RXRG_PIG
ID RXRG_PIG Reviewed; 463 AA.
AC Q0GFF6; Q69B31;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 111.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yu H., Song Y., Ding J., Lee L.;
RT "Cloning and expression of RXR gamma in porcine.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-463.
RX PubMed=15389320; DOI=10.1007/s00335-004-2366-4;
RA Moller M., Berg F., Riquet J., Pomp D., Archibald A., Anderson S., Feve K.,
RA Zhang Y., Rothschild M., Milan D., Andersson L., Tuggle C.K.;
RT "High-resolution comparative mapping of pig Chromosome 4, emphasizing the
RT FAT1 region.";
RL Mamm. Genome 15:717-731(2004).
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 {ECO:0000305}.
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; DQ866834; ABI24018.1; -; mRNA.
DR EMBL; AY429474; AAR96256.1; -; mRNA.
DR RefSeq; NP_001123685.1; NM_001130213.1.
DR AlphaFoldDB; Q0GFF6; -.
DR SMR; Q0GFF6; -.
DR STRING; 9823.ENSSSCP00000006747; -.
DR PaxDb; Q0GFF6; -.
DR PeptideAtlas; Q0GFF6; -.
DR PRIDE; Q0GFF6; -.
DR Ensembl; ENSSSCT00000048789; ENSSSCP00000057363; ENSSSCG00000006328.
DR Ensembl; ENSSSCT00015035538; ENSSSCP00015014139; ENSSSCG00015026690.
DR Ensembl; ENSSSCT00025041192; ENSSSCP00025017525; ENSSSCG00025030180.
DR Ensembl; ENSSSCT00030007294; ENSSSCP00030003258; ENSSSCG00030005341.
DR Ensembl; ENSSSCT00035052016; ENSSSCP00035020895; ENSSSCG00035039148.
DR Ensembl; ENSSSCT00040055167; ENSSSCP00040022926; ENSSSCG00040041165.
DR Ensembl; ENSSSCT00045044077; ENSSSCP00045030586; ENSSSCG00045025767.
DR Ensembl; ENSSSCT00050068762; ENSSSCP00050029521; ENSSSCG00050050513.
DR Ensembl; ENSSSCT00055017133; ENSSSCP00055013529; ENSSSCG00055008734.
DR Ensembl; ENSSSCT00060094058; ENSSSCP00060040695; ENSSSCG00060068866.
DR Ensembl; ENSSSCT00065071761; ENSSSCP00065031278; ENSSSCG00065052386.
DR Ensembl; ENSSSCT00070049233; ENSSSCP00070041586; ENSSSCG00070024660.
DR GeneID; 445465; -.
DR KEGG; ssc:445465; -.
DR CTD; 6258; -.
DR VGNC; VGNC:92530; RXRG.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000161269; -.
DR HOGENOM; CLU_007368_5_4_1; -.
DR InParanoid; Q0GFF6; -.
DR OrthoDB; 912470at2759; -.
DR TreeFam; TF352097; -.
DR Reactome; R-SSC-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-SSC-5362517; Signaling by Retinoic Acid.
DR Proteomes; UP000008227; Chromosome 4.
DR Proteomes; UP000314985; Chromosome 4.
DR Bgee; ENSSSCG00000006328; Expressed in heart left ventricle and 33 other tissues.
DR ExpressionAtlas; Q0GFF6; baseline and differential.
DR Genevisible; Q0GFF6; SS.
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: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: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; IBA:GO_Central.
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 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_0000317030"
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 17..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..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 361
FT /note="M -> T (in Ref. 1; ABI24018)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="I -> V (in Ref. 1; ABI24018)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 463 AA; 50943 MW; 697501F0F570FF78 CRC64;
MYGNYSHFMK FPTGFGGSPG HSGSTSMSPS AALSTGKPMD SHPSYTDTPV SAPRTLSAVG
TPLNALGSPY RVITSTMGPP SGTLAAPPGI NLVAPPSSQL NVVNSVSISE 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
