Rxra
entrez
20181
canonical
uniprot
P28700
canonical
ensembl
ENSMUSG00000015846
resolver
ensp
ENSMUSP00000076491
resolver
ensp
ENSMUSP00000097822
resolver
ensp
ENSMUSP00000109567
resolver
ensp
ENSMUSP00000159198
resolver
enst
ENSMUST00000077257
resolver
enst
ENSMUST00000100251
resolver
enst
ENSMUST00000113934
resolver
genesymbol
Rxra
resolver
genesymbol_syn
Nr2b1
resolver
genesymbol_syn
RXR alpha
resolver
uniprot
A2AJP1
resolver
uniprot
F6UTA4
resolver
uniprot
Q3UMU4
resolver
uniprot
Q6LC96
resolver
uniprot_entry
A2AJP1_MOUSE
resolver
uniprot_entry
F6UTA4_MOUSE
resolver
uniprot_entry
Q3UMU4_MOUSE
resolver
uniprot_entry
Q6LC96_MOUSE
resolver
uniprot_entry
RXRA_MOUSE
resolver
amino_acid_sequence
MDTKHFLPLDFSTQVNSSSLNSPTGRGSMAVPSLHPSLGPGIGSPLGSPGQLHSPISTLSSPINGMGPPFSVISSPMGPHSMSVPTTPTLGFGTGSPQLNSPMNPVSSTEDIKPPLGLNGVLKVPAHPSGNMASFTKHICAICGDRSSGKHYGVYSCEGCKGFFKRTVRKDLTYTCRDNKDCLIDKRQRNRCQYCRYQKCLAMGMKREAVQEERQRGKDRNENEVESTSSANEDMPVEKILEAELAVEPKTETYVEANMGLNPSSPNDPVTNICQAADKQLFTLVEWAKRIPHFSELPLDDQVILLRAGWNELLIASFSHRSIAVKDGILLATGLHVHRNSAHSAGVGAIFDRVLTELVSKMRDMQMDKTELGCLRAIVLFNPDSKGLSNPAEVEALREKVYASLEAYCKHKYPEQPGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQAT
uniprot
proteins
function
FUNCTION: Receptor for retinoic acid that acts as a transcription factor (PubMed:10383391, PubMed:12032153, PubMed:25417649). 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:10383391, PubMed:1310259). 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:1310259). The high affinity ligand for retinoid X receptors (RXRs) is 9-cis retinoic acid (PubMed:10383391, PubMed:25417649). 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 (By similarity). On ligand binding, the corepressors dissociate from the receptors and coactivators are recruited leading to transcriptional activation (By similarity). Serves as a common heterodimeric partner for a number of nuclear receptors, such as RARA, RARB and PPARA (PubMed:1310259). The RXRA/RARB heterodimer can act as a transcriptional repressor or transcriptional activator, depending on the RARE DNA element context (By similarity). The RXRA/PPARA heterodimer is required for PPARA transcriptional activity on fatty acid oxidation genes such as ACOX1 and the P450 system genes (By similarity). Together with RARA, positively regulates microRNA-10a expression, thereby inhibiting the GATA6/VCAM1 signaling response to pulsatile shear stress in vascular endothelial cells (By similarity). Acts as an enhancer of RARA binding to RARE DNA element (By similarity). May facilitate the nuclear import of heterodimerization partners such as VDR and NR4A1 (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:P19793, ECO:0000269|PubMed:10383391, ECO:0000269|PubMed:12032153, ECO:0000269|PubMed:1310259, ECO:0000269|PubMed:25417649, ECO:0000269|PubMed:26463675}.
uniprot
proteins
mass_dalton
51217
uniprot
proteins
mutagenesis
MUTAGEN 22; /note="S->A: Loss of constituitive phosphorylation. No effect on RXRA transcriptional activity."; /evidence="ECO:0000269|PubMed:10383391, ECO:0000269|PubMed:12032153"; MUTAGEN 44; /note="S->A: No effect on constituitive phosphorylation."; /evidence="ECO:0000269|PubMed:10383391"; MUTAGEN 48; /note="S->A: No effect on constituitive phosphorylation."; /evidence="ECO:0000269|PubMed:10383391"; MUTAGEN 54; /note="S->A: No effect on constituitive phosphorylation."; /evidence="ECO:0000269|PubMed:10383391"; MUTAGEN 61; /note="S->A: No effect on constituitive phosphorylation, decreased stress-induced phosphorylation but no effect on RXRA transcriptional activity. Abolishes stress-induced phosphorylation but no effect on RXRA transcriptional activity; when associated with A-75 and A-87. No effect on RXRA transcriptional activity."; /evidence="ECO:0000269|PubMed:10383391"; MUTAGEN 75; /note="S->A: No effect on constituitive phosphorylation, decreased stress-induced phosphorylation but no effect on RXRA transcriptional activity. Abolishes stress-induced phosphorylation but no effect on RXRA transcriptional activity; when associated with A-61 and A-87."; /evidence="ECO:0000269|PubMed:10383391"; MUTAGEN 87; /note="T->A: No effect on constituitive phosphorylation, decreased stress-induced phosphorylation but no effect on RXRA transcriptional activity. Abolishes stress-induced phosphorylation but no effect on RXRA transcriptional activity; when associated with A-61 and A-75. phosphorylation. No effect on RXRA transcriptional activity."; /evidence="ECO:0000269|PubMed:10383391"; MUTAGEN 96; /note="S->A: No effect on constituitive phosphorylation."; /evidence="ECO:0000269|PubMed:10383391"; MUTAGEN 101; /note="S->A: No effect on constituitive phosphorylation."; /evidence="ECO:0000269|PubMed:10383391"; MUTAGEN 265; /note="S->A: No effect on constiuitive phosphorylation but loss of stress-induced phosphorylation. No effect on RXRA transcriptional activity."; /evidence="ECO:0000269|PubMed:10383391"; MUTAGEN 455..456; /note="FL->AA: Abolishes interaction with ASXL1 and NCOA1."; /evidence="ECO:0000269|PubMed:16606617"; MUTAGEN 459..460; /note="ML->AA: Abolishes interaction with ASXL1 and NCOA1."; /evidence="ECO:0000269|PubMed:16606617
uniprot
proteins
post_translational_modification
PTM: Acetylated by EP300; acetylation enhances DNA binding and transcriptional activity. {ECO:0000250|UniProtKB:P19793}.; PTM: Phosphorylated on serine and threonine residues mainly in the N-terminal modulating domain (PubMed:10383391, PubMed:12032153). Constitutively phosphorylated on Ser-22 in the presence or absence of ligand (PubMed:10383391, PubMed:12032153). Under stress conditions, hyperphosphorylated by activated JNK on Ser-61, Ser-75, Thr-87 and Ser-265 (PubMed:10383391). Phosphorylated on Ser-28, in vitro, by PKA (By similarity). This phosphorylation is required for repression of cAMP-mediated transcriptional activity of RARA (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P19793, ECO:0000269|PubMed:10383391, ECO:0000269|PubMed:12032153}.; PTM: Ubiquitinated by UBR5, leading to its degradation: UBR5 specifically recognizes and binds ligand-bound RXRA when it is not associated with coactivators (NCOAs). In presence of NCOAs, the UBR5-degron is not accessible, preventing its ubiquitination and degradation. {ECO:0000250|UniProtKB:P19793}.; PTM: Sumoylation negatively regulates transcriptional activity. Desumoylated specifically by SENP6. {ECO:0000250|UniProtKB:P19793}.
uniprot
proteins
protein_family
NR2 subfamily
uniprot
proteins
protein_family
Nuclear hormone receptor family
uniprot
proteins
pubmed
10383391
uniprot
proteins
pubmed
10788465
uniprot
proteins
pubmed
10882070
uniprot
proteins
pubmed
12032153
uniprot
proteins
pubmed
1310259
uniprot
proteins
pubmed
1312497
uniprot
proteins
pubmed
15528208
uniprot
proteins
pubmed
16606617
uniprot
proteins
pubmed
17595322
uniprot
proteins
pubmed
20078863
uniprot
proteins
pubmed
21152046
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
25417649
uniprot
proteins
pubmed
26463675
uniprot
proteins
pubmed
7838715
uniprot
proteins
sequence_length
467
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26463675}. Cytoplasm {ECO:0000250|UniProtKB:P19793}. Mitochondrion {ECO:0000250|UniProtKB:P19793}. Note=Localization to the nucleus is enhanced by vitamin D3 (By similarity). Nuclear localization may be enhanced by the interaction with heterodimerization partner VDR (By similarity). Translocation to the mitochondrion upon interaction with NR4A1 (By similarity). Increased nuclear localization upon pulsatile shear stress (By similarity). {ECO:0000250|UniProtKB:P19793}.
uniprot
proteins