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   27-MAR-2024, entry version 191.
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   GlyGen; P28705; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P28705; -.
DR   PhosphoSitePlus; P28705; -.
DR   MaxQB; P28705; -.
DR   PaxDb; 10090-ENSMUSP00000015987; -.
DR   ProteomicsDB; 256553; -.
DR   Antibodypedia; 3620; 437 antibodies from 43 providers.
DR   DNASU; 20183; -.
DR   Ensembl; ENSMUST00000015987.10; ENSMUSP00000015987.4; ENSMUSG00000015843.11.
DR   Ensembl; ENSMUST00000111384.8; ENSMUSP00000107015.2; ENSMUSG00000015843.11.
DR   Ensembl; ENSMUST00000111386.8; ENSMUSP00000107017.2; ENSMUSG00000015843.11.
DR   GeneID; 20183; -.
DR   KEGG; mmu:20183; -.
DR   UCSC; uc007dla.2; mouse.
DR   AGR; MGI:98216; -.
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; MDSHASY; -.
DR   OrthoDB; 5400963at2759; -.
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; 4 hits in 82 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 177 other cell types or tissues.
DR   ExpressionAtlas; P28705; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
DR   GO; GO:0140693; F:molecular condensate scaffold activity; ISO:MGI.
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: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: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:0032526; P:response to retinoic acid; IBA:GO_Central.
DR   GO; GO:0048384; P:retinoic acid receptor signaling pathway; IDA:MGI.
DR   CDD; cd06956; NR_DBD_RXR; 1.
DR   CDD; cd06943; NR_LBD_RXR_like; 1.
DR   Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1.
DR   Gene3D; 1.10.565.10; Retinoid X Receptor; 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   PANTHER; PTHR24083; NUCLEAR HORMONE RECEPTOR; 1.
DR   PANTHER; PTHR24083:SF100; RETINOIC ACID RECEPTOR RXR-GAMMA; 1.
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; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   SUPFAM; SSF48508; Nuclear receptor ligand-binding domain; 1.
DR   PROSITE; PS51843; NR_LBD; 1.
DR   PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR   PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
DR   Genevisible; P28705; MM.
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
//