ID   RXRG_XENLA              Reviewed;         470 AA.
AC   P51129;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 113.
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   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1312717; DOI=10.1073/pnas.89.6.2321;
RA   Blumberg B., Mangelsdorf D.J., Dyck J.A., Bittner D.A., Evans R.M.,
RA   De Robertis E.M.;
RT   "Multiple retinoid-responsive receptors in a single cell: families of
RT   retinoid 'X' receptors and retinoic acid receptors in the Xenopus egg.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:2321-2325(1992).
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. Heterodimer; with a rar molecule. Binds DNA
CC       preferentially as a rar/rxr heterodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
CC   -!- DEVELOPMENTAL STAGE: It is synthesized during oogenesis and persists in
CC       the cleaving embryo at approximately constant levels until it is
CC       degraded just before gastrulation.
CC   -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC       DNA-binding domain and a C-terminal ligand-binding domain.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; L11443; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; D41977; D41977.
DR   AlphaFoldDB; P51129; -.
DR   SMR; P51129; -.
DR   PRIDE; P51129; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0003707; F:nuclear steroid receptor activity; IEA:InterPro.
DR   GO; GO:0046966; F:nuclear thyroid hormone receptor binding; IPI:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IPI:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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   DNA-binding; Metal-binding; Nucleus; Receptor; Reference proteome;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..470
FT                   /note="Retinoic acid receptor RXR-gamma"
FT                   /id="PRO_0000053580"
FT   DOMAIN          238..466
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        146..211
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         146..166
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         182..206
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   REGION          1..145
FT                   /note="Modulating"
FT                   /evidence="ECO:0000250"
FT   REGION          212..235
FT                   /note="Hinge"
FT   REGION          217..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..233
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   470 AA;  51925 MW;  DD1172DC53CF3A5F CRC64;
     MHLATETAPS MATYSSTYFN SSLHAHSTSV SSSNLAAMNS LDTHPGYMGN SLNGPRSMTT
     NMNSMCSPGN NIGLPYRVIA SSMGPHSLPS PTILNYPGHE SPPFNILNNV SCSEDIKPPP
     GLSSLGSPCM NNYSCNSPGA LTKHICAICG DRSSGKHYGV YSCEGCKGFF KRTIRKDLVY
     TCRDSKDCLI DKRQRNRCQY CRYQKCLAMG MKREAVQEER QRSREKSDTE AESTSSTSEE
     MPVERILEAE LAVDPKIEAF GDAGLPNSTN DPVTNICHAA DKQLFTLVEW AKRIPYFSDL
     PLEDQVILLR AGWNELLIAS FSHRSVSVQD GILLATGLHV HRSSAHNAGV GSIFDRVLTE
     LVSKMKDMDM DKSELGCLRA IVLFNPDAKG LSNAAEVEAL REKVYATLES YTKQKYPDQP
     GRFAKLLLRL PALRSIGLKC LEHLFFFKLI GDTPIDTFLM EMLETPHQIS