P11416 (RARA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Retinoic acid receptor alpha
Short name=RAR-alpha

Alternative name(s):
Nuclear receptor subfamily 1 group B member 1

Gene names

Name:	Rara
Synonyms:	Nr1b1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	462 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. In concert with RARG, required for skeletal growth, matrix homeostasis and growth plate function. Ref.7 Ref.8 Ref.10 Ref.13 Ref.14 Ref.15 Ref.16
Subunit structure	Interacts with PRMT2 By similarity. Interacts with LRIF1 By similarity. 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 PRKAR1A; the interaction negatively. regulates RARA transcriptional activity. 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 ASXL1 and NCOA1 By similarity. Ref.7 Ref.8 Ref.9 Ref.11 Ref.16
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. Ref.10 Ref.12
Tissue specificity	Expressed in Sertoli cells and germ cells. Ref.14
Induction	By retinoic acid. Ref.14
Domain	Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.
Post-translational modification	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. Ref.8 Ref.12 Ref.16 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.
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. Double Rara-Rarg but not Rara-Rarb null 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. Ref.13 Ref.14 Ref.15
Sequence similarities	Belongs to the nuclear hormone receptor family. NR1 subfamily. Contains 1 nuclear receptor DNA-binding domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Receptor
PTM	Isopeptide bond Methylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	Sertoli cell fate commitment Inferred from mutant phenotype Ref.14. Source: UniProtKB apoptotic cell clearance Inferred from electronic annotation. Source: Compara cellular response to estrogen stimulus Inferred from electronic annotation. Source: Compara cellular response to lipopolysaccharide Inferred from direct assay PubMed 19752193. Source: UniProtKB cellular response to retinoic acid Inferred from electronic annotation. Source: Compara chondroblast differentiation Inferred from mutant phenotype PubMed 10684250. Source: MGI germ cell development Inferred from mutant phenotype Ref.13. Source: UniProtKB growth plate cartilage development Inferred from genetic interaction Ref.15. Source: MGI intracellular estrogen receptor signaling pathway Inferred from electronic annotation. Source: Compara multicellular organism growth Inferred from genetic interaction Ref.15. Source: MGI negative regulation of cartilage development Inferred from mutant phenotype PubMed 10684250. Source: MGI negative regulation of cell differentiation Inferred from mutant phenotype PubMed 10684250. Source: MGI negative regulation of granulocyte differentiation Inferred from electronic annotation. Source: Compara negative regulation of interferon-gamma production Inferred from electronic annotation. Source: Compara negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 8152920. Source: MGI negative regulation of transcription, DNA-dependent Inferred from direct assay PubMed 11641275. Source: MGI negative regulation of translational initiation Inferred from direct assay PubMed 18495661. Source: MGI negative regulation of tumor necrosis factor production Inferred from electronic annotation. Source: Compara positive regulation of ERK1 and ERK2 cascade Inferred from electronic annotation. Source: Compara positive regulation of T-helper 2 cell differentiation Inferred from electronic annotation. Source: Compara positive regulation of binding Inferred from electronic annotation. Source: Compara positive regulation of cell cycle Inferred from electronic annotation. Source: Compara positive regulation of cell proliferation Inferred from genetic interaction PubMed 18026104. Source: MGI positive regulation of gene expression Inferred from mutant phenotype PubMed 19752193. Source: UniProtKB positive regulation of interleukin-13 production Inferred from electronic annotation. Source: Compara positive regulation of interleukin-4 production Inferred from electronic annotation. Source: Compara positive regulation of interleukin-5 production Inferred from electronic annotation. Source: Compara positive regulation of phosphatidylinositol 3-kinase cascade Inferred from electronic annotation. Source: Compara positive regulation of protein kinase B signaling cascade Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara protein phosphorylation Inferred from electronic annotation. Source: Compara regulation of granulocyte differentiation Inferred from mutant phenotype PubMed 11222375. Source: MGI response to estradiol stimulus Inferred from electronic annotation. Source: Compara response to retinoic acid Inferred from mutant phenotype PubMed 11222375. Source: MGI spermatogenesis Inferred from mutant phenotype PubMed 8394014. Source: MGI ureteric bud development Inferred from mutant phenotype PubMed 12195422. Source: MGI ventricular cardiac muscle cell differentiation Inferred from mutant phenotype PubMed 9428411. Source: MGI
Cellular_component	cytoplasm Inferred from direct assay Ref.12. Source: MGI dendrite Inferred from direct assay PubMed 18495661. Source: MGI neuronal cell body Inferred from direct assay PubMed 18495661. Source: MGI nuclear chromatin Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay PubMed 19752193. Source: UniProtKB
Molecular_function	chromatin DNA binding Inferred from electronic annotation. Source: Compara phosphatidylinositol 3-kinase regulator activity Inferred from electronic annotation. Source: Compara retinoic acid binding Inferred from electronic annotation. Source: Compara retinoic acid receptor activity Inferred from direct assay PubMed 15528198. Source: MGI retinoic acid-responsive element binding Inferred from electronic annotation. Source: Compara sequence-specific DNA binding Inferred from direct assay PubMed 17928865. Source: MGI steroid hormone receptor activity Inferred from electronic annotation. Source: InterPro transcription coactivator activity Inferred from electronic annotation. Source: Compara transcription corepressor activity Inferred from electronic annotation. Source: Compara transcription regulatory region DNA binding Inferred from mutant phenotype PubMed 19752193. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Alpha-1 (identifier: P11416-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Alpha-2 (identifier: P11416-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: MASNSSSCPT...SGYSTPSPAT → MYESVEVGGL...TPLWNGSNHS

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 462	462	Retinoic acid receptor alpha		PRO_0000053462
Regions
	DNA binding	88 – 153	66	Nuclear receptor
	Zinc finger	88 – 108	21	NR C4-type
	Zinc finger	124 – 148	25	NR C4-type
	Region	1 – 87	87	Modulating
	Region	154 – 199	46	Hinge
	Region	200 – 419	220	Ligand-binding
	Region	404 – 419	16	Required for binding corepressor NCOR1
Amino acid modifications
	Modified residue	77	1	Phosphoserine; by CDK7 Ref.8 Ref.16
	Modified residue	96	1	Phosphoserine; by PKB/AKT1 By similarity
	Modified residue	219	1	Phosphoserine; by PKA By similarity
	Modified residue	347	1	N6,N6,N6-trimethyllysine Ref.7
	Modified residue	369	1	Phosphoserine; by PKA and RPS6KA5 Ref.16
	Cross-link	166		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
	Cross-link	171		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
	Cross-link	399		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Natural variations
	Alternative sequence	1 – 60	60	MASNS…PSPAT → MYESVEVGGLTPAPNPFLVV DFYNQNRACLLQEKGLPAPG PYSTPLRTPLWNGSNHS in isoform Alpha-2.		VSP_003630
	Natural variant	391	1	G → A in embryonal carcinoma cell line RAC65.
	Natural variant	392 – 462	71	Missing in embryonal carcinoma cell line RAC65.
Experimental info
	Mutagenesis	74	1	S → A: No effect on phosphorylation, no effect on transcriptional activity. Ref.8
	Mutagenesis	77	1	S → A: Decreases phosphorylation and no effect on interaction with CDK7. Strongly reduces transcriptional activity. Ref.8 Ref.16
	Mutagenesis	347	1	K → A or Q: Greatly reduced interaction with RXRA and NCOR1 and transcriptional activation. Ref.7
	Mutagenesis	347	1	K → F: Reduced methylation levels. Little effect on interaction with RXRA or NCOR1. Small loss in transcriptional activation. Ref.7
	Mutagenesis	369	1	S → A: Abolishes phosphorylation and prevents phosphorylation of S-77. Ref.16
	Mutagenesis	449	1	S → A: No change in phosphorylation levels and no effect on transcriptional activity. Ref.8
	Mutagenesis	456	1	S → A: No change in phosphorylation levels and no effect on transcriptional activity. Ref.8
	Mutagenesis	461	1	S → A: No change in phosphorylation levels and no effect on transcriptional activity. Ref.8
	Sequence conflict	163	1	N → K in AAA40031. Ref.5
	Sequence conflict	179	1	T → S in AAA40031. Ref.5
	Sequence conflict	284	1	M → L in AAA40031. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform Alpha-1 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: 726F7799633A85AD	FASTA	462	50,735
	10 20 30 40 50 60 MASNSSSCPT PGGGHLNGYP VPPYAFFFPP MLGGLSPPGA LTSLQHQLPV SGYSTPSPAT 70 80 90 100 110 120 IETQSSSSEE IVPSPPSPPP LPRIYKPCFV CQDKSSGYHY GVSACEGCKG FFRRSIQKNM 130 140 150 160 170 180 VYTCHRDKNC IINKVTRNRC QYCRLQKCFD VGMSKESVRN DRNKKKKEAP KPECSESYTL 190 200 210 220 230 240 TPEVGELIEK VRKAHQETFP ALCQLGKYTT NNSSEQRVSL DIDLWDKFSE LSTKCIIKTV 250 260 270 280 290 300 EFAKQLPGFT TLTIADQITL LKAACLDILI LRICTRYTPE QDTMTFSDGL TLNRTQMHNA 310 320 330 340 350 360 GFGPLTDLVF AFANQLLPLE MDDAETGLLS AICLICGDRQ DLEQPDKVDM LQEPLLEALK 370 380 390 400 410 420 VYVRKRRPSR PHMFPKMLMK ITDLRSISAK GAERVITLKM EIPGSMPPLI QEMLENSEGL 430 440 450 460 DTLSGQSGGG TRDGGGLAPP PGSCSPSLSP SSHRSSPATQ SP
	Isoform Alpha-2 [UniParc]. Checksum: 15096242FF09896E	FASTA	459	50,935
	10 20 30 40 50 60 MYESVEVGGL TPAPNPFLVV DFYNQNRACL LQEKGLPAPG PYSTPLRTPL WNGSNHSIET 70 80 90 100 110 120 QSSSSEEIVP SPPSPPPLPR IYKPCFVCQD KSSGYHYGVS ACEGCKGFFR RSIQKNMVYT 130 140 150 160 170 180 CHRDKNCIIN KVTRNRCQYC RLQKCFDVGM SKESVRNDRN KKKKEAPKPE CSESYTLTPE 190 200 210 220 230 240 VGELIEKVRK AHQETFPALC QLGKYTTNNS SEQRVSLDID LWDKFSELST KCIIKTVEFA 250 260 270 280 290 300 KQLPGFTTLT IADQITLLKA ACLDILILRI CTRYTPEQDT MTFSDGLTLN RTQMHNAGFG 310 320 330 340 350 360 PLTDLVFAFA NQLLPLEMDD AETGLLSAIC LICGDRQDLE QPDKVDMLQE PLLEALKVYV 370 380 390 400 410 420 RKRRPSRPHM FPKMLMKITD LRSISAKGAE RVITLKMEIP GSMPPLIQEM LENSEGLDTL 430 440 450 SGQSGGGTRD GGGLAPPPGS CSPSLSPSSH RSSPATQSP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of murine alpha and beta retinoic acid receptors and a novel receptor gamma predominantly expressed in skin." Zelent A., Krust A., Petkovich M., Kastner P., Chambon P. Nature 339:714-717(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-1).
[2]	"Cloning of several genes coding for retinoic acid nuclear receptors in the mouse embryonal carcinoma cell line PCC7-MZ1." Heiermann R., Rentrop M., Lang E., Maelicke A. J. Recept. Res. 13:693-709(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-1).
[3]	"Multiple isoforms of the mouse retinoic acid receptor alpha are generated by alternative splicing and differential induction by retinoic acid." Leroy P., Krust A., Zelent A., Mendelsohn C., Garnier J.-M., Kastner P., Dierich A., Chambon P. EMBO J. 10:59-69(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA-1 AND ALPHA-2).
[4]	"Retinoic acid resistance of the variant embryonal carcinoma cell line RAC65 is caused by expression of a truncated RAR alpha." 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. Differentiation 49:27-37(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (VARIANT IN EMBRYONAL CARCINOMA CELL LINE RAC65).
[5]	"A dominant negative mutation of the alpha retinoic acid receptor gene in a retinoic acid-nonresponsive embryonal carcinoma cell." Pratt M.A.C., Kralova J., McBurney M.W. Mol. Cell. Biol. 10:6445-6453(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (VARIANT IN EMBRYONAL CARCINOMA CELL LINE RAC65).
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-1). Strain: FVB/N. Tissue: Mammary gland.
[7]	"Lysine trimethylation of retinoic acid receptor-alpha: a novel means to regulate receptor function." Huq M.D., Tsai N.-P., Khan S.A., Wei L.-N. Mol. Cell. Proteomics 6:677-688(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 340-359, METHYLATION AT LYS-347, FUNCTION, INTERACTION WITH RXRA AND NCOR1, MASS SPECTROMETRY, MUTAGENESIS OF LYS-347.
[8]	"Stimulation of RAR alpha activation function AF-1 through binding to the general transcription factor TFIIH and phosphorylation by CDK7." Rochette-Egly C., Adam S., Rossignol M., Egly J.-M., Chambon P. Cell 90:97-107(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CDK7 AND GTF2H3, PHOSPHORYLATION AT SER-77, FUNCTION, MUTAGENESIS OF SER-74; SER-77; SER-449; SER-456 AND SER-461.
[9]	"The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function." Torchia J., Rose D.W., Inostroza J., Kamei Y., Westin S., Glass C.K., Rosenfeld M.G. Nature 387:677-684(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NCOA3.
[10]	"Follicle-stimulating hormone inhibits all-trans-retinoic acid-induced retinoic acid receptor alpha nuclear localization and transcriptional activation in mouse Sertoli cell lines." Braun K.W., Tribley W.A., Griswold M.D., Kim K.H. J. Biol. Chem. 275:4145-4151(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]	"Isolation and characterization of peroxisome proliferator-activated receptor (PPAR) interacting protein (PRIP) as a coactivator for PPAR." Zhu Y.-J., Kan L., Qi C., Kanwar Y.S., Yeldandi A.V., Rao M.S., Reddy J.K. J. Biol. Chem. 275:13510-13516(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NCOA6.
[12]	"Positive regulation of retinoic acid receptor alpha by protein kinase C and mitogen-activated protein kinase in sertoli cells." Braun K.W., Vo M.N., Kim K.H. Biol. Reprod. 67:29-37(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION, SUBCELLULAR LOCATION.
[13]	"Male sterility in mice lacking retinoic acid receptor alpha involves specific abnormalities in spermiogenesis." Chung S.S., Wang X., Wolgemuth D.J. Differentiation 73:188-198(2005) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[14]	"Potential functions of retinoic acid receptor A in Sertoli cells and germ cells during spermatogenesis." Doyle T.J., Braun K.W., McLean D.J., Wright R.W., Griswold M.D., Kim K.H. Ann. N. Y. Acad. Sci. 1120:114-130(2007) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, INDUCTION.
[15]	"Retinoic acid receptors are required for skeletal growth, matrix homeostasis and growth plate function in postnatal mouse." 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. Dev. Biol. 328:315-327(2009) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[16]	"A coordinated phosphorylation cascade initiated by p38MAPK/MSK1 directs RARalpha to target promoters." Bruck N., Vitoux D., Ferry C., Duong V., Bauer A., de The H., Rochette-Egly C. EMBO J. 28:34-47(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-77 AND SER-369, FUNCTION, INTERACTION WITH GTF2H3, MUTAGENESIS OF SER-77 AND SER-369.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X56572 mRNA. Translation: CAA39919.1. X56565 mRNA. Translation: CAA39917.1. S56656 mRNA. Translation: AAB25783.1. X57528 mRNA. Translation: CAA40749.1. M60909 mRNA. Translation: AAA40031.1. BC010216 mRNA. Translation: AAH10216.1.
IPI	IPI00114447. IPI00223075.
PIR	S05050.
RefSeq	NP_001169999.1. NM_001176528.1. NP_001170773.1. NM_001177302.1. NP_001170774.1. NM_001177303.1. NP_033050.2. NM_009024.2.
UniGene	Mm.439744.
3D structure databases
ProteinModelPortal	P11416.
SMR	P11416. Positions 87-416.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-31480N.
IntAct	P11416. 7 interactions.
MINT	MINT-5210296.
PTM databases
PhosphoSite	P11416.
Proteomic databases
PRIDE	P11416.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000068133; ENSMUSP00000069744; ENSMUSG00000037992. ENSMUST00000107473; ENSMUSP00000103097; ENSMUSG00000037992. ENSMUST00000107474; ENSMUSP00000103098; ENSMUSG00000037992. ENSMUST00000107475; ENSMUSP00000103099; ENSMUSG00000037992. ENSMUST00000164748; ENSMUSP00000129791; ENSMUSG00000037992.
GeneID	19401.
KEGG	mmu:19401.
UCSC	uc007lhz.2. mouse.
Organism-specific databases
CTD	5914.
MGI	MGI:97856. Rara.
Phylogenomic databases
eggNOG	NOG297448.
GeneTree	ENSGT00680000099662.
HOGENOM	HOG000010312.
HOVERGEN	HBG005606.
InParanoid	P11416.
KO	K08527.
OMA	RTENVCI.
OrthoDB	EOG4F7NK7.
Gene expression databases
ArrayExpress	P11416.
Bgee	P11416.
CleanEx	MM_RARA.
Genevestigator	P11416.
GermOnline	ENSMUSG00000037992. Mus musculus.
Family and domain databases
Gene3D	1.10.565.10. 1 hit. 3.30.50.10. 1 hit.
InterPro	IPR008946. Nucl_hormone_rcpt_ligand-bd. IPR000536. Nucl_hrmn_rcpt_lig-bd_core. IPR003078. Retinoic_acid_rcpt. IPR001723. Str_hrmn_rcpt. IPR001628. Znf_hrmn_rcpt. IPR013088. Znf_NHR/GATA. [Graphical view]
Pfam	PF00104. Hormone_recep. 1 hit. PF00105. zf-C4. 1 hit. [Graphical view]
PRINTS	PR01292. RETNOICACIDR. PR00398. STRDHORMONER. PR00047. STROIDFINGER.
SMART	SM00430. HOLI. 1 hit. SM00399. ZnF_C4. 1 hit. [Graphical view]
SUPFAM	SSF48508. Str_ncl_receptor. 1 hit.
PROSITE	PS00031. NUCLEAR_REC_DBD_1. 1 hit. PS51030. NUCLEAR_REC_DBD_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P11416.
ChEMBL	CHEMBL2792.
NextBio	296513.
SOURCE	Search...

Entry information

Entry name

RARA_MOUSE

Accession

Primary (citable) accession number: P11416
Secondary accession number(s): P22603

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	May 1, 2013
This is version 151 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program