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Retinoic acid receptor alpha (RAR-alpha) (Nuclear receptor subfamily 1 group B member 1)

 RARA_MOUSE              Reviewed;         462 AA.
P11416; P22603;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
22-NOV-2017, entry version 196.
RecName: Full=Retinoic acid receptor alpha;
Short=RAR-alpha;
AltName: Full=Nuclear receptor subfamily 1 group B member 1;
Name=Rara; Synonyms=Nr1b1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-1).
PubMed=2544807; DOI=10.1038/339714a0;
Zelent A., Krust A., Petkovich M., Kastner P., Chambon P.;
"Cloning of murine alpha and beta retinoic acid receptors and a novel
receptor gamma predominantly expressed in skin.";
Nature 339:714-717(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-1).
PubMed=8383767; DOI=10.3109/10799899309073687;
Heiermann R., Rentrop M., Lang E., Maelicke A.;
"Cloning of several genes coding for retinoic acid nuclear receptors
in the mouse embryonal carcinoma cell line PCC7-MZ1.";
J. Recept. Res. 13:693-709(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA-1 AND ALPHA-2).
PubMed=1846598;
Leroy P., Krust A., Zelent A., Mendelsohn C., Garnier J.-M.,
Kastner P., Dierich A., Chambon P.;
"Multiple isoforms of the mouse retinoic acid receptor alpha are
generated by alternative splicing and differential induction by
retinoic acid.";
EMBO J. 10:59-69(1991).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (VARIANT IN EMBRYONAL CARCINOMA CELL LINE
RAC65).
PubMed=1320576; DOI=10.1111/j.1432-0436.1992.tb00766.x;
Kruyt F.A.E., van der Veer L., Mader S., van den Brink C.E.,
Feijen A., Jonk L.J., Kruijer W., van der Saag P.T.;
"Retinoic acid resistance of the variant embryonal carcinoma cell line
RAC65 is caused by expression of a truncated RAR alpha.";
Differentiation 49:27-37(1992).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (VARIANT IN EMBRYONAL CARCINOMA CELL LINE
RAC65).
PubMed=2174108; DOI=10.1128/MCB.10.12.6445;
Pratt M.A.C., Kralova J., McBurney M.W.;
"A dominant negative mutation of the alpha retinoic acid receptor gene
in a retinoic acid-nonresponsive embryonal carcinoma cell.";
Mol. Cell. Biol. 10:6445-6453(1990).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-1).
STRAIN=FVB/N; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 340-359, METHYLATION AT LYS-347, FUNCTION,
INTERACTION WITH RXRA AND NCOR1, IDENTIFICATION BY MASS SPECTROMETRY,
AND MUTAGENESIS OF LYS-347.
PubMed=17205979; DOI=10.1074/mcp.M600223-MCP200;
Huq M.D., Tsai N.-P., Khan S.A., Wei L.-N.;
"Lysine trimethylation of retinoic acid receptor-alpha: a novel means
to regulate receptor function.";
Mol. Cell. Proteomics 6:677-688(2007).
[8]
INTERACTION WITH CDK7 AND GTF2H3, PHOSPHORYLATION AT SER-77, FUNCTION,
AND MUTAGENESIS OF SER-74; SER-77; SER-449; SER-456 AND SER-461.
PubMed=9230306; DOI=10.1016/S0092-8674(00)80317-7;
Rochette-Egly C., Adam S., Rossignol M., Egly J.-M., Chambon P.;
"Stimulation of RAR alpha activation function AF-1 through binding to
the general transcription factor TFIIH and phosphorylation by CDK7.";
Cell 90:97-107(1997).
[9]
INTERACTION WITH NCOA3.
PubMed=9192892; DOI=10.1038/42652;
Torchia J., Rose D.W., Inostroza J., Kamei Y., Westin S., Glass C.K.,
Rosenfeld M.G.;
"The transcriptional co-activator p/CIP binds CBP and mediates
nuclear-receptor function.";
Nature 387:677-684(1997).
[10]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10660575; DOI=10.1074/jbc.275.6.4145;
Braun K.W., Tribley W.A., Griswold M.D., Kim K.H.;
"Follicle-stimulating hormone inhibits all-trans-retinoic acid-induced
retinoic acid receptor alpha nuclear localization and transcriptional
activation in mouse Sertoli cell lines.";
J. Biol. Chem. 275:4145-4151(2000).
[11]
INTERACTION WITH NCOA6.
PubMed=10788465; DOI=10.1074/jbc.275.18.13510;
Zhu Y.-J., Kan L., Qi C., Kanwar Y.S., Yeldandi A.V., Rao M.S.,
Reddy J.K.;
"Isolation and characterization of peroxisome proliferator-activated
receptor (PPAR) interacting protein (PRIP) as a coactivator for
PPAR.";
J. Biol. Chem. 275:13510-13516(2000).
[12]
PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
PubMed=12079996; DOI=10.1095/biolreprod67.1.29;
Braun K.W., Vo M.N., Kim K.H.;
"Positive regulation of retinoic acid receptor alpha by protein kinase
C and mitogen-activated protein kinase in sertoli cells.";
Biol. Reprod. 67:29-37(2002).
[13]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=15901285; DOI=10.1111/j.1432-0436.2005.00018.x;
Chung S.S., Wang X., Wolgemuth D.J.;
"Male sterility in mice lacking retinoic acid receptor alpha involves
specific abnormalities in spermiogenesis.";
Differentiation 73:188-198(2005).
[14]
DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=17905941; DOI=10.1196/annals.1411.008;
Doyle T.J., Braun K.W., McLean D.J., Wright R.W., Griswold M.D.,
Kim K.H.;
"Potential functions of retinoic acid receptor A in Sertoli cells and
germ cells during spermatogenesis.";
Ann. N. Y. Acad. Sci. 1120:114-130(2007).
[15]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=19389355; DOI=10.1016/j.ydbio.2009.01.031;
Williams J.A., Kondo N., Okabe T., Takeshita N., Pilchak D.M.,
Koyama E., Ochiai T., Jensen D., Chu M.L., Kane M.A., Napoli J.L.,
Enomoto-Iwamoto M., Ghyselinck N., Chambon P., Pacifici M.,
Iwamoto M.;
"Retinoic acid receptors are required for skeletal growth, matrix
homeostasis and growth plate function in postnatal mouse.";
Dev. Biol. 328:315-327(2009).
[16]
PHOSPHORYLATION AT SER-77 AND SER-369, FUNCTION, INTERACTION WITH
GTF2H3, AND MUTAGENESIS OF SER-77 AND SER-369.
PubMed=19078967; DOI=10.1038/emboj.2008.256;
Bruck N., Vitoux D., Ferry C., Duong V., Bauer A., de The H.,
Rochette-Egly C.;
"A coordinated phosphorylation cascade initiated by p38MAPK/MSK1
directs RARalpha to target promoters.";
EMBO J. 28:34-47(2009).
-!- 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 KMT2E/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. In concert with RARG, required for skeletal growth,
matrix homeostasis and growth plate function.
{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}.
-!- SUBUNIT: Interacts with PRMT2 (By similarity). Interacts with
LRIF1 (By similarity). Interacts with NCOA7 in a ligand-inducible
manner. Interacts with KMT2E/MLL5. Interacts (via the ligand-
binding domain) with PRAME; interaction is direct and ligand
(retinoic acid)-dependent. Interacts with PRKAR1A; the interaction
negatively. regulates RARA transcriptional activity. Interacts
with NCOR1 and NCOR2; the interaction occurs in the absence of
ligand and represses transcriptional 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 ASXL1
and NCOA1. Interacts with ACTN4. {ECO:0000250|UniProtKB:P10276,
ECO:0000269|PubMed:10788465, ECO:0000269|PubMed:17205979,
ECO:0000269|PubMed:19078967, ECO:0000269|PubMed:9192892,
ECO:0000269|PubMed:9230306}.
-!- INTERACTION:
Q8C050:Rps6ka5; NbExp=2; IntAct=EBI-346736, EBI-8391218;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nuclear
localization depends on ligand binding, phosphorylation and
sumoylation. Transloaction to the nucleus is dependent on
activation of PKC and the downstream MAPK phosphorylation.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Alpha-1;
IsoId=P11416-1; Sequence=Displayed;
Name=Alpha-2;
IsoId=P11416-2; Sequence=VSP_003630;
-!- TISSUE SPECIFICITY: Expressed in Sertoli cells and germ cells.
{ECO:0000269|PubMed:17905941}.
-!- INDUCTION: By retinoic acid. {ECO:0000269|PubMed:17905941}.
-!- DOMAIN: Composed of three domains: a modulating N-terminal domain,
a DNA-binding domain and a C-terminal ligand-binding domain.
-!- 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: Sumoylated with SUMO2, mainly on Lys-399 which is also
required for SENP6 binding. On all-trans retinoic acid (ATRA)
binding, a confromational 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}.
-!- DISRUPTION PHENOTYPE: Seminiferous tubules of 6 month-old animals
display varying degrees of testicular degeneration, with moderate
to severe levels of germ-cell degeneration. Epithelial cells in
the epididymis show general disorganization. Sperm count is
reduced to about 1.7% of wild-type and sperm mobility reduced by
half. Rara and Rarg, but not Rara and Rarb, double knockout mice
exhibit growth retardation after 3 weeks. Defects are found in the
growth plates with deficiency in cartilage. Growth retardation was
noticable in limb sketal elements such as femurs. Early lethality
and male sterility due to squamous metaplasia of the seminal
vesicles and prostate are also observed.
{ECO:0000269|PubMed:15901285, ECO:0000269|PubMed:17905941,
ECO:0000269|PubMed:19389355}.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
subfamily. {ECO:0000305}.
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EMBL; X56572; CAA39919.1; -; mRNA.
EMBL; X56565; CAA39917.1; -; mRNA.
EMBL; S56656; AAB25783.1; -; mRNA.
EMBL; X57528; CAA40749.1; -; mRNA.
EMBL; M60909; AAA40031.1; -; mRNA.
EMBL; BC010216; AAH10216.1; -; mRNA.
CCDS; CCDS36304.1; -. [P11416-1]
CCDS; CCDS48905.1; -. [P11416-2]
PIR; S05050; S05050.
RefSeq; NP_001169999.1; NM_001176528.1. [P11416-2]
RefSeq; NP_001170773.1; NM_001177302.1. [P11416-1]
RefSeq; NP_001170774.1; NM_001177303.1. [P11416-1]
RefSeq; NP_033050.2; NM_009024.2. [P11416-1]
RefSeq; XP_006532655.1; XM_006532592.3. [P11416-1]
RefSeq; XP_006532656.1; XM_006532593.2. [P11416-1]
RefSeq; XP_017169842.1; XM_017314353.1. [P11416-1]
UniGene; Mm.439744; -.
ProteinModelPortal; P11416; -.
SMR; P11416; -.
BioGrid; 202586; 74.
DIP; DIP-31480N; -.
IntAct; P11416; 12.
MINT; MINT-5210296; -.
STRING; 10090.ENSMUSP00000069744; -.
BindingDB; P11416; -.
ChEMBL; CHEMBL2792; -.
GuidetoPHARMACOLOGY; 590; -.
iPTMnet; P11416; -.
PhosphoSitePlus; P11416; -.
PaxDb; P11416; -.
PRIDE; P11416; -.
Ensembl; ENSMUST00000068133; ENSMUSP00000069744; ENSMUSG00000037992. [P11416-1]
Ensembl; ENSMUST00000107473; ENSMUSP00000103097; ENSMUSG00000037992. [P11416-2]
Ensembl; ENSMUST00000107474; ENSMUSP00000103098; ENSMUSG00000037992. [P11416-1]
Ensembl; ENSMUST00000107475; ENSMUSP00000103099; ENSMUSG00000037992. [P11416-1]
Ensembl; ENSMUST00000164748; ENSMUSP00000129791; ENSMUSG00000037992. [P11416-1]
GeneID; 19401; -.
KEGG; mmu:19401; -.
UCSC; uc007lhx.1; mouse. [P11416-1]
UCSC; uc007lhz.2; mouse. [P11416-2]
CTD; 5914; -.
MGI; MGI:97856; Rara.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
GeneTree; ENSGT00870000136372; -.
HOGENOM; HOG000010312; -.
HOVERGEN; HBG005606; -.
InParanoid; P11416; -.
KO; K08527; -.
OMA; QECSESY; -.
OrthoDB; EOG091G0XCQ; -.
PhylomeDB; P11416; -.
TreeFam; TF328382; -.
Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
Reactome; R-MMU-5362517; Signaling by Retinoic Acid.
PRO; PR:P11416; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000037992; -.
CleanEx; MM_RARA; -.
ExpressionAtlas; P11416; baseline and differential.
Genevisible; P11416; MM.
GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0030425; C:dendrite; IDA:MGI.
GO; GO:0043025; C:neuronal cell body; IDA:MGI.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0051393; F:alpha-actinin binding; ISO:MGI.
GO; GO:0031490; F:chromatin DNA binding; ISO:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0008144; F:drug binding; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
GO; GO:0048027; F:mRNA 5'-UTR binding; IEA:Ensembl.
GO; GO:0004879; F:nuclear receptor activity; IDA:MGI.
GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0051018; F:protein kinase A binding; ISO:MGI.
GO; GO:0043422; F:protein kinase B binding; ISO:MGI.
GO; GO:0005102; F:receptor binding; ISO:MGI.
GO; GO:0000975; F:regulatory region DNA binding; IDA:MGI.
GO; GO:0001972; F:retinoic acid binding; ISO:MGI.
GO; GO:0003708; F:retinoic acid receptor activity; IDA:MGI.
GO; GO:0044323; F:retinoic acid-responsive element binding; ISO:MGI.
GO; GO:0001012; F:RNA polymerase II regulatory region DNA binding; IDA:MGI.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0003707; F:steroid hormone receptor activity; IEA:InterPro.
GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:MGI.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IMP:UniProtKB.
GO; GO:0000900; F:translation repressor activity, nucleic acid binding; IEA:Ensembl.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0043277; P:apoptotic cell clearance; ISO:MGI.
GO; GO:0060348; P:bone development; IGI:MGI.
GO; GO:0071391; P:cellular response to estrogen stimulus; ISO:MGI.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:UniProtKB.
GO; GO:0071300; P:cellular response to retinoic acid; ISO:MGI.
GO; GO:0060591; P:chondroblast differentiation; IMP:MGI.
GO; GO:0031076; P:embryonic camera-type eye development; IGI:MGI.
GO; GO:0060324; P:face development; IGI:MGI.
GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
GO; GO:0007281; P:germ cell development; IMP:UniProtKB.
GO; GO:0002068; P:glandular epithelial cell development; IGI:MGI.
GO; GO:0003417; P:growth plate cartilage development; IGI:MGI.
GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
GO; GO:0060173; P:limb development; IGI:MGI.
GO; GO:0001889; P:liver development; IEA:Ensembl.
GO; GO:0035264; P:multicellular organism growth; IGI:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IGI:MGI.
GO; GO:0061037; P:negative regulation of cartilage development; IMP:MGI.
GO; GO:0045596; P:negative regulation of cell differentiation; IMP:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:0010629; P:negative regulation of gene expression; IGI:MGI.
GO; GO:0030853; P:negative regulation of granulocyte differentiation; ISO:MGI.
GO; GO:0032689; P:negative regulation of interferon-gamma production; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0045947; P:negative regulation of translational initiation; IDA:MGI.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISO:MGI.
GO; GO:0001843; P:neural tube closure; IGI:MGI.
GO; GO:0003148; P:outflow tract septum morphogenesis; IGI:MGI.
GO; GO:0051099; P:positive regulation of binding; ISO:MGI.
GO; GO:0045787; P:positive regulation of cell cycle; ISO:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; IGI:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0032736; P:positive regulation of interleukin-13 production; ISO:MGI.
GO; GO:0032753; P:positive regulation of interleukin-4 production; ISO:MGI.
GO; GO:0032754; P:positive regulation of interleukin-5 production; ISO:MGI.
GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
GO; GO:0045630; P:positive regulation of T-helper 2 cell differentiation; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0030850; P:prostate gland development; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
GO; GO:0030852; P:regulation of granulocyte differentiation; IMP:MGI.
GO; GO:0031641; P:regulation of myelination; IEA:Ensembl.
GO; GO:0048167; P:regulation of synaptic plasticity; IEA:Ensembl.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0034097; P:response to cytokine; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0032526; P:response to retinoic acid; IMP:MGI.
GO; GO:0033189; P:response to vitamin A; IEA:Ensembl.
GO; GO:0048384; P:retinoic acid receptor signaling pathway; ISO:MGI.
GO; GO:0060010; P:Sertoli cell fate commitment; IMP:UniProtKB.
GO; GO:0007165; P:signal transduction; ISO:MGI.
GO; GO:0007283; P:spermatogenesis; IMP:MGI.
GO; GO:0060534; P:trachea cartilage development; IMP:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0001657; P:ureteric bud development; IMP:MGI.
GO; GO:0055012; P:ventricular cardiac muscle cell differentiation; IMP:MGI.
Gene3D; 1.10.565.10; -; 1.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR035500; NHR_like_dom_sf.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
InterPro; IPR003078; Retinoic_acid_rcpt.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF00105; zf-C4; 1.
PRINTS; PR01292; RETNOICACIDR.
PRINTS; PR00398; STRDHORMONER.
PRINTS; PR00047; STROIDFINGER.
SMART; SM00430; HOLI; 1.
SMART; SM00399; ZnF_C4; 1.
SUPFAM; SSF48508; SSF48508; 2.
PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; DNA-binding; Isopeptide bond;
Metal-binding; Methylation; Nucleus; Phosphoprotein; Polymorphism;
Receptor; Reference proteome; Transcription; Transcription regulation;
Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 462 Retinoic acid receptor alpha.
/FTId=PRO_0000053462.
DNA_BIND 88 153 Nuclear receptor. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 88 108 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 124 148 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
REGION 1 87 Modulating.
REGION 154 199 Hinge.
REGION 200 419 Ligand-binding.
REGION 404 419 Required for binding corepressor NCOR1.
MOD_RES 77 77 Phosphoserine; by CDK7.
{ECO:0000269|PubMed:19078967,
ECO:0000269|PubMed:9230306}.
MOD_RES 96 96 Phosphoserine; by PKB/AKT1.
{ECO:0000250|UniProtKB:P10276}.
MOD_RES 219 219 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:P10276}.
MOD_RES 347 347 N6,N6,N6-trimethyllysine.
{ECO:0000269|PubMed:17205979}.
MOD_RES 369 369 Phosphoserine; by PKA and RPS6KA5.
{ECO:0000269|PubMed:19078967}.
CROSSLNK 166 166 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CROSSLNK 171 171 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CROSSLNK 399 399 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
VAR_SEQ 1 60 MASNSSSCPTPGGGHLNGYPVPPYAFFFPPMLGGLSPPGAL
TSLQHQLPVSGYSTPSPAT -> MYESVEVGGLTPAPNPFL
VVDFYNQNRACLLQEKGLPAPGPYSTPLRTPLWNGSNHS
(in isoform Alpha-2).
{ECO:0000303|PubMed:1846598}.
/FTId=VSP_003630.
VARIANT 391 391 G -> A (in embryonal carcinoma cell line
RAC65).
VARIANT 392 462 Missing (in embryonal carcinoma cell line
RAC65).
MUTAGEN 74 74 S->A: No effect on phosphorylation, no
effect on transcriptional activity.
{ECO:0000269|PubMed:9230306}.
MUTAGEN 77 77 S->A: Decreases phosphorylation and no
effect on interaction with CDK7. Strongly
reduces transcriptional activity.
{ECO:0000269|PubMed:19078967,
ECO:0000269|PubMed:9230306}.
MUTAGEN 347 347 K->A,Q: Greatly reduced interaction with
RXRA and NCOR1 and transcriptional
activation.
{ECO:0000269|PubMed:17205979}.
MUTAGEN 347 347 K->F: Reduced methylation levels. Little
effect on interaction with RXRA or NCOR1.
Small loss in transcriptional activation.
{ECO:0000269|PubMed:17205979}.
MUTAGEN 369 369 S->A: Abolishes phosphorylation and
prevents phosphorylation of S-77.
{ECO:0000269|PubMed:19078967}.
MUTAGEN 449 449 S->A: No change in phosphorylation levels
and no effect on transcriptional
activity. {ECO:0000269|PubMed:9230306}.
MUTAGEN 456 456 S->A: No change in phosphorylation levels
and no effect on transcriptional
activity. {ECO:0000269|PubMed:9230306}.
MUTAGEN 461 461 S->A: No change in phosphorylation levels
and no effect on transcriptional
activity. {ECO:0000269|PubMed:9230306}.
CONFLICT 163 163 N -> K (in Ref. 5; AAA40031).
{ECO:0000305}.
CONFLICT 179 179 T -> S (in Ref. 5; AAA40031).
{ECO:0000305}.
CONFLICT 284 284 M -> L (in Ref. 5; AAA40031).
{ECO:0000305}.
SEQUENCE 462 AA; 50735 MW; 726F7799633A85AD CRC64;
MASNSSSCPT PGGGHLNGYP VPPYAFFFPP MLGGLSPPGA LTSLQHQLPV SGYSTPSPAT
IETQSSSSEE IVPSPPSPPP LPRIYKPCFV CQDKSSGYHY GVSACEGCKG FFRRSIQKNM
VYTCHRDKNC IINKVTRNRC QYCRLQKCFD VGMSKESVRN DRNKKKKEAP KPECSESYTL
TPEVGELIEK VRKAHQETFP ALCQLGKYTT NNSSEQRVSL DIDLWDKFSE LSTKCIIKTV
EFAKQLPGFT TLTIADQITL LKAACLDILI LRICTRYTPE QDTMTFSDGL TLNRTQMHNA
GFGPLTDLVF AFANQLLPLE MDDAETGLLS AICLICGDRQ DLEQPDKVDM LQEPLLEALK
VYVRKRRPSR PHMFPKMLMK ITDLRSISAK GAERVITLKM EIPGSMPPLI QEMLENSEGL
DTLSGQSGGG TRDGGGLAPP PGSCSPSLSP SSHRSSPATQ SP


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