RXRG_MOUSE
ID RXRG_MOUSE Reviewed; 463 AA.
AC P28705;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Retinoic acid receptor RXR-gamma;
DE AltName: Full=Nuclear receptor subfamily 2 group B member 3;
DE AltName: Full=Retinoid X receptor gamma;
GN Name=Rxrg; Synonyms=Nr2b3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=1310259; DOI=10.1016/0092-8674(92)90478-u;
RA Leid M., Kastner P., Lyons R., Nakshatri H., Saunders M., Zacharewsi T.,
RA Chen J.Y., Staub A., Garnier J.-M., Mader S., Chambon P.;
RT "Purification, cloning, and RXR identity of the HeLa cell factor with which
RT RAR or TR heterodimerizes to bind target sequences efficiently.";
RL Cell 68:377-395(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1312497; DOI=10.1101/gad.6.3.329;
RA Mangelsdorf D.J., Borgmeyer U., Heyman R.A., Zhou J.Y., Ong E.S., Oro A.E.,
RA Kakizuka A., Evans R.M.;
RT "Characterization of three RXR genes that mediate the action of 9-cis
RT retinoic acid.";
RL Genes Dev. 6:329-344(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/10J; TISSUE=Skeletal muscle;
RX PubMed=8391126; DOI=10.1210/mend.7.5.8391126;
RA Liu Q., Linney E.;
RT "The mouse retinoid-X receptor-gamma gene: genomic organization and
RT evidence for functional isoforms.";
RL Mol. Endocrinol. 7:651-658(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=26030625; DOI=10.1371/journal.pgen.1005213;
RA Ruehl R., Krzyzosiak A., Niewiadomska-Cimicka A., Rochel N., Szeles L.,
RA Vaz B., Wietrzych-Schindler M., Alvarez S., Szklenar M., Nagy L.,
RA de Lera A.R., Krezel W.;
RT "9-cis-13,14-Dihydroretinoic Acid Is an Endogenous Retinoid Acting as RXR
RT Ligand in Mice.";
RL PLoS Genet. 11:E1005213-E1005213(2015).
CC -!- FUNCTION: Receptor for retinoic acid. Retinoic acid receptors bind as
CC heterodimers to their target response elements in response to their
CC ligands, all-trans or 9-cis retinoic acid, and regulate gene expression
CC in various biological processes. The RAR/RXR heterodimers bind to the
CC retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3'
CC sites known as DR1-DR5. The high affinity ligand for RXRs is 9-cis
CC retinoic acid (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer (By similarity). Heterodimer with a RAR molecule (By
CC similarity). Binds DNA preferentially as a RAR/RXR heterodimer (By
CC similarity). Interacts with RARA (By similarity).
CC {ECO:0000250|UniProtKB:P19793, ECO:0000250|UniProtKB:P48443}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P48443}. Cytoplasm
CC {ECO:0000250|UniProtKB:P48443}.
CC -!- DEVELOPMENTAL STAGE: Expressed from embryo day 10.5 to birth. At day
CC 10-13, expression in somites and the ventral horns of the spinal chord.
CC At day 13.5, strongly expressed in the corpus striatum. At day 16.5,
CC expression also in the pituitary with weaker expression in the neck,
CC skeletal muscle and tongue. Expression in the corpus striatum continues
CC until at least 7 days after birth. {ECO:0000269|PubMed:1310259}.
CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC DNA-binding domain and a C-terminal ligand-binding domain.
CC -!- PTM: Acetylated by EP300. {ECO:0000250|UniProtKB:P48443}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice exhibit memory deficits.
CC {ECO:0000269|PubMed:26030625}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
CC subfamily. {ECO:0000305}.
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DR EMBL; M84819; AAA40082.1; -; mRNA.
DR EMBL; X66225; CAA46964.1; -; mRNA.
DR EMBL; S62948; AAB27244.1; -; mRNA.
DR EMBL; BC058401; AAH58401.1; -; mRNA.
DR CCDS; CCDS15459.1; -.
DR PIR; B41727; B41727.
DR PIR; S26670; S26670.
DR RefSeq; NP_001153203.1; NM_001159731.1.
DR RefSeq; NP_033133.1; NM_009107.3.
DR AlphaFoldDB; P28705; -.
DR SMR; P28705; -.
DR BioGRID; 203040; 12.
DR IntAct; P28705; 8.
DR STRING; 10090.ENSMUSP00000015987; -.
DR BindingDB; P28705; -.
DR ChEMBL; CHEMBL4402; -.
DR DrugCentral; P28705; -.
DR GuidetoPHARMACOLOGY; 612; -.
DR iPTMnet; P28705; -.
DR PhosphoSitePlus; P28705; -.
DR MaxQB; P28705; -.
DR PaxDb; P28705; -.
DR PRIDE; P28705; -.
DR ProteomicsDB; 256553; -.
DR Antibodypedia; 3620; 412 antibodies from 43 providers.
DR DNASU; 20183; -.
DR Ensembl; ENSMUST00000015987; ENSMUSP00000015987; ENSMUSG00000015843.
DR Ensembl; ENSMUST00000111384; ENSMUSP00000107015; ENSMUSG00000015843.
DR Ensembl; ENSMUST00000111386; ENSMUSP00000107017; ENSMUSG00000015843.
DR GeneID; 20183; -.
DR KEGG; mmu:20183; -.
DR UCSC; uc007dla.2; mouse.
DR CTD; 6258; -.
DR MGI; MGI:98216; Rxrg.
DR VEuPathDB; HostDB:ENSMUSG00000015843; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000161269; -.
DR HOGENOM; CLU_007368_5_4_1; -.
DR InParanoid; P28705; -.
DR OMA; YGDVNME; -.
DR OrthoDB; 912470at2759; -.
DR PhylomeDB; P28705; -.
DR TreeFam; TF352097; -.
DR Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-MMU-5362517; Signaling by Retinoic Acid.
DR BioGRID-ORCS; 20183; 3 hits in 77 CRISPR screens.
DR PRO; PR:P28705; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P28705; protein.
DR Bgee; ENSMUSG00000015843; Expressed in lumbar dorsal root ganglion and 174 other tissues.
DR ExpressionAtlas; P28705; baseline and differential.
DR Genevisible; P28705; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
DR GO; GO:0004879; F:nuclear receptor activity; IDA:MGI.
DR GO; GO:0003707; F:nuclear steroid receptor activity; IEA:InterPro.
DR GO; GO:0044323; F:retinoic acid-responsive element binding; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IGI:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR GO; GO:0007422; P:peripheral nervous system development; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0031641; P:regulation of myelination; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0032526; P:response to retinoic acid; IBA:GO_Central.
DR GO; GO:0048384; P:retinoic acid receptor signaling pathway; IDA:MGI.
DR GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR021780; Nuc_recep-AF1.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR000003; Retinoid-X_rcpt/HNF4.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF11825; Nuc_recep-AF1; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR00545; RETINOIDXR.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; DNA-binding; Metal-binding; Nucleus; Receptor;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..463
FT /note="Retinoic acid receptor RXR-gamma"
FT /id="PRO_0000053577"
FT DOMAIN 231..459
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 139..204
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 139..159
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 175..199
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..138
FT /note="Modulating"
FT /evidence="ECO:0000250"
FT REGION 16..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..230
FT /note="Hinge"
FT REGION 211..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 341
FT /note="A -> R (in Ref. 2; CAA46964)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 463 AA; 50893 MW; 1E29C86FACCE1DD9 CRC64;
MYGNYSHFMK FPTGFGGSPG HTGSTSMSPS VALPTGKPMD SHPSYTDTPV SAPRTLSAVG
TPLNALGSPY RVITSAMGPP SGALAAPPGI NLVAPPSSQL NVVNSVSSSE DIKPLPGLPG
IGNMNYPSTS PGSLVKHICA ICGDRSSGKH YGVYSCEGCK GFFKRTIRKD LIYTCRDNKD
CLIDKRQRNR CQYCRYQKCL VMGMKREAVQ EERQRSRERA ESEAECASSS HEDMPVERIL
EAELAVEPKT ESYGDMNVEN STNDPVTNIC HAADKQLFTL VEWAKRIPHF SDLTLEDQVI
LLRAGWNELL IASFSHRSVS VQDGILLATG LHVHRSSAHS AGVGSIFDRV LTELVSKMKD
MQMDKSELGC LRAIVLFNPD AKGLSNPSEV ETLREKVYAT LEAYTKQKYP EQPGRFAKLL
LRLPALRSIG LKCLEHLFFF KLIGDTPIDS FLMEMLETPL QIT
