RARG_XENLA
ID RARG_XENLA Reviewed; 476 AA.
AC P28699; P51127; P79878; P79879;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Retinoic acid receptor gamma;
DE Short=RAR-gamma;
DE AltName: Full=Nuclear receptor subfamily 1 group B member 3;
GN Name=rarg; Synonyms=nr1b3;
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] (ISOFORM RAR-GAMMA-1).
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM RAR-GAMMA-2), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Neurula;
RX PubMed=1846602; DOI=10.1101/gad.5.1.94;
RA Ellinger-Ziegelbauer H., Dreyer C.;
RT "A retinoic acid receptor expressed in the early development of Xenopus
RT laevis.";
RL Genes Dev. 5:94-104(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM RAR-GAMMA-2), AND DEVELOPMENTAL STAGE.
RX PubMed=8641047; DOI=10.1002/dvg.1020170402;
RA Crawford M.J., Liversage R.A., Varmuza S.L.;
RT "Two isoforms of Xenopus retinoic acid receptor gamma 2 (B) exhibit
RT differential expression and sensitivity to retinoic acid during
RT embryogenesis.";
RL Dev. Genet. 17:291-302(1995).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer; with a rxr molecule. Binds DNA preferentially as
CC a rar/rxr heterodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Isoforms differ in their N-terminal section.;
CC Name=RAR-gamma-1;
CC IsoId=P28699-1; Sequence=Displayed;
CC Name=RAR-gamma-2;
CC IsoId=P28699-2; Sequence=VSP_003642;
CC -!- TISSUE SPECIFICITY: Expressed in embryos, tadpoles and various adult
CC tissue such as kidney, testis, brain, liver, skeletal muscle and
CC spleen. {ECO:0000269|PubMed:1846602}.
CC -!- DEVELOPMENTAL STAGE: It is synthesized during oogenesis and persists
CC during early cleavage. It accumulates at gastrulation (stage 10), peaks
CC in quantity during neurulation (stage 17), then drops to a low level
CC after stage 26. Isoform 1 is strongly expressed in branchial arches and
CC to a lesser extent in the neural floor plate, but is not expressed
CC neither in the pre-somitic mesoderm nor notochord. At gastrula stages
CC 10-11, isoform 2 is mainly found in ectoderm and mesoderm with greater
CC expression in the prospective dorsal side. At neurula stage, expressed
CC anteriorly in the head mesoderm and in the archenteron roof. In early
CC tadpole stage, expressed in head mesenchyme and in the tailbud.
CC {ECO:0000269|PubMed:1846602, ECO:0000269|PubMed:8641047}.
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. NR1
CC subfamily. {ECO:0000305}.
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DR EMBL; L11444; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; X59396; CAA42039.1; -; mRNA.
DR EMBL; S82175; AAB47116.1; -; mRNA.
DR EMBL; S82173; AAB47115.1; -; mRNA.
DR PIR; A38592; A38592.
DR PIR; B41977; B41977.
DR RefSeq; NP_001081663.1; NM_001088194.1.
DR RefSeq; XP_018103594.1; XM_018248105.1. [P28699-1]
DR AlphaFoldDB; P28699; -.
DR SMR; P28699; -.
DR DNASU; 397983; -.
DR GeneID; 397983; -.
DR KEGG; xla:397983; -.
DR CTD; 397983; -.
DR Xenbase; XB-GENE-865050; rarg.S.
DR OMA; MQYTCHK; -.
DR OrthoDB; 1165737at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 397983; Expressed in neurula embryo and 19 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004879; F:nuclear receptor activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048384; P:retinoic acid receptor signaling pathway; 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; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR003078; Retinoic_acid_rcpt.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR01292; RETNOICACIDR.
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 Alternative splicing; DNA-binding; Metal-binding; Nucleus; Receptor;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..476
FT /note="Retinoic acid receptor gamma"
FT /id="PRO_0000053476"
FT DOMAIN 206..440
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 110..175
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 110..130
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 146..170
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..109
FT /note="Modulating"
FT REGION 81..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..205
FT /note="Hinge"
FT REGION 435..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 184..189
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 451..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..82
FT /note="MANSSKERLCGAGAPLGHANGFPPSVYPFAFSGGIRRSPPFEVLANGGFFRS
FT FPTDLPKEMASLSLTMGAAERSAHSDCIST -> MYDCMEAFPLMPRPLYDMSPQGPCM
FT LRKAGCFGGLDPFGWMQSHSMQS (in isoform RAR-gamma-2)"
FT /evidence="ECO:0000303|PubMed:1846602,
FT ECO:0000303|PubMed:8641047"
FT /id="VSP_003642"
FT CONFLICT 242
FT /note="Q -> R (in Ref. 3; AAB47116/AAB47115)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="A -> G (in Ref. 2; CAA42039)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 53034 MW; 2AB7728B0448F7FF CRC64;
MANSSKERLC GAGAPLGHAN GFPPSVYPFA FSGGIRRSPP FEVLANGGFF RSFPTDLPKE
MASLSLTMGA AERSAHSDCI STVETQSTSS EEMVPSSPSP PPPPRVYKPC FVCNDKSSGY
HYGVSSCEGC KGFFRRSIQK NMVYTCHRDK NCQINKVTRN RCQFCRLQKC FQVGMSKEAV
RNDRNKKKKE IKEEVVLPDS YEMPPEMEEL IQKVSKAHQE TFPSLCQLGK YTTNSSADQR
VQLDLGLWDK FSELSTKCII KIVEFAKRLP GFTTLTIADQ ITLLKSACLD ILMLRICTRY
TPEQDTMTFS DGLTLNRTQM HNAGFGPLTD LVFSFADQLL PLEMDDTETG LLSAICLICG
DRMDLEEPEK VEKLQEPLLE ALKFYARRRR PDKPYMFPRM LMKITDLRGI STKGAERAIT
LKLEIPGPMP PLIREMLENP EAFEDGAATP KPSERSSSES SNGSPTGEDS SGSKTP
