RXRA_XENLA
ID RXRA_XENLA Reviewed; 488 AA.
AC P51128;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Retinoic acid receptor RXR-alpha;
DE AltName: Full=Nuclear receptor subfamily 2 group B member 1;
DE AltName: Full=Retinoid X receptor alpha;
GN Name=rxra; Synonyms=nr2b1;
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).
RN [2]
RP INTERACTION WITH NCOA3.
RX PubMed=9658407; DOI=10.1210/mend.12.7.0139;
RA Kim H.-J., Lee S.-K., Na S.-Y., Choi H.-S., Lee J.W.;
RT "Molecular cloning of xSRC-3, a novel transcription coactivator from
RT Xenopus, that is related to AIB1, p/CIP and TIF2.";
RL Mol. Endocrinol. 12:1038-1047(1998).
RN [3]
RP INTERACTION WITH SENP6.
RX PubMed=16912044; DOI=10.1074/jbc.m604033200;
RA Choi S.J., Chung S.S., Rho E.J., Lee H.W., Lee M.H., Choi H.S., Seol J.H.,
RA Baek S.H., Bang O.S., Chung C.H.;
RT "Negative modulation of RXRalpha transcriptional activity by small
RT ubiquitin-related modifier (SUMO) modification and its reversal by SUMO-
RT specific protease SUSP1.";
RL J. Biol. Chem. 281:30669-30677(2006).
CC -!- FUNCTION: Receptor for retinoic acid that acts as a transcription
CC factor. Forms homo- or heterodimers with retinoic acid receptors (rars)
CC and binds to target response elements in response to their ligands,
CC all-trans or 9-cis retinoic acid, to regulate gene expression in
CC 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 to regulate transcription. The high affinity
CC ligand for rxrs is 9-cis retinoic acid. In the absence of ligand, the
CC rar/rxr heterodimers associate with a multiprotein complex containing
CC transcription corepressors that induce histone deacetylation, chromatin
CC condensation and transcriptional suppression. On ligand binding, the
CC corepressors dissociate from the receptors and coactivators are
CC recruited leading to transcriptional activation.
CC {ECO:0000250|UniProtKB:P19793}.
CC -!- SUBUNIT: Homodimer. Heterodimer; with a rar molecule. Binds DNA
CC preferentially as a rar/rxr heterodimer (By similarity). Interacts with
CC coactivator ncoa3 and with senp6 (PubMed:16912044, PubMed:9658407).
CC {ECO:0000250|UniProtKB:P19793, ECO:0000269|PubMed:16912044,
CC ECO:0000269|PubMed:9658407}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
CC -!- DEVELOPMENTAL STAGE: It is synthesized during oogenesis and persists
CC during early cleavage, levels drop before gastrulation and remain low
CC until the tailbud stage, and then increase in the later stages.
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: Sumoylated on Lys-134; which negatively regulates transcriptional
CC activity. Desumoylated specifically by SENP6 (By similarity).
CC {ECO:0000250}.
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; L11446; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; C41977; C41977.
DR RefSeq; XP_018084982.1; XM_018229493.1.
DR AlphaFoldDB; P51128; -.
DR SMR; P51128; -.
DR GeneID; 378685; -.
DR KEGG; xla:378685; -.
DR CTD; 378685; -.
DR Xenbase; XB-GENE-865207; rxra.L.
DR OMA; EHAVEPK; -.
DR OrthoDB; 912470at2759; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 378685; Expressed in muscle tissue and 17 other tissues.
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; IEA:InterPro.
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 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Receptor;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..488
FT /note="Retinoic acid receptor RXR-alpha"
FT /id="PRO_0000053569"
FT DOMAIN 253..484
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 158..233
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 161..181
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 197..216
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..160
FT /note="Modulating"
FT /evidence="ECO:0000250"
FT REGION 186..191
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT REGION 227..250
FT /note="Hinge"
FT REGION 232..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..394
FT /note="Required for nuclear export"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT REGION 473..484
FT /note="AF-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT COMPBIAS 232..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT BINDING 342
FT /ligand="9-cis-retinoate"
FT /ligand_id="ChEBI:CHEBI:78630"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT BINDING 342
FT /ligand="all-trans-retinoate"
FT /ligand_id="ChEBI:CHEBI:35291"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT BINDING 353
FT /ligand="9-cis-retinoate"
FT /ligand_id="ChEBI:CHEBI:78630"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT BINDING 353
FT /ligand="all-trans-retinoate"
FT /ligand_id="ChEBI:CHEBI:35291"
FT /evidence="ECO:0000250|UniProtKB:P19793"
FT CROSSLNK 134
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 488 AA; 53469 MW; 876FE43E901905D8 CRC64;
MSSAAMDTKH FLPLGGRTCA DTLRCTTSWT AGYDFSSQVN SSSLSSSGLR GSMTAPLLHP
SLGNSGLNNS LGSPTQLPSP LSSPINGMGP PFSVISPPLG PSMAIPSTPG LGYGTGSPQI
HSPMNSVSST EDIKPPPGIN GILKVPMHPS GAMASFTKHI CAICGDRSSG KHYGVYSCEG
CKGFFKRTVR KDLTYTCRDS KDCMIDKRQR NRCQYCRYQK CLAMGMKREA VQEERQRGKE
RNENEVESSN SANEDMPVEK ILEAEHAVEP KTETYTEANM GLAPNSPSDP VTNICQAADK
QLFTLVEWAK RIPHFSELPL DDQVILLRAG WNELLIASFS HRSIAVKDGI LLATGLHVHR
NSAHSAGVGA IFDRVLTELV SKMRDMQMDK TELGCLRAIV LFNPDSKGLS NPLEVEALRE
KVYASLEAYC KQKYPEQPGR FAKLLLRLPA LRSIGLKCLE HLFFFKLIGD TPIDTFLMEM
LEAPHQMT
