA/PPARA heterodimer is required for PPARA transcriptional activity on fatty acid oxidation genes such as ACOX1 and the P450 system genes (PubMed : 10195690). Together with RARA, positively regulates microRNA-10a expression, thereby inhibiting the GATA6/VCAM1 signaling response to pulsatile shear stress in vascular endothelial cells (PubMed : 28167758). Acts as an enhancer of RARA binding to RARE DNA element (PubMed : 28167758). May facilitate the nuclear import of heterodimerization partners such as VDR and NR4A1 (PubMed : 12145331, PubMed : 15509776). Promotes myelin debris phagocytosis and remyelination by macrophages (PubMed : 26463675). Plays a role in the attenuation of the innate immune system in response to viral infections, possibly by negatively regulating the transcription of antiviral genes such as type I IFN genes (PubMed : 25417649). Involved in the regulation of calcium signaling by repressing ITPR2 gene expression, thereby controlling cellular senescence (PubMed : 30216632).

Sequence similarities

Belongs to the nuclear hormone receptor family. NR2 subfamily.

Post-translational modifications

Acetylated by EP300; acetylation enhances DNA binding and transcriptional activity.. Phosphorylated on serine and threonine residues mainly in the N-terminal modulating domain (By similarity). Constitutively phosphorylated on Ser-21 in the presence or absence of ligand (By similarity). Under stress conditions, hyperphosphorylated by activated JNK on Ser-56, Ser-70, Thr-82 and Ser-260 (By similarity). Phosphorylated on Ser-27, in vitro, by PKA (PubMed:11162439). This phosphorylation is required for repression of cAMP-mediated transcriptional activity of RARA (PubMed:11162439).. Ubiquitinated by UBR5, leading to its degradation: UBR5 specifically recognizes and binds ligand-bound RXRA when it is not associated with coactivators (NCOAs) (PubMed:37478846). In presence of NCOAs, the UBR5-degron is not accessible, preventing its ubiquitination and degradation (PubMed:37478846).. Sumoylation negatively regulates transcriptional activity. Desumoylated specifically by SENP6.

Subcellular localisation

Nucleus