RXRB_MOUSE
ID RXRB_MOUSE Reviewed; 520 AA.
AC P28704; P33243;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Retinoic acid receptor RXR-beta;
DE AltName: Full=MHC class I regulatory element-binding protein H-2RIIBP;
DE AltName: Full=Nuclear receptor subfamily 2 group B member 2;
DE AltName: Full=Retinoid X receptor beta;
GN Name=Rxrb; Synonyms=Nr2b2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, AND TISSUE
RP SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=8194750; DOI=10.1016/0378-1119(94)90259-3;
RA Nagata T., Kanno Y., Ozato K., Taketo M.;
RT "The mouse Rxrb gene encoding RXR beta: genomic organization and two mRNA
RT isoforms generated by alternative splicing of transcripts initiated from
RT CpG island promoters.";
RL Gene 142:183-189(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129/SvJ;
RA Rowen L., Qin S., Madan A., Loretz C., James R., Dors M., Mix L., Hall J.,
RA Lasky S., Hood L.;
RT "Sequence of the mouse major histocomaptibility locus class II region.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC TISSUE=Limb;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 73-520 (ISOFORM LONG), AND FUNCTION.
RC TISSUE=Embryo;
RX PubMed=1310259; DOI=10.1016/0092-8674(92)90478-u;
RA Leid M., Kastner P., Lyons R., Nakshatri H., Saunders M., Zacharewsi T.,
RA Chen J.Y., Staub A., Garnier J.-M., Mader S., Chambon P.;
RT "Purification, cloning, and RXR identity of the HeLa cell factor with which
RT RAR or TR heterodimerizes to bind target sequences efficiently.";
RL Cell 68:377-395(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 75-520 (ISOFORM LONG).
RC TISSUE=Liver;
RX PubMed=2554307; DOI=10.1073/pnas.86.21.8289;
RA Hamada K., Gleason S.L., Levi B.-Z., Hirschfeld S., Appella E., Ozato K.;
RT "H-2RIIBP, a member of the nuclear hormone receptor superfamily that binds
RT to both the regulatory element of major histocompatibility class I genes
RT and the estrogen response element.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:8289-8293(1989).
RN [6]
RP NUCLEOTIDE SEQUENCE (ISOFORM SHORT), FUNCTION, TISSUE SPECIFICITY, AND
RP DOMAIN.
RC TISSUE=Liver;
RX PubMed=1312497; DOI=10.1101/gad.6.3.329;
RA Mangelsdorf D.J., Borgmeyer U., Heyman R.A., Zhou J.Y., Ong E.S., Oro A.E.,
RA Kakizuka A., Evans R.M.;
RT "Characterization of three RXR genes that mediate the action of 9-cis
RT retinoic acid.";
RL Genes Dev. 6:329-344(1992).
RN [7]
RP INTERACTION WITH AKAP13.
RX PubMed=20139090; DOI=10.1074/jbc.m110.106856;
RA Mayers C.M., Wadell J., McLean K., Venere M., Malik M., Shibata T.,
RA Driggers P.H., Kino T., Guo X.C., Koide H., Gorivodsky M., Grinberg A.,
RA Mukhopadhyay M., Abu-Asab M., Westphal H., Segars J.H.;
RT "The Rho guanine nucleotide exchange factor AKAP13 (BRX) is essential for
RT cardiac development in mice.";
RL J. Biol. Chem. 285:12344-12354(2010).
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). {ECO:0000269|PubMed:1310259,
CC ECO:0000269|PubMed:1312497}.
CC -!- SUBUNIT: Homodimer (in vitro). Heterodimer with other retinoic acid
CC receptor family members. Binds DNA preferentially as a RAR/RXR
CC heterodimer. Interacts with NR1H3 (By similarity). Interacts with
CC AKAP13 (PubMed:20139090). {ECO:0000250|UniProtKB:P28702,
CC ECO:0000269|PubMed:20139090}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P28702}. Cytoplasm
CC {ECO:0000250|UniProtKB:P28702}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=Long;
CC IsoId=P28704-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P28704-2; Sequence=VSP_003678;
CC -!- TISSUE SPECIFICITY: In all tissues tested, including brain, thymus,
CC spleen and liver. {ECO:0000269|PubMed:1312497,
CC ECO:0000269|PubMed:8194750}.
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|PubMed:1312497}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
CC subfamily. {ECO:0000305}.
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DR EMBL; D21831; BAA04858.1; -; Genomic_DNA.
DR EMBL; D21831; BAA04859.1; -; Genomic_DNA.
DR EMBL; AF100956; AAC69904.1; -; Genomic_DNA.
DR EMBL; BC049773; AAH49773.1; -; mRNA.
DR EMBL; M84818; AAA40081.2; -; mRNA.
DR EMBL; M26804; AAA37772.1; -; mRNA.
DR EMBL; X66224; CAA46963.1; -; mRNA.
DR CCDS; CCDS57068.1; -. [P28704-2]
DR CCDS; CCDS89073.1; -. [P28704-1]
DR PIR; A34418; A34418.
DR PIR; D41727; D41727.
DR PIR; I84718; I84718.
DR PIR; S26669; S26669.
DR RefSeq; NP_001192145.1; NM_001205216.1. [P28704-2]
DR RefSeq; NP_035436.1; NM_011306.4. [P28704-1]
DR AlphaFoldDB; P28704; -.
DR SMR; P28704; -.
DR BioGRID; 203039; 2.
DR ComplexPortal; CPX-706; RXRbeta-LXRbeta nuclear hormone receptor complex.
DR ComplexPortal; CPX-717; RXRbeta-LXRalpha nuclear hormone receptor complex.
DR ComplexPortal; CPX-872; RXRbeta-VDR nuclear hormone receptor complex.
DR IntAct; P28704; 1.
DR STRING; 10090.ENSMUSP00000036585; -.
DR BindingDB; P28704; -.
DR ChEMBL; CHEMBL4047; -.
DR DrugCentral; P28704; -.
DR GuidetoPHARMACOLOGY; 611; -.
DR iPTMnet; P28704; -.
DR PhosphoSitePlus; P28704; -.
DR EPD; P28704; -.
DR MaxQB; P28704; -.
DR PaxDb; P28704; -.
DR PeptideAtlas; P28704; -.
DR PRIDE; P28704; -.
DR ProteomicsDB; 256850; -. [P28704-1]
DR ProteomicsDB; 256851; -. [P28704-2]
DR Antibodypedia; 28936; 341 antibodies from 43 providers.
DR DNASU; 20182; -.
DR Ensembl; ENSMUST00000116612; ENSMUSP00000112311; ENSMUSG00000039656. [P28704-2]
DR Ensembl; ENSMUST00000174299; ENSMUSP00000133775; ENSMUSG00000039656. [P28704-1]
DR GeneID; 20182; -.
DR KEGG; mmu:20182; -.
DR UCSC; uc008cax.2; mouse. [P28704-1]
DR CTD; 6257; -.
DR MGI; MGI:98215; Rxrb.
DR VEuPathDB; HostDB:ENSMUSG00000039656; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000159208; -.
DR HOGENOM; CLU_007368_5_4_1; -.
DR InParanoid; P28704; -.
DR PhylomeDB; P28704; -.
DR Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-MMU-5362517; Signaling by Retinoic Acid.
DR Reactome; R-MMU-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR Reactome; R-MMU-9623433; NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis.
DR BioGRID-ORCS; 20182; 7 hits in 79 CRISPR screens.
DR ChiTaRS; Rxrb; mouse.
DR PRO; PR:P28704; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P28704; protein.
DR Bgee; ENSMUSG00000039656; Expressed in ileal epithelium and 266 other tissues.
DR ExpressionAtlas; P28704; baseline and differential.
DR Genevisible; P28704; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0004879; F:nuclear receptor activity; ISO:MGI.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISO:MGI.
DR GO; GO:0042974; F:nuclear retinoic acid receptor binding; ISO:MGI.
DR GO; GO:0003707; F:nuclear steroid receptor activity; IEA:InterPro.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; ISO:MGI.
DR GO; GO:0042809; F:nuclear vitamin D receptor binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
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:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IGI:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; IGI:MGI.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0071300; P:cellular response to retinoic acid; IDA:UniProtKB.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IC:ComplexPortal.
DR GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
DR GO; GO:0001893; P:maternal placenta development; IGI:MGI.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0070564; P:positive regulation of vitamin D receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:0031641; P:regulation of myelination; ISO:MGI.
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 GO; GO:0055012; P:ventricular cardiac muscle cell differentiation; IMP:MGI.
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; 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; 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 Alternative splicing; Cytoplasm; DNA-binding; Metal-binding; Methylation;
KW Nucleus; Receptor; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..520
FT /note="Retinoic acid receptor RXR-beta"
FT /id="PRO_0000053573"
FT DOMAIN 283..516
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 192..257
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 192..212
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 228..252
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..191
FT /note="Modulating"
FT /evidence="ECO:0000250"
FT REGION 1..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..382
FT /note="Hinge"
FT REGION 263..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..120
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..142
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 25
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P28702"
FT VAR_SEQ 1..110
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_003678"
FT CONFLICT 73..75
FT /note="SGR -> MGP (in Ref. 4; AAA40081)"
FT /evidence="ECO:0000305"
FT CONFLICT 75..77
FT /note="RDS -> EFP (in Ref. 5; AAA37772)"
FT /evidence="ECO:0000305"
FT CONFLICT 433
FT /note="L -> M (in Ref. 4; AAA40081)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 520 AA; 55866 MW; 71FAEAEC0D2DB505 CRC64;
MSWATRPPFL PPRHAAGQCG PVGVRKEMHC GVASRWRRRR PWLDPAAAAA AAGEQQALEP
EPGEAGRDGM GDSGRDSRSP DSSSPNPLSQ GIRPSSPPGP PLTPSAPPPP MPPPPLGSPF
PVISSSMGSP GLPPPAPPGF SGPVSSPQIN STVSLPGGGS GPPEDVKPPV LGVRGLHCPP
PPGGPGAGKR LCAICGDRSS GKHYGVYSCE GCKGFFKRTI RKDLTYSCRD NKDCTVDKRQ
RNRCQYCRYQ KCLATGMKRE AVQEERQRGK DKDGDGDGAG GAPEEMPVDR ILEAELAVEQ
KSDQGVEGPG ATGGGGSSPN DPVTNICQAA DKQLFTLVEW AKRIPHFSSL PLDDQVILLR
AGWNELLIAS FSHRSIDVRD GILLATGLHV HRNSAHSAGV GAIFDRVLTE LVSKMRDMRM
DKTELGCLRA IILFNPDAKG LSNPGEVEIL REKVYASLET YCKQKYPEQQ GRFAKLLLRL
PALRSIGLKC LEHLFFFKLI GDTPIDTFLM EMLEAPHQLA
