Retinoic acid receptor RXR-gamma - Mus musculus (Mouse)

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P28705 (RXRG_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 122. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Retinoic acid receptor RXR-gamma

Alternative name(s):
Nuclear receptor subfamily 2 group B member 3
Retinoid X receptor gamma

Gene names

Name:	Rxrg
Synonyms:	Nr2b3

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	463 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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. The high affinity ligand for RXRs is 9-cis retinoic acid By similarity.
Subunit structure	Homodimer By similarity Heterodimer with a RAR molecule By similarity. Binds DNA preferentially as a RAR/RXR heterodimer By similarity.
Subcellular location	Nucleus.
Developmental stage	Expressed from embryo day 10.5 to birth. At day 10-13, expression in somites and the ventral horns of the spinal chord. At day 13.5, strongly expressed in the corpus striatum. At day 16.5, expression also in the pituitary with weaker expression in the neck, skeletal muscle and tongue. Expression in the corpus striatum continues until at least 7 days after birth. Ref.1
Domain	Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.
Sequence similarities	Belongs to the nuclear hormone receptor family. NR2 subfamily. Contains 1 nuclear receptor DNA-binding domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Receptor
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	heart development Inferred from electronic annotation. Source: Compara neuron differentiation Inferred from electronic annotation. Source: Compara peripheral nervous system development Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from genetic interaction PubMed 7823919. Source: MGI regulation of myelination Inferred from electronic annotation. Source: Compara response to retinoic acid Inferred from electronic annotation. Source: Compara skeletal muscle tissue development Inferred from electronic annotation. Source: Compara
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	9-cis retinoic acid receptor activity Inferred from direct assay Ref.2. Source: MGI sequence-specific DNA binding Inferred from genetic interaction PubMed 7823919. Source: MGI steroid hormone receptor activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 463

463

Retinoic acid receptor RXR-gamma

PRO_0000053577

Regions

DNA binding

139 – 204

Nuclear receptor

Zinc finger

139 – 159

NR C4-type

Zinc finger

175 – 199

NR C4-type

Region

1 – 138

138

Modulating By similarity

Region

205 – 260

Hinge

Region

261 – 463

203

Ligand-binding By similarity

Experimental info

Sequence conflict

341

A → R in CAA46964. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P28705 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 1E29C86FACCE1DD9
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FASTA

463

50,893

        10         20         30         40         50         60 
MYGNYSHFMK FPTGFGGSPG HTGSTSMSPS VALPTGKPMD SHPSYTDTPV SAPRTLSAVG 

        70         80         90        100        110        120 
TPLNALGSPY RVITSAMGPP SGALAAPPGI NLVAPPSSQL NVVNSVSSSE DIKPLPGLPG 

       130        140        150        160        170        180 
IGNMNYPSTS PGSLVKHICA ICGDRSSGKH YGVYSCEGCK GFFKRTIRKD LIYTCRDNKD 

       190        200        210        220        230        240 
CLIDKRQRNR CQYCRYQKCL VMGMKREAVQ EERQRSRERA ESEAECASSS HEDMPVERIL 

       250        260        270        280        290        300 
EAELAVEPKT ESYGDMNVEN STNDPVTNIC HAADKQLFTL VEWAKRIPHF SDLTLEDQVI 

       310        320        330        340        350        360 
LLRAGWNELL IASFSHRSVS VQDGILLATG LHVHRSSAHS AGVGSIFDRV LTELVSKMKD 

       370        380        390        400        410        420 
MQMDKSELGC LRAIVLFNPD AKGLSNPSEV ETLREKVYAT LEAYTKQKYP EQPGRFAKLL 

       430        440        450        460 
LRLPALRSIG LKCLEHLFFF KLIGDTPIDS FLMEMLETPL QIT

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Purification, cloning, and RXR identity of the HeLa cell factor with which RAR or TR heterodimerizes to bind target sequences efficiently." Leid M., Kastner P., Lyons R., Nakshatri H., Saunders M., Zacharewsi T., Chen J.Y., Staub A., Garnier J.-M., Mader S., Chambon P. Cell 68:377-395(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
[2]	"Characterization of three RXR genes that mediate the action of 9-cis retinoic acid." Mangelsdorf D.J., Borgmeyer U., Heyman R.A., Zhou J.Y., Ong E.S., Oro A.E., Kakizuka A., Evans R.M. Genes Dev. 6:329-344(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The mouse retinoid-X receptor-gamma gene: genomic organization and evidence for functional isoforms." Liu Q., Linney E. Mol. Endocrinol. 7:651-658(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/10J. Tissue: Skeletal muscle.
[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]. Strain: C57BL/6. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M84819 mRNA. Translation: AAA40082.1. X66225 mRNA. Translation: CAA46964.1. S62948 mRNA. Translation: AAB27244.1. BC058401 mRNA. Translation: AAH58401.1.
IPI	IPI00124345.
PIR	B41727. S26670.
RefSeq	NP_001153203.1. NM_001159731.1. NP_033133.1. NM_009107.3.
UniGene	Mm.3475.
3D structure databases
ProteinModelPortal	P28705.
SMR	P28705. Positions 136-456.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000107017.
PTM databases
PhosphoSite	P28705.
Proteomic databases
PaxDb	P28705.
PRIDE	P28705.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000015987; ENSMUSP00000015987; ENSMUSG00000015843. ENSMUST00000111384; ENSMUSP00000107015; ENSMUSG00000015843. ENSMUST00000111386; ENSMUSP00000107017; ENSMUSG00000015843.
GeneID	20183.
KEGG	mmu:20183.
UCSC	uc007dla.2. mouse.
Organism-specific databases
CTD	6258.
MGI	MGI:98216. Rxrg.
Phylogenomic databases
eggNOG	NOG327099.
GeneTree	ENSGT00690000101777.
HOGENOM	HOG000260821.
HOVERGEN	HBG005606.
InParanoid	P28705.
KO	K08526.
OMA	FMKFPTG.
OrthoDB	EOG42RD7K.
Gene expression databases
ArrayExpress	P28705.
Bgee	P28705.
CleanEx	MM_RXRG.
Genevestigator	P28705.
GermOnline	ENSMUSG00000015843. Mus musculus.
Family and domain databases
Gene3D	1.10.565.10. 1 hit. 3.30.50.10. 1 hit.
InterPro	IPR021780. Nuc_recep-AF1. IPR008946. Nucl_hormone_rcpt_ligand-bd. IPR000536. Nucl_hrmn_rcpt_lig-bd_core. IPR000003. Retinoid-X_rcpt/HNF4. IPR001723. Str_hrmn_rcpt. IPR001628. Znf_hrmn_rcpt. IPR013088. Znf_NHR/GATA. [Graphical view]
Pfam	PF00104. Hormone_recep. 1 hit. PF11825. Nuc_recep-AF1. 1 hit. PF00105. zf-C4. 1 hit. [Graphical view]
PRINTS	PR00545. RETINOIDXR. 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	P28705.
ChEMBL	CHEMBL4402.
NextBio	297713.
SOURCE	Search...

Entry information

Entry name

RXRG_MOUSE

Accession

Primary (citable) accession number: P28705

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	February 1, 1996
Last modified:	April 3, 2013
This is version 122 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents