RXRG_HUMAN
ID RXRG_HUMAN Reviewed; 463 AA.
AC P48443; A6NIP1; Q6IBU7;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 209.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RA Cooke T.A., Allegretto E.A., Heyman R.A., Lamph W.W.;
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [6]
RP ACETYLATION BY EP300.
RX PubMed=17761950; DOI=10.1210/me.2007-0107;
RA Zhao W.X., Tian M., Zhao B.X., Li G.D., Liu B., Zhan Y.Y., Chen H.Z.,
RA Wu Q.;
RT "Orphan receptor TR3 attenuates the p300-induced acetylation of retinoid X
RT receptor-alpha.";
RL Mol. Endocrinol. 21:2877-2889(2007).
RN [7]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH RARA.
RX PubMed=28167758; DOI=10.1073/pnas.1621425114;
RA Lee D.Y., Lin T.E., Lee C.I., Zhou J., Huang Y.H., Lee P.L., Shih Y.T.,
RA Chien S., Chiu J.J.;
RT "MicroRNA-10a is crucial for endothelial response to different flow
RT patterns via interaction of retinoid acid receptors and histone
RT deacetylases.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:2072-2077(2017).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 227-463.
RG Structural genomics consortium (SGC);
RT "Human retinoic acid receptor Rxr-gamma ligand-binding domain.";
RL Submitted (APR-2006) to the PDB data bank.
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
CC (PubMed:28167758). Binds DNA preferentially as a RAR/RXR heterodimer
CC (PubMed:28167758). Interacts with RARA (PubMed:28167758).
CC {ECO:0000250|UniProtKB:P19793, ECO:0000269|PubMed:28167758}.
CC -!- INTERACTION:
CC P48443; P12532: CKMT1B; NbExp=5; IntAct=EBI-712405, EBI-1050662;
CC P48443; P02489: CRYAA; NbExp=3; IntAct=EBI-712405, EBI-6875961;
CC P48443; G5E9A7: DMWD; NbExp=3; IntAct=EBI-712405, EBI-10976677;
CC P48443; Q14204: DYNC1H1; NbExp=3; IntAct=EBI-712405, EBI-356015;
CC P48443; O14908-2: GIPC1; NbExp=3; IntAct=EBI-712405, EBI-25913156;
CC P48443; P42858: HTT; NbExp=18; IntAct=EBI-712405, EBI-466029;
CC P48443; Q15777: MPPED2; NbExp=6; IntAct=EBI-712405, EBI-2350461;
CC P48443; F1D8P7: NR1H2; NbExp=14; IntAct=EBI-712405, EBI-10177172;
CC P48443; P55055: NR1H2; NbExp=5; IntAct=EBI-712405, EBI-745354;
CC P48443; Q13133: NR1H3; NbExp=7; IntAct=EBI-712405, EBI-781356;
CC P48443; Q13133-3: NR1H3; NbExp=11; IntAct=EBI-712405, EBI-11952806;
CC P48443; Q96RI1-1: NR1H4; NbExp=3; IntAct=EBI-712405, EBI-12417284;
CC P48443; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-712405, EBI-79165;
CC P48443; P10276: RARA; NbExp=18; IntAct=EBI-712405, EBI-413374;
CC P48443; P10276-2: RARA; NbExp=6; IntAct=EBI-712405, EBI-10197061;
CC P48443; P10826-2: RARB; NbExp=7; IntAct=EBI-712405, EBI-8583223;
CC P48443; P13631: RARG; NbExp=5; IntAct=EBI-712405, EBI-2568901;
CC P48443; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-712405, EBI-5235340;
CC P48443; Q86WV8: TSC1; NbExp=3; IntAct=EBI-712405, EBI-12806590;
CC P48443; P11473-2: VDR; NbExp=4; IntAct=EBI-712405, EBI-12874016;
CC P48443; Q91XC0: Ajuba; Xeno; NbExp=2; IntAct=EBI-712405, EBI-1565930;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407,
CC ECO:0000269|PubMed:28167758}. Cytoplasm {ECO:0000269|PubMed:28167758}.
CC -!- TISSUE SPECIFICITY: Expressed in aortic endothelial cells (at protein
CC level). {ECO:0000269|PubMed:28167758}.
CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC DNA-binding domain and a C-terminal ligand-binding domain.
CC {ECO:0000250}.
CC -!- PTM: Acetylated by EP300. {ECO:0000269|PubMed:17761950}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U38480; AAA80681.1; -; mRNA.
DR EMBL; CR456705; CAG32986.1; -; mRNA.
DR EMBL; AL160058; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW90745.1; -; Genomic_DNA.
DR EMBL; BC012063; AAH12063.1; -; mRNA.
DR CCDS; CCDS1248.1; -.
DR RefSeq; NP_001243500.1; NM_001256571.1.
DR RefSeq; NP_008848.1; NM_006917.4.
DR PDB; 2GL8; X-ray; 2.40 A; A/B/C/D=227-463.
DR PDB; 7A79; X-ray; 2.05 A; A/B=233-463.
DR PDBsum; 2GL8; -.
DR PDBsum; 7A79; -.
DR AlphaFoldDB; P48443; -.
DR SMR; P48443; -.
DR BioGRID; 112170; 35.
DR DIP; DIP-56220N; -.
DR IntAct; P48443; 32.
DR MINT; P48443; -.
DR STRING; 9606.ENSP00000352900; -.
DR BindingDB; P48443; -.
DR ChEMBL; CHEMBL2004; -.
DR DrugBank; DB00459; Acitretin.
DR DrugBank; DB00210; Adapalene.
DR DrugBank; DB00523; Alitretinoin.
DR DrugBank; DB00307; Bexarotene.
DR DrugBank; DB01393; Bezafibrate.
DR DrugBank; DB03756; Doconexent.
DR DrugBank; DB00926; Etretinate.
DR DrugBank; DB02746; Phthalic Acid.
DR DrugBank; DB00412; Rosiglitazone.
DR DrugBank; DB00755; Tretinoin.
DR DrugCentral; P48443; -.
DR GuidetoPHARMACOLOGY; 612; -.
DR GlyGen; P48443; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P48443; -.
DR PhosphoSitePlus; P48443; -.
DR BioMuta; RXRG; -.
DR DMDM; 1350913; -.
DR jPOST; P48443; -.
DR MassIVE; P48443; -.
DR MaxQB; P48443; -.
DR PaxDb; P48443; -.
DR PeptideAtlas; P48443; -.
DR PRIDE; P48443; -.
DR ProteomicsDB; 55890; -.
DR Antibodypedia; 3620; 412 antibodies from 43 providers.
DR DNASU; 6258; -.
DR Ensembl; ENST00000359842.10; ENSP00000352900.5; ENSG00000143171.13.
DR GeneID; 6258; -.
DR KEGG; hsa:6258; -.
DR MANE-Select; ENST00000359842.10; ENSP00000352900.5; NM_006917.5; NP_008848.1.
DR UCSC; uc001gda.4; human.
DR CTD; 6258; -.
DR DisGeNET; 6258; -.
DR GeneCards; RXRG; -.
DR HGNC; HGNC:10479; RXRG.
DR HPA; ENSG00000143171; Tissue enhanced (brain, pituitary gland, retina, skeletal muscle).
DR MIM; 180247; gene.
DR neXtProt; NX_P48443; -.
DR OpenTargets; ENSG00000143171; -.
DR PharmGKB; PA34892; -.
DR VEuPathDB; HostDB:ENSG00000143171; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000161269; -.
DR HOGENOM; CLU_007368_5_4_1; -.
DR InParanoid; P48443; -.
DR OMA; YGDVNME; -.
DR OrthoDB; 912470at2759; -.
DR PhylomeDB; P48443; -.
DR TreeFam; TF352097; -.
DR PathwayCommons; P48443; -.
DR Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-HSA-5362517; Signaling by Retinoic Acid.
DR SignaLink; P48443; -.
DR SIGNOR; P48443; -.
DR BioGRID-ORCS; 6258; 12 hits in 1094 CRISPR screens.
DR ChiTaRS; RXRG; human.
DR EvolutionaryTrace; P48443; -.
DR GeneWiki; Retinoid_X_receptor_gamma; -.
DR GenomeRNAi; 6258; -.
DR Pharos; P48443; Tclin.
DR PRO; PR:P48443; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P48443; protein.
DR Bgee; ENSG00000143171; Expressed in hindlimb stylopod muscle and 109 other tissues.
DR ExpressionAtlas; P48443; baseline and differential.
DR Genevisible; P48443; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central.
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:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
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; IBA:GO_Central.
DR GO; GO:0031641; P:regulation of myelination; IEA:Ensembl.
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; IBA:GO_Central.
DR GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl.
DR DisProt; DP02915; -.
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 3D-structure; Acetylation; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW Receptor; Reference proteome; Transcription; Transcription regulation;
KW Zinc; Zinc-finger.
FT CHAIN 1..463
FT /note="Retinoic acid receptor RXR-gamma"
FT /id="PRO_0000053576"
FT DOMAIN 231..459
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 136..211
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 18..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..230
FT /note="Hinge"
FT COMPBIAS 19..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 236..245
FT /evidence="ECO:0007829|PDB:7A79"
FT HELIX 265..286
FT /evidence="ECO:0007829|PDB:7A79"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:7A79"
FT HELIX 295..317
FT /evidence="ECO:0007829|PDB:7A79"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:7A79"
FT STRAND 321..326
FT /evidence="ECO:0007829|PDB:7A79"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:7A79"
FT HELIX 335..340
FT /evidence="ECO:0007829|PDB:7A79"
FT HELIX 344..353
FT /evidence="ECO:0007829|PDB:7A79"
FT HELIX 355..361
FT /evidence="ECO:0007829|PDB:7A79"
FT HELIX 365..376
FT /evidence="ECO:0007829|PDB:7A79"
FT HELIX 387..408
FT /evidence="ECO:0007829|PDB:7A79"
FT HELIX 415..420
FT /evidence="ECO:0007829|PDB:7A79"
FT HELIX 423..443
FT /evidence="ECO:0007829|PDB:7A79"
FT HELIX 450..456
FT /evidence="ECO:0007829|PDB:7A79"
SQ SEQUENCE 463 AA; 50871 MW; AED5C94BB62A3157 CRC64;
MYGNYSHFMK FPAGYGGSPG HTGSTSMSPS AALSTGKPMD SHPSYTDTPV SAPRTLSAVG
TPLNALGSPY RVITSAMGPP SGALAAPPGI NLVAPPSSQL NVVNSVSSSE DIKPLPGLPG
IGNMNYPSTS PGSLVKHICA ICGDRSSGKH YGVYSCEGCK GFFKRTIRKD LIYTCRDNKD
CLIDKRQRNR CQYCRYQKCL VMGMKREAVQ EERQRSRERA ESEAECATSG HEDMPVERIL
EAELAVEPKT ESYGDMNMEN STNDPVTNIC HAADKQLFTL VEWAKRIPHF SDLTLEDQVI
LLRAGWNELL IASFSHRSVS VQDGILLATG LHVHRSSAHS AGVGSIFDRV LTELVSKMKD
MQMDKSELGC LRAIVLFNPD AKGLSNPSEV ETLREKVYAT LEAYTKQKYP EQPGRFAKLL
LRLPALRSIG LKCLEHLFFF KLIGDTPIDT FLMEMLETPL QIT
