RXRG_PONAB
ID RXRG_PONAB Reviewed; 463 AA.
AC Q5REL6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. Interacts with RARA (By
CC similarity). {ECO:0000250|UniProtKB:P48443}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
CC Cytoplasm {ECO:0000250|UniProtKB:P48443}.
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; CR857508; CAH89791.1; -; mRNA.
DR RefSeq; NP_001124824.1; NM_001131352.1.
DR AlphaFoldDB; Q5REL6; -.
DR SMR; Q5REL6; -.
DR STRING; 9601.ENSPPYP00000000669; -.
DR Ensembl; ENSPPYT00000000695; ENSPPYP00000000669; ENSPPYG00000000571.
DR GeneID; 100171682; -.
DR KEGG; pon:100171682; -.
DR CTD; 6258; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000161269; -.
DR HOGENOM; CLU_007368_5_4_1; -.
DR InParanoid; Q5REL6; -.
DR OrthoDB; 912470at2759; -.
DR Proteomes; UP000001595; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProt.
DR GO; GO:0004879; F:nuclear receptor activity; IEA:Ensembl.
DR GO; GO:0003707; F:nuclear steroid receptor activity; IEA:InterPro.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0048384; P:retinoic acid receptor signaling pathway; 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_0000317031"
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..194
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 REGION 211..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 463 AA; 50857 MW; 7ED5C94A064137E4 CRC64;
MYGNYSHFMK FPAGYGGSPG HTGSTSMSPS AALSTGKPMD SHPSYTDTPV SAPRTLSAVG
TPLNALGSPY RVITSAMGPP SGALAAPPGI NLVAPPSSQL NVVNSVSSSE DIKPLPGLPG
IGNMNYPSTS PGSLVKHICA ICGDRSSGKH YGVYSCEGCK GFFKRTIRKD LIYTCRDNKD
CLIDKRQRNR CQYCRYQKCL VMGMKREAVQ EERQRSRERA ESEAECASSG HEDMPVERIL
EAELAVEPKT ESYGDMNMEN STNDPVTNIC HAADKQLFTL VEWAKRIPHF SDLTLEDQVI
LLRAGWNELL IASFSHRSVS VQDGILLATG LHVHRSSAHS AGVGSIFDRV LTELVSKMKD
MQMDKSELGC LRAIVLFNPD AKGLSNPSEV ETLREKVYAT LEAYTKQKYP EQPGRFAKLL
LRLPALRSIG LKCLEHLFFF KLIGDTPIDT FLMEMLETPL QIT
