RXRG_RAT
ID RXRG_RAT Reviewed; 463 AA.
AC Q5BJR8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 135.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 [2]
RP TISSUE SPECIFICITY.
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 TISSUE SPECIFICITY.
RX PubMed=28267642; DOI=10.1016/j.jsbmb.2017.03.002;
RA Cheng B., Al-Shammari F.H., Ghader I.A., Sequeira F., Thakkar J.,
RA Mathew T.C.;
RT "Fundamental studies of adrenal retinoid-X-receptor: Protein isoform,
RT tissue expression, subcellular distribution, and ligand availability.";
RL J. Steroid Biochem. Mol. Biol. 171:110-120(2017).
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,
CC ECO:0000255|PROSITE-ProRule:PRU00407}. Cytoplasm
CC {ECO:0000250|UniProtKB:P48443}.
CC -!- TISSUE SPECIFICITY: Expressed in the liver, but not detected in the
CC adrenal gland (at protein level) (PubMed:28267642). Restricted
CC expression in adrenal gland, kidney, liver, brain and lungs
CC (PubMed:1312497). Strong expression in heart and muscles
CC (PubMed:1312497). {ECO:0000269|PubMed:1312497,
CC ECO:0000269|PubMed:28267642}.
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 -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
CC subfamily. {ECO:0000305}.
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DR EMBL; BC091363; AAH91363.1; -; mRNA.
DR RefSeq; NP_113953.1; NM_031765.1.
DR AlphaFoldDB; Q5BJR8; -.
DR SMR; Q5BJR8; -.
DR STRING; 10116.ENSRNOP00000006117; -.
DR BindingDB; Q5BJR8; -.
DR ChEMBL; CHEMBL4277; -.
DR PhosphoSitePlus; Q5BJR8; -.
DR PaxDb; Q5BJR8; -.
DR PRIDE; Q5BJR8; -.
DR GeneID; 83574; -.
DR KEGG; rno:83574; -.
DR UCSC; RGD:620046; rat.
DR CTD; 6258; -.
DR RGD; 620046; Rxrg.
DR VEuPathDB; HostDB:ENSRNOG00000004537; -.
DR eggNOG; KOG3575; Eukaryota.
DR HOGENOM; CLU_007368_5_4_1; -.
DR InParanoid; Q5BJR8; -.
DR OrthoDB; 912470at2759; -.
DR PhylomeDB; Q5BJR8; -.
DR TreeFam; TF352097; -.
DR Reactome; R-RNO-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-RNO-5362517; Signaling by Retinoic Acid.
DR PRO; PR:Q5BJR8; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000004537; Expressed in skeletal muscle tissue and 19 other tissues.
DR ExpressionAtlas; Q5BJR8; baseline and differential.
DR Genevisible; Q5BJR8; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
DR GO; GO:0004879; F:nuclear receptor activity; ISO:RGD.
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; ISO:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
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:0032870; P:cellular response to hormone stimulus; IEP:RGD.
DR GO; GO:0007507; P:heart development; IEP:RGD.
DR GO; GO:0030182; P:neuron differentiation; IEP:RGD.
DR GO; GO:0007422; P:peripheral nervous system development; IEP:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:1901522; P:positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus; ISO:RGD.
DR GO; GO:0031641; P:regulation of myelination; IDA:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
DR GO; GO:0048384; P:retinoic acid receptor signaling pathway; ISO:RGD.
DR GO; GO:0007519; P:skeletal muscle tissue development; IEP:RGD.
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 1: Evidence at protein 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_0000317032"
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 COMPBIAS 18..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 463 AA; 50893 MW; 1D3A6607A068C837 CRC64;
MYGNYSHFMK FPTGFGGSPG HTGSTSMSPS VALPTGKPMD SHPSYTDTPV SAPRTLSAVG
TPLNALGSPY RVITSAMGPP SGALAAPPGI NLVVPPSSQL NVVNSVSSSE DIKPLPGLPG
IGNMNYPSTS PGSLVKHICA ICGDRSSGKH YGVYSCEGCK GFFKRTIRKD LIYTCRDNKD
CLIDKRQRNR CQYCRYQKCL VMGMKREAVQ EERQRSRERA ESEAECASTG HEDMPVERIL
EAELAVEPKT ESYGDMSVES STNDPVTNIC HAADKQLFTL VEWAKRIPHF SDLTLEDQVI
LLRAGWNELL IASFSHRSVS VQDGILLATG LHVHRSSAHS AGVGSIFDRV LTELVSKMKD
MRMDKSELGC LRAIVLFNPD AKGLSNPSEV ETLREKVYAT LEAYTKQKYP EQPGRFAKLL
LRLPALRSIG LKCLEHLFFF KLIGDTPIDT FLMEMLETPL QIT
