Rara
entrez
19401
canonical
uniprot
P11416
canonical
ensembl
ENSMUSG00000037992
resolver
ensp
ENSMUSP00000069744
resolver
ensp
ENSMUSP00000103097
resolver
ensp
ENSMUSP00000103098
resolver
ensp
ENSMUSP00000103099
resolver
ensp
ENSMUSP00000129791
resolver
genesymbol
Rara
resolver
genesymbol_syn
Nr1b1
resolver
uniprot
P22603
resolver
uniprot
Q3U3R3
resolver
uniprot
Q3U5E7
resolver
uniprot_entry
Q3U3R3_MOUSE
resolver
uniprot_entry
Q3U5E7_MOUSE
resolver
uniprot_entry
RARA_MOUSE
resolver
uniprot_sec
P22603
resolver
amino_acid_sequence
MASNSSSCPTPGGGHLNGYPVPPYAFFFPPMLGGLSPPGALTSLQHQLPVSGYSTPSPATIETQSSSSEEIVPSPPSPPPLPRIYKPCFVCQDKSSGYHYGVSACEGCKGFFRRSIQKNMVYTCHRDKNCIINKVTRNRCQYCRLQKCFDVGMSKESVRNDRNKKKKEAPKPECSESYTLTPEVGELIEKVRKAHQETFPALCQLGKYTTNNSSEQRVSLDIDLWDKFSELSTKCIIKTVEFAKQLPGFTTLTIADQITLLKAACLDILILRICTRYTPEQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFAFANQLLPLEMDDAETGLLSAICLICGDRQDLEQPDKVDMLQEPLLEALKVYVRKRRPSRPHMFPKMLMKITDLRSISAKGAERVITLKMEIPGSMPPLIQEMLENSEGLDTLSGQSGGGTRDGGGLAPPPGSCSPSLSPSSHRSSPATQSP
uniprot
proteins
function
FUNCTION: Receptor for retinoic acid (PubMed:17205979). 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 (PubMed:17205979). The RXR/RAR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 (PubMed:17205979). 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 associate with the coactivators leading to transcriptional activation (PubMed:17205979, PubMed:19078967, PubMed:9230306). Formation of heterocomplex with histone deacetylases might lead to inhibition of RARE DNA element binding and to transcriptional repression (By similarity). Transcriptional activation and RARE DNA element binding might be supported by the transcription factor KLF2 (By similarity). RARA plays an essential role in the regulation of retinoic acid-induced germ cell development during spermatogenesis (PubMed:15901285). Has a role in the survival of early spermatocytes at the beginning prophase of meiosis (PubMed:15901285, PubMed:17905941). In Sertoli cells, may promote the survival and development of early meiotic prophase spermatocytes (PubMed:10660575, PubMed:17905941). In concert with RARG, required for skeletal growth, matrix homeostasis and growth plate function (PubMed:19389355). Together with RXRA, positively regulates microRNA-10a expression, thereby inhibiting the GATA6/VCAM1 signaling response to pulsatile shear stress in vascular endothelial cells (By similarity). In association with HDAC3, HDAC5 and HDAC7 corepressors, plays a role in the repression of microRNA-10a and thereby promotes the inflammatory response (By similarity). {ECO:0000250|UniProtKB:P10276, ECO:0000269|PubMed:10660575, ECO:0000269|PubMed:15901285, ECO:0000269|PubMed:17205979, ECO:0000269|PubMed:17905941, ECO:0000269|PubMed:19078967, ECO:0000269|PubMed:19389355, ECO:0000269|PubMed:9230306}.
uniprot
proteins
mass_dalton
50735
uniprot
proteins
mutagenesis
MUTAGEN 74; /note="S->A: No effect on phosphorylation, no effect on transcriptional activity."; /evidence="ECO:0000269|PubMed:9230306"; MUTAGEN 77; /note="S->A: Decreases phosphorylation and no effect on interaction with CDK7. Strongly reduces transcriptional activity."; /evidence="ECO:0000269|PubMed:19078967, ECO:0000269|PubMed:9230306"; MUTAGEN 347; /note="K->A,Q: Greatly reduced interaction with RXRA and NCOR1 and transcriptional activation."; /evidence="ECO:0000269|PubMed:17205979"; MUTAGEN 347; /note="K->F: Reduced methylation levels. Little effect on interaction with RXRA or NCOR1. Small loss in transcriptional activation."; /evidence="ECO:0000269|PubMed:17205979"; MUTAGEN 369; /note="S->A: Abolishes phosphorylation and prevents phosphorylation of S-77."; /evidence="ECO:0000269|PubMed:19078967"; MUTAGEN 449; /note="S->A: No change in phosphorylation levels and no effect on transcriptional activity."; /evidence="ECO:0000269|PubMed:9230306"; MUTAGEN 456; /note="S->A: No change in phosphorylation levels and no effect on transcriptional activity."; /evidence="ECO:0000269|PubMed:9230306"; MUTAGEN 461; /note="S->A: No change in phosphorylation levels and no effect on transcriptional activity."; /evidence="ECO:0000269|PubMed:9230306
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on serine and threonine residues. Phosphorylation does not change during cell cycle. Phosphorylation on Ser-77 is crucial for the N-terminal AF1 transcriptional activity. Under stress conditions, MAPK8 enhances phosphorylation on Thr-181, Ser-445 and Ser-461 leading to RARA ubiquitination and degradation. Phosphorylation by AKT1 inhibits the transactivation activity. On retinoic acid stimulation, phosphorylation on Ser-369 by RPS6KA5 promotes interaction with GTF2H3 and the CDK7-mediated phosphorylation of Ser-77. {ECO:0000269|PubMed:12079996, ECO:0000269|PubMed:19078967, ECO:0000269|PubMed:9230306}.; PTM: Ubiquitinated by UBR5, leading to its degradation: UBR5 specifically recognizes and binds ligand-bound RARA 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:P10276}.; PTM: Sumoylated with SUMO2, mainly on Lys-399 which is also required for SENP6 binding. On all-trans retinoic acid (ATRA) binding, a conformational change may occur that allows sumoylation on two additional site, Lys-166 and Lys-171. Probably desumoylated by SENP6. Sumoylation levels determine nuclear localization and regulate ATRA-mediated transcriptional activity (By similarity). {ECO:0000250}.; PTM: Acetylated; acetylation is increased upon pulsatile shear stress and decreased upon oscillatory shear stress. {ECO:0000250|UniProtKB:P10276}.
uniprot
proteins
protein_family
NR1 subfamily
uniprot
proteins
protein_family
Nuclear hormone receptor family
uniprot
proteins
pubmed
10660575
uniprot
proteins
pubmed
10788465
uniprot
proteins
pubmed
12079996
uniprot
proteins
pubmed
1320576
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15901285
uniprot
proteins
pubmed
17205979
uniprot
proteins
pubmed
17905941
uniprot
proteins
pubmed
1846598
uniprot
proteins
pubmed
19078967
uniprot
proteins
pubmed
19389355
uniprot
proteins
pubmed
20078863
uniprot
proteins
pubmed
2174108
uniprot
proteins
pubmed
2544807
uniprot
proteins
pubmed
8383767
uniprot
proteins
pubmed
9192892
uniprot
proteins
pubmed
9230306
uniprot
proteins
sequence_length
462
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10660575, ECO:0000269|PubMed:12079996}. Cytoplasm {ECO:0000269|PubMed:10660575, ECO:0000269|PubMed:12079996}. Note=Nuclear localization depends on ligand binding, phosphorylation and sumoylation (PubMed:10660575, PubMed:12079996). Translocation to the nucleus is dependent on activation of PKC and the downstream MAPK phosphorylation (PubMed:10660575, PubMed:12079996). Increased nuclear localization upon pulsatile shear stress (By similarity). {ECO:0000250|UniProtKB:P10276, ECO:0000269|PubMed:10660575, ECO:0000269|PubMed:12079996}.
uniprot
proteins