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P18911 (RARG_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Retinoic acid receptor gamma

Short name=RAR-gamma
Alternative name(s):
Nuclear receptor subfamily 1 group B member 3
Gene names
Name:Rarg
Synonyms:Nr1b3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length458 AA.
Sequence statusComplete.
Protein existenceEvidence 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 RAR/RXR 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, acts mainly as an activator of gene expression due to weak binding to corepressors By similarity. Required for limb bud development. In concert with RARA or RARB, required for skeletal growth, matrix homeostasis and growth plate function. Ref.6 Ref.8 Ref.9

Subunit structure

Homodimer By similarity. Heterodimer with a RXR molecule By similarity. Binds DNA preferentially as a RAR/RXR heterodimer By similarity. Forms a complex with PUS1 and the SRA1 RNA in the nucleus. Ref.7

Subcellular location

Nucleus Ref.7.

Developmental stage

In E9.5-E12.5 embryos, expression throughout limb bud mesenchyme. This expression overlaps with that of CYP26B1. Also strongly expressed in the caudal and craniofacial regions. Ref.9

Domain

Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.

Disruption phenotype

Rarg and Rarb double null mice exhibit growth retardation 3 weeks after birth. 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. Isoform 2 mutants appear normal. The Rarg and Cyp26b1 double null mutation is able to partially rescue limb skeletal morphology without restoring normal expression of proximo-distal patterning genes. Ref.6 Ref.8 Ref.9

Sequence similarities

Belongs to the nuclear hormone receptor family. NR1 subfamily.

Contains 1 nuclear receptor DNA-binding domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionReceptor
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processHarderian gland development

Inferred from mutant phenotype Ref.6. Source: MGI

anterior/posterior pattern specification

Inferred from mutant phenotype PubMed 11784046Ref.6. Source: MGI

bone development

Inferred from mutant phenotype Ref.8. Source: UniProtKB

bone morphogenesis

Inferred from mutant phenotype PubMed 11784046Ref.6. Source: MGI

cellular response to retinoic acid

Inferred from electronic annotation. Source: Ensembl

chondrocyte development

Inferred from mutant phenotype Ref.8. Source: UniProtKB

embryonic eye morphogenesis

Inferred from genetic interaction PubMed 16207763. Source: MGI

embryonic hindlimb morphogenesis

Inferred from genetic interaction PubMed 10075839. Source: MGI

epithelium development

Inferred from mutant phenotype Ref.6. Source: MGI

gland development

Inferred from mutant phenotype Ref.6. Source: MGI

growth plate cartilage chondrocyte growth

Inferred from mutant phenotype Ref.8. Source: UniProtKB

growth plate cartilage development

Inferred from genetic interaction Ref.8. Source: MGI

limb development

Inferred from mutant phenotype Ref.8. Source: UniProtKB

multicellular organism growth

Inferred from genetic interaction Ref.8. 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 cell proliferation

Inferred from genetic interaction PubMed 10075839. Source: MGI

negative regulation of chondrocyte differentiation

Inferred from mutant phenotype PubMed 10684250. Source: MGI

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 8152920. Source: MGI

positive regulation of apoptotic process

Inferred from genetic interaction PubMed 16207763. Source: MGI

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of gene expression

Inferred from direct assay Ref.8. Source: MGI

positive regulation of programmed cell death

Inferred from genetic interaction PubMed 10075839. Source: MGI

positive regulation of transcription from RNA polymerase II promoter

Inferred by curator PubMed 18439490. Source: BHF-UCL

prostate gland epithelium morphogenesis

Inferred from mutant phenotype Ref.6. Source: MGI

regulation of gene expression

Inferred from genetic interaction Ref.8. Source: MGI

regulation of myelination

Inferred from electronic annotation. Source: Ensembl

reproductive structure development

Inferred from mutant phenotype Ref.6. Source: MGI

retinoic acid receptor signaling pathway

Inferred from mutant phenotype Ref.6. Source: MGI

trachea cartilage development

Inferred from mutant phenotype Ref.6PubMed 9376317. Source: MGI

   Cellular_componentnucleus

Inferred from direct assay Ref.7PubMed 1655807. Source: MGI

transcription factor complex

Inferred from direct assay PubMed 18439490. Source: BHF-UCL

   Molecular_functionDNA binding

Inferred by curator PubMed 18439490. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.7Ref.8. Source: MGI

retinoic acid receptor activity

Inferred from electronic annotation. Source: Ensembl

retinoid X receptor binding

Inferred from mutant phenotype PubMed 18439490. Source: BHF-UCL

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 18439490. Source: BHF-UCL

steroid hormone receptor activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P18911-1)

Also known as: A;

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 2 (identifier: P18911-2)

Also known as: B;

The sequence of this isoform differs from the canonical sequence as follows:
     1-61: MATNKERLFA...PDLPKEMASL → MYDCMESFVP...FAWAQPASLQ
Isoform 3 (identifier: P18911-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-62: MATNKERLFA...DLPKEMASLS → MHKGDNSGHQ...LSSHAAFHSA

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 458458Retinoic acid receptor gamma
PRO_0000053474

Regions

DNA binding90 – 15566Nuclear receptor
Zinc finger90 – 11021NR C4-type
Zinc finger126 – 15025NR C4-type
Region1 – 8989Modulating
Region156 – 20146Hinge
Region202 – 421220Ligand-binding

Natural variations

Alternative sequence1 – 6262MATNK…MASLS → MHKGDNSGHQQVPRKRGHGM RVLLLSFCLSSHAAFHSA in isoform 3.
VSP_031081
Alternative sequence1 – 6161MATNK…EMASL → MYDCMESFVPGPRRLYGAAG PGAGLLRRATGSSCFAGLES FAWAQPASLQ in isoform 2.
VSP_031082

Experimental info

Sequence conflict631V → E in BAE28323. Ref.3
Sequence conflict781P → A in BAE28323. Ref.3
Sequence conflict1761S → L in AAH13709. Ref.4
Sequence conflict369 – 3724RPSQ → DPAK in AAA40035. Ref.2
Sequence conflict369 – 3724RPSQ → DPAK in AAA40036. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (A) [UniParc].

Last modified February 5, 2008. Version 3.
Checksum: 1D13D2F1482D7194

FASTA45850,891
        10         20         30         40         50         60 
MATNKERLFA PGALGPGSGY PGAGFPFAFP GALRGSPPFE MLSPSFRGLG QPDLPKEMAS 

        70         80         90        100        110        120 
LSVETQSTSS EEMVPSSPSP PPPPRVYKPC FVCNDKSSGY HYGVSSCEGC KGFFRRSIQK 

       130        140        150        160        170        180 
NMVYTCHRDK NCIINKVTRN RCQYCRLQKC FEVGMSKEAV RNDRNKKKKE VKEEGSPDSY 

       190        200        210        220        230        240 
ELSPQLEELI TKVSKAHQET FPSLCQLGKY TTNSSADHRV QLDLGLWDKF SELATKCIIK 

       250        260        270        280        290        300 
IVEFAKRLPG FTGLSIADQI TLLKAACLDI LMLRICTRYT PEQDTMTFSD GLTLNRTQMH 

       310        320        330        340        350        360 
NAGFGPLTDL VFAFAGQLLP LEMDDTETGL LSAICLICGD RMDLEEPEKV DKLQEPLLEA 

       370        380        390        400        410        420 
LRLYARRRRP SQPYMFPRML MKITDLRGIS TKGAERAITL KMEIPGPMPP LIREMLENPE 

       430        440        450 
MFEDDSSKPG PHPKASSEDE APGGQGKRGQ SPQPDQGP 

« Hide

Isoform 2 (B) [UniParc] [UniParc].

Checksum: 75E0BCB50BC9AD3B
Show »

FASTA44749,849
Isoform 3 [UniParc].

Checksum: D0885E92CB7B2966
Show »

FASTA43448,708

References

« Hide '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 1), TISSUE SPECIFICITY.
[2]"Identification of a novel isoform of the retinoic acid receptor gamma expressed in the mouse embryo."
Giguere V., Shago M., Zirngibl R., Tate P., Rossant J., Varmuza S.
Mol. Cell. Biol. 10:2335-2340(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
[4]"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 1).
Strain: Czech II.
Tissue: Mammary tumor.
[5]"Murine isoforms of retinoic acid receptor gamma with specific patterns of expression."
Kastner P., Krust A., Mendelsohn C., Garnier J.-M., Zelent A., Leroy P., Staub A., Chambon P.
Proc. Natl. Acad. Sci. U.S.A. 87:2700-2704(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-74 (ISOFORMS 1; 2 AND 3).
[6]"Function of retinoic acid receptor gamma in the mouse."
Lohnes D., Kastner P., Dierich A., Mark M., LeMeur M., Chambon P.
Cell 73:643-658(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[7]"Regulation of nuclear receptor activity by a pseudouridine synthase through posttranscriptional modification of steroid receptor RNA activator."
Zhao X., Patton J.R., Davis S.L., Florence B., Ames S.J., Spanjaard R.A.
Mol. Cell 15:549-558(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH PUS1 AND SRA1, SUBCELLULAR LOCATION.
[8]"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.
[9]"Analysis of Cyp26b1/Rarg compound-null mice reveals two genetically separable effects of retinoic acid on limb outgrowth."
Pennimpede T., Cameron D.A., MacLean G.A., Petkovich M.
Dev. Biol. 339:179-186(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, POSSIBLE FUNCTION, DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X15848 mRNA. Translation: CAA33845.1.
M34475 mRNA. Translation: AAA40036.1.
M34476 mRNA. Translation: AAA40035.1.
AK148064 mRNA. Translation: BAE28323.1.
BC012923 mRNA. Translation: AAH12923.1.
BC013709 mRNA. Translation: AAH13709.1.
M32068 mRNA. Translation: AAA40032.1.
M32069 mRNA. Translation: AAA40033.1.
M32070 mRNA. Translation: AAA40034.1.
CCDSCCDS27875.1. [P18911-1]
CCDS37226.1. [P18911-2]
PIRB34714.
A34714. S05052.
RefSeqNP_001036192.1. NM_001042727.2. [P18911-2]
NP_035374.3. NM_011244.4. [P18911-1]
XP_006520712.1. XM_006520649.1. [P18911-1]
XP_006520713.1. XM_006520650.1. [P18911-1]
UniGeneMm.1273.

3D structure databases

ProteinModelPortalP18911.
SMRP18911. Positions 89-419.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202595. 4 interactions.
DIPDIP-42822N.
IntActP18911. 1 interaction.
MINTMINT-2834553.

Chemistry

BindingDBP18911.
ChEMBLCHEMBL4177.
GuidetoPHARMACOLOGY592.

PTM databases

PhosphoSiteP18911.

Proteomic databases

PRIDEP18911.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000043172; ENSMUSP00000048838; ENSMUSG00000001288. [P18911-1]
ENSMUST00000063339; ENSMUSP00000067266; ENSMUSG00000001288. [P18911-2]
GeneID19411.
KEGGmmu:19411.
UCSCuc007xvc.1. mouse. [P18911-2]
uc007xvd.1. mouse. [P18911-1]

Organism-specific databases

CTD5916.
MGIMGI:97858. Rarg.

Phylogenomic databases

eggNOGNOG297448.
GeneTreeENSGT00740000114969.
HOGENOMHOG000010312.
HOVERGENHBG005606.
InParanoidP18911.
KOK08529.
OMARSPQPDQ.
OrthoDBEOG738053.
PhylomeDBP18911.
TreeFamTF328382.

Gene expression databases

ArrayExpressP18911.
BgeeP18911.
CleanExMM_RARG.
GenevestigatorP18911.

Family and domain databases

Gene3D1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProIPR008946. 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]
PfamPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSPR01292. RETNOICACIDR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMSSF48508. SSF48508. 1 hit.
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio296533.
PROP18911.
SOURCESearch...

Entry information

Entry nameRARG_MOUSE
AccessionPrimary (citable) accession number: P18911
Secondary accession number(s): P20787 expand/collapse secondary AC list , Q3UG86, Q62149, Q91VK5, Q91YX2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: February 5, 2008
Last modified: July 9, 2014
This is version 151 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot