RARB_HUMAN
ID RARB_HUMAN Reviewed; 455 AA.
AC P10826; P12891; Q00989; Q15298; Q9UN48;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 247.
DE RecName: Full=Retinoic acid receptor beta;
DE Short=RAR-beta;
DE AltName: Full=HBV-activated protein;
DE AltName: Full=Nuclear receptor subfamily 1 group B member 2;
DE AltName: Full=RAR-epsilon;
GN Name=RARB; Synonyms=HAP, NR1B2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-2).
RC TISSUE=Placenta;
RX PubMed=2836738; DOI=10.1038/333669a0;
RA Benbrook D., Lernherdt E., Pfahl M.;
RT "A new retinoic acid receptor identified from a hepatocellular carcinoma.";
RL Nature 333:669-672(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-2).
RX PubMed=2825037; DOI=10.1038/330667a0;
RA de The H., Marchio A., Tiollais P., Dejean A.;
RT "A novel steroid thyroid hormone receptor-related gene inappropriately
RT expressed in human hepatocellular carcinoma.";
RL Nature 330:667-670(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-4).
RC TISSUE=Mammary tumor;
RX PubMed=10411930; DOI=10.1073/pnas.96.15.8651;
RA Sommer K.M., Chen L.I., Treuting P.M., Smith L.T., Swisshelm K.;
RT "Elevated retinoic acid receptor beta(4) protein in human breast tumor
RT cells with nuclear and cytoplasmic localization.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:8651-8656(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-2).
RC TISSUE=Placenta;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52 (ISOFORM BETA-2).
RX PubMed=1663808; DOI=10.3109/10425179109039679;
RA Shen S., Kruyt F.A., den Hertog J., van der Saag P.T., Kruijer W.;
RT "Mouse and human retinoic acid receptor beta 2 promoters: sequence
RT comparison and localization of retinoic acid responsiveness.";
RL DNA Seq. 2:111-119(1991).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72 (ISOFORM BETA-1).
RX PubMed=8275470;
RA Houle B., Pelletier M., Wu J., Goodyer C., Bradley W.E.;
RT "Fetal isoform of human retinoic acid receptor beta expressed in small cell
RT lung cancer lines.";
RL Cancer Res. 54:365-369(1994).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 61-109.
RX PubMed=3014347; DOI=10.1038/322070a0;
RA Dejean A., Bougueleret L., Grzeschik K.-H., Tiollais P.;
RT "Hepatitis B virus DNA integration in a sequence homologous to v-erb-A and
RT steroid receptor genes in a hepatocellular carcinoma.";
RL Nature 322:70-72(1986).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 61-109.
RC TISSUE=Liver;
RX PubMed=2170809;
RA Dejean A., de The H.;
RT "Hepatitis B virus as an insertional mutagene in a human hepatocellular
RT carcinoma.";
RL Mol. Biol. Med. 7:213-222(1990).
RN [9]
RP IDENTIFICATION OF LIGAND.
RX PubMed=2833708; DOI=10.1038/332850a0;
RA Brand N., Petkovitch M., Krust A., Chambon P., de The H., Marchio A.,
RA Tiollais P., Dejean A.;
RT "Identification of a second human retinoic acid receptor.";
RL Nature 332:850-853(1988).
RN [10]
RP FUNCTION, HETERODIMERIZATION, INTERACTION WITH NCOR2, AND MUTAGENESIS OF
RP THR-188; ILE-191; LEU-222; GLY-223 AND ALA-232.
RX PubMed=12554770; DOI=10.1210/me.2002-0340;
RA Hauksdottir H., Farboud B., Privalsky M.L.;
RT "Retinoic acid receptors beta and gamma do not repress, but instead
RT activate target gene transcription in both the absence and presence of
RT hormone ligand.";
RL Mol. Endocrinol. 17:373-385(2003).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=28167758; DOI=10.1073/pnas.1621425114;
RA Lee D.Y., Lin T.E., Lee C.I., Zhou J., Huang Y.H., Lee P.L., Shih Y.T.,
RA Chien S., Chiu J.J.;
RT "MicroRNA-10a is crucial for endothelial response to different flow
RT patterns via interaction of retinoid acid receptors and histone
RT deacetylases.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:2072-2077(2017).
RN [13]
RP STRUCTURE BY NMR OF 82-160.
RX PubMed=1321662; DOI=10.1021/bi00143a017;
RA Kathira M., Knegtel R.M.A., Boelens R., Eib D., Schilthuis J.G.,
RA van der Saag P.T., Kaptein R.;
RT "Homo- and heteronuclear NMR studies of the human retinoic acid receptor
RT beta DNA-binding domain: sequential assignments and identification of
RT secondary structure elements.";
RL Biochemistry 31:6474-6480(1992).
RN [14]
RP STRUCTURE BY NMR OF 82-160.
RX PubMed=8383553; DOI=10.1007/bf00242472;
RA Knegtel R.M.A., Katahira M., Schilthuis J.G., Bonvin A.M., Boelens R.,
RA Eib D., van der Saag P.T., Kaptein R.;
RT "The solution structure of the human retinoic acid receptor-beta DNA-
RT binding domain.";
RL J. Biomol. NMR 3:1-17(1993).
RN [15] {ECO:0007744|PDB:5UAN}
RP X-RAY CRYSTALLOGRAPHY (3.51 ANGSTROMS) OF 80-455 IN COMPLEX WITH RXRA AND
RP DNA, FUNCTION, DOMAIN, AND MUTAGENESIS OF GLU-106; ARG-113; MET-120;
RP THR-123; LYS-365; ARG-366; ARG-367; SER-369 AND LYS-370.
RX PubMed=29021580; DOI=10.1038/s41467-017-00981-y;
RA Chandra V., Wu D., Li S., Potluri N., Kim Y., Rastinejad F.;
RT "The quaternary architecture of RARbeta-RXRalpha heterodimer facilitates
RT domain-domain signal transmission.";
RL Nat. Commun. 8:868-868(2017).
RN [16]
RP VARIANT [LARGE SCALE ANALYSIS] ILE-90.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [17]
RP VARIANTS MCOPS12 SER-394 AND CYS-394, AND CHARACTERIZATION OF VARIANTS
RP MCOPS12 SER-394 AND CYS-394.
RX PubMed=24075189; DOI=10.1016/j.ajhg.2013.08.014;
RA Srour M., Chitayat D., Caron V., Chassaing N., Bitoun P., Patry L.,
RA Cordier M.P., Capo-Chichi J.M., Francannet C., Calvas P., Ragge N.,
RA Dobrzeniecka S., Hamdan F.F., Rouleau G.A., Tremblay A., Michaud J.L.;
RT "Recessive and dominant mutations in retinoic acid receptor beta in cases
RT with microphthalmia and diaphragmatic hernia.";
RL Am. J. Hum. Genet. 93:765-772(2013).
RN [18]
RP VARIANTS MCOPS12 PRO-220; ALA-303 AND CYS-394, AND CHARACTERIZATION OF
RP VARIANT MCOPS12 PRO-220; ALA-303; SER-394 AND CYS-394.
RX PubMed=27120018; DOI=10.1002/humu.23004;
RA Srour M., Caron V., Pearson T., Nielsen S.B., Levesque S., Delrue M.A.,
RA Becker T.A., Hamdan F.F., Kibar Z., Sattler S.G., Schneider M.C.,
RA Bitoun P., Chassaing N., Rosenfeld J.A., Xia F., Desai S., Roeder E.,
RA Kimonis V., Schneider A., Littlejohn R.O., Douzgou S., Tremblay A.,
RA Michaud J.L.;
RT "Gain-of-function mutations in RARB cause intellectual disability with
RT progressive motor impairment.";
RL Hum. Mutat. 37:786-793(2016).
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 RXR/RAR heterodimers bind to the
CC retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3'
CC sites known as DR1-DR5. In the absence or presence of hormone ligand,
CC acts mainly as an activator of gene expression due to weak binding to
CC corepressors (PubMed:12554770). The RXRA/RARB heterodimer can act as a
CC repressor on the DR1 element and as an activator on the DR5 element
CC (PubMed:29021580). In concert with RARG, required for skeletal growth,
CC matrix homeostasis and growth plate function (By similarity).
CC {ECO:0000250|UniProtKB:P22605, ECO:0000269|PubMed:12554770,
CC ECO:0000269|PubMed:29021580}.
CC -!- SUBUNIT: Homodimer (By similarity). Heterodimer; with a RXR molecule
CC (By similarity). Binds DNA preferentially as a RAR/RXR heterodimer (By
CC similarity). Heterodimerizes (via NR LBD) with RXRA (PubMed:29021580).
CC Interacts weakly with NCOR2 (PubMed:12554770).
CC {ECO:0000250|UniProtKB:P28702, ECO:0000269|PubMed:12554770,
CC ECO:0000269|PubMed:29021580}.
CC -!- INTERACTION:
CC P10826-2; O95273: CCNDBP1; NbExp=3; IntAct=EBI-8583223, EBI-748961;
CC P10826-2; P50222: MEOX2; NbExp=3; IntAct=EBI-8583223, EBI-748397;
CC P10826-2; Q9UBK2: PPARGC1A; NbExp=3; IntAct=EBI-8583223, EBI-765486;
CC P10826-2; P62195: PSMC5; NbExp=3; IntAct=EBI-8583223, EBI-357745;
CC P10826-2; P28702: RXRB; NbExp=10; IntAct=EBI-8583223, EBI-748576;
CC P10826-2; P28702-3: RXRB; NbExp=3; IntAct=EBI-8583223, EBI-16429492;
CC P10826-2; P48443: RXRG; NbExp=7; IntAct=EBI-8583223, EBI-712405;
CC P10826-2; P03255; Xeno; NbExp=2; IntAct=EBI-8583223, EBI-2603114;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28167758}. Cytoplasm
CC {ECO:0000269|PubMed:28167758}.
CC -!- SUBCELLULAR LOCATION: [Isoform Beta-1]: Nucleus.
CC -!- SUBCELLULAR LOCATION: [Isoform Beta-2]: Nucleus.
CC -!- SUBCELLULAR LOCATION: [Isoform Beta-4]: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=Beta-1;
CC IsoId=P10826-1; Sequence=Displayed;
CC Name=Beta-2;
CC IsoId=P10826-2; Sequence=VSP_003634;
CC Name=Beta-3;
CC IsoId=P10826-4; Sequence=Not described;
CC Name=Beta-4;
CC IsoId=P10826-3; Sequence=VSP_003635;
CC -!- TISSUE SPECIFICITY: Expressed in aortic endothelial cells (at protein
CC level). {ECO:0000269|PubMed:28167758}.
CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC DNA-binding domain and a C-terminal ligand-binding domain.
CC -!- DOMAIN: The DNA-binding nuclear receptor domain and the NR LBD domain
CC are required for binding of the RARB/RXRA heterodimer to both DR1 and
CC DR5 DNA elements. {ECO:0000269|PubMed:1663808}.
CC -!- DISEASE: Microphthalmia, syndromic, 12 (MCOPS12) [MIM:615524]: A form
CC of microphthalmia, a disorder of eye formation, ranging from small size
CC of a single eye to complete bilateral absence of ocular tissues
CC (anophthalmia). In many cases, microphthalmia/anophthalmia occurs in
CC association with syndromes that include non-ocular abnormalities.
CC MCOPS12 patients manifest variable features, including diaphragmatic
CC hernia, pulmonary hypoplasia, and cardiac abnormalities.
CC {ECO:0000269|PubMed:24075189, ECO:0000269|PubMed:27120018}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA27637.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X07282; CAA30262.1; -; mRNA.
DR EMBL; Y00291; CAA68398.1; -; mRNA.
DR EMBL; AF157483; AAD45688.1; -; mRNA.
DR EMBL; BC060794; AAH60794.1; -; mRNA.
DR EMBL; X56849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X77664; CAA54740.1; -; Genomic_DNA.
DR EMBL; X04014; CAA27637.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M57445; AAA58728.1; -; Genomic_DNA.
DR CCDS; CCDS2642.1; -. [P10826-2]
DR CCDS; CCDS46775.1; -. [P10826-3]
DR PIR; S02827; S02827.
DR PIR; S49021; S49021.
DR RefSeq; NP_000956.2; NM_000965.4. [P10826-2]
DR RefSeq; NP_001277145.1; NM_001290216.2. [P10826-1]
DR RefSeq; NP_001277146.1; NM_001290217.1. [P10826-3]
DR RefSeq; NP_001277195.1; NM_001290266.1.
DR RefSeq; NP_001277205.1; NM_001290276.1. [P10826-3]
DR RefSeq; NP_057236.1; NM_016152.3. [P10826-3]
DR PDB; 1HRA; NMR; -; A=82-160.
DR PDB; 1XAP; X-ray; 2.10 A; A=176-421.
DR PDB; 4DM6; X-ray; 1.90 A; A/B=176-421.
DR PDB; 4DM8; X-ray; 2.30 A; A/B=176-421.
DR PDB; 4JYG; X-ray; 2.35 A; A/B=176-421.
DR PDB; 4JYH; X-ray; 2.60 A; A/B=176-421.
DR PDB; 4JYI; X-ray; 1.90 A; A/B=176-421.
DR PDB; 5UAN; X-ray; 3.51 A; B=80-455.
DR PDB; 6SSQ; X-ray; 2.30 A; A/B=176-421.
DR PDBsum; 1HRA; -.
DR PDBsum; 1XAP; -.
DR PDBsum; 4DM6; -.
DR PDBsum; 4DM8; -.
DR PDBsum; 4JYG; -.
DR PDBsum; 4JYH; -.
DR PDBsum; 4JYI; -.
DR PDBsum; 5UAN; -.
DR PDBsum; 6SSQ; -.
DR AlphaFoldDB; P10826; -.
DR SMR; P10826; -.
DR BioGRID; 111850; 25.
DR IntAct; P10826; 22.
DR MINT; P10826; -.
DR STRING; 9606.ENSP00000332296; -.
DR BindingDB; P10826; -.
DR ChEMBL; CHEMBL2008; -.
DR DrugBank; DB00459; Acitretin.
DR DrugBank; DB00210; Adapalene.
DR DrugBank; DB00523; Alitretinoin.
DR DrugBank; DB02877; Arotinoid acid.
DR DrugBank; DB00926; Etretinate.
DR DrugBank; DB05785; LGD-1550.
DR DrugBank; DB04942; Tamibarotene.
DR DrugBank; DB00799; Tazarotene.
DR DrugBank; DB00755; Tretinoin.
DR DrugBank; DB12808; Trifarotene.
DR DrugCentral; P10826; -.
DR GuidetoPHARMACOLOGY; 591; -.
DR GlyGen; P10826; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; P10826; -.
DR PhosphoSitePlus; P10826; -.
DR BioMuta; RARB; -.
DR DMDM; 17380507; -.
DR jPOST; P10826; -.
DR MassIVE; P10826; -.
DR MaxQB; P10826; -.
DR PaxDb; P10826; -.
DR PeptideAtlas; P10826; -.
DR PRIDE; P10826; -.
DR ProteomicsDB; 52654; -. [P10826-1]
DR ProteomicsDB; 52655; -. [P10826-2]
DR ProteomicsDB; 52656; -. [P10826-3]
DR Antibodypedia; 934; 531 antibodies from 44 providers.
DR DNASU; 5915; -.
DR Ensembl; ENST00000330688.9; ENSP00000332296.4; ENSG00000077092.20. [P10826-2]
DR Ensembl; ENST00000383772.9; ENSP00000373282.5; ENSG00000077092.20. [P10826-1]
DR Ensembl; ENST00000437042.7; ENSP00000398840.2; ENSG00000077092.20. [P10826-3]
DR Ensembl; ENST00000458646.2; ENSP00000391391.1; ENSG00000077092.20. [P10826-3]
DR Ensembl; ENST00000686715.1; ENSP00000510539.1; ENSG00000077092.20. [P10826-1]
DR Ensembl; ENST00000687353.1; ENSP00000508588.1; ENSG00000077092.20. [P10826-1]
DR Ensembl; ENST00000687676.1; ENSP00000510313.1; ENSG00000077092.20. [P10826-1]
DR Ensembl; ENST00000688892.1; ENSP00000510650.1; ENSG00000077092.20. [P10826-1]
DR Ensembl; ENST00000693261.1; ENSP00000508421.1; ENSG00000077092.20. [P10826-3]
DR GeneID; 5915; -.
DR KEGG; hsa:5915; -.
DR MANE-Select; ENST00000330688.9; ENSP00000332296.4; NM_000965.5; NP_000956.2. [P10826-2]
DR UCSC; uc003cdh.4; human. [P10826-1]
DR CTD; 5915; -.
DR DisGeNET; 5915; -.
DR GeneCards; RARB; -.
DR HGNC; HGNC:9865; RARB.
DR HPA; ENSG00000077092; Low tissue specificity.
DR MalaCards; RARB; -.
DR MIM; 180220; gene.
DR MIM; 615524; phenotype.
DR neXtProt; NX_P10826; -.
DR OpenTargets; ENSG00000077092; -.
DR Orphanet; 2470; Matthew-Wood syndrome.
DR PharmGKB; PA34226; -.
DR VEuPathDB; HostDB:ENSG00000077092; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000156196; -.
DR HOGENOM; CLU_007368_18_0_1; -.
DR InParanoid; P10826; -.
DR OMA; PFHATRN; -.
DR OrthoDB; 1165737at2759; -.
DR PhylomeDB; P10826; -.
DR TreeFam; TF328382; -.
DR PathwayCommons; P10826; -.
DR Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-HSA-5362517; Signaling by Retinoic Acid.
DR Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
DR SignaLink; P10826; -.
DR SIGNOR; P10826; -.
DR BioGRID-ORCS; 5915; 13 hits in 1100 CRISPR screens.
DR ChiTaRS; RARB; human.
DR EvolutionaryTrace; P10826; -.
DR GeneWiki; Retinoic_acid_receptor_beta; -.
DR GenomeRNAi; 5915; -.
DR Pharos; P10826; Tclin.
DR PRO; PR:P10826; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P10826; protein.
DR Bgee; ENSG00000077092; Expressed in choroid plexus epithelium and 138 other tissues.
DR ExpressionAtlas; P10826; baseline and differential.
DR Genevisible; P10826; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0048566; P:embryonic digestive tract development; IMP:DFLAT.
DR GO; GO:0048048; P:embryonic eye morphogenesis; IEA:Ensembl.
DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; IEA:Ensembl.
DR GO; GO:0002068; P:glandular epithelial cell development; IEA:Ensembl.
DR GO; GO:0003417; P:growth plate cartilage development; IEA:Ensembl.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IEA:Ensembl.
DR GO; GO:2000647; P:negative regulation of stem cell proliferation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0022008; P:neurogenesis; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0048384; P:retinoic acid receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0072089; P:stem cell proliferation; IEA:Ensembl.
DR GO; GO:0021756; P:striatum development; IEA:Ensembl.
DR GO; GO:0001657; P:ureteric bud development; IEA:Ensembl.
DR GO; GO:0055012; P:ventricular cardiac muscle cell differentiation; IEA:Ensembl.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR IDEAL; IID00439; -.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Disease variant;
KW DNA-binding; Metal-binding; Microphthalmia; Nucleus; Phosphoprotein;
KW Proto-oncogene; Receptor; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..455
FT /note="Retinoic acid receptor beta"
FT /id="PRO_0000053467"
FT DOMAIN 183..417
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 88..153
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 88..108
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 124..148
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..87
FT /note="Modulating"
FT REGION 47..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..182
FT /note="Hinge"
FT REGION 415..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..119
FT /note="Missing (in isoform Beta-4)"
FT /evidence="ECO:0000303|PubMed:10411930"
FT /id="VSP_003635"
FT VAR_SEQ 1..60
FT /note="MTTSGHACPVPAVNGHMTHYPATPYPLLFPPVIGGLSLPPLHGLHGHPPPSG
FT CSTPSPAT -> MFDCMDVLSVSPGQILDFYTASPSSCMLQEKALKACFSGLTQTEWQH
FT RHTAQS (in isoform Beta-2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:2825037, ECO:0000303|PubMed:2836738"
FT /id="VSP_003634"
FT VARIANT 90
FT /note="V -> I (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036060"
FT VARIANT 220
FT /note="L -> P (in MCOPS12; increased transcriptional
FT response to retinoic acid ligands)"
FT /evidence="ECO:0000269|PubMed:27120018"
FT /id="VAR_077141"
FT VARIANT 303
FT /note="G -> A (in MCOPS12; increased transcriptional
FT response to retinoic acid ligands)"
FT /evidence="ECO:0000269|PubMed:27120018"
FT /id="VAR_077142"
FT VARIANT 394
FT /note="R -> C (in MCOPS12; increased transcriptional
FT response to retinoic acid ligands)"
FT /evidence="ECO:0000269|PubMed:24075189,
FT ECO:0000269|PubMed:27120018"
FT /id="VAR_070780"
FT VARIANT 394
FT /note="R -> S (in MCOPS12; increases transcriptional
FT response to retinoic acid)"
FT /evidence="ECO:0000269|PubMed:24075189"
FT /id="VAR_070781"
FT MUTAGEN 106
FT /note="E->A: As a heterodimer with RXRA, abolishes
FT transcriptional repression on DR1, reduces transcriptional
FT activation on DR5 and binding affinity for DR1 and DR5 DNA
FT elements."
FT /evidence="ECO:0000269|PubMed:29021580"
FT MUTAGEN 113
FT /note="R->A: As a heterodimer with RXRA, abolishes
FT transcriptional repression on DR1 and reduces
FT transcriptional activation on DR5."
FT /evidence="ECO:0000269|PubMed:29021580"
FT MUTAGEN 120
FT /note="M->E: As a heterodimer with RXRA, reduces
FT transcriptional repression on DR1 and reduces
FT transcriptional activation on DR5. Reduces binding affinity
FT for DR1 and DR5 DNA elements; when associated with E-366."
FT /evidence="ECO:0000269|PubMed:29021580"
FT MUTAGEN 123
FT /note="T->V: Reduces transcriptional repression on DR1 and
FT reduces transcriptional activation on DR5; when associated
FT with E-369 and E-370."
FT MUTAGEN 188
FT /note="T->I: No effect on transcriptional activation in the
FT absence of hormone."
FT /evidence="ECO:0000269|PubMed:12554770"
FT MUTAGEN 191
FT /note="I->V: No effect on transcriptional activation in the
FT absence of hormone."
FT /evidence="ECO:0000269|PubMed:12554770"
FT MUTAGEN 222
FT /note="L->I: Reduced transcriptional activation in the
FT absence of hormone. Even greater reduction in
FT transcriptional activation in the absence of hormone; when
FT associated with D-223 or S-232. Great reduction in
FT transcriptional activation in the absence of hormone; when
FT associated with D-223 and S-232."
FT /evidence="ECO:0000269|PubMed:12554770"
FT MUTAGEN 223
FT /note="G->D: Greatly reduced transcriptional activation in
FT the absence of hormone. Even greater reduction in
FT transcriptional activation in the absence of hormone; when
FT associated with I-222 or S-232. Great reduction in
FT transcriptional activation in the absence of hormone; when
FT associated with I-222 and S-232."
FT /evidence="ECO:0000269|PubMed:12554770"
FT MUTAGEN 232
FT /note="A->S: Reduced transcriptional activation in the
FT absence of hormone. Some further reduction of
FT transcriptional activity in the absence of hormone; when
FT associated with I-222 or D-223. Great reduction in
FT transcriptional activation in the absence of hormone; when
FT associated with I-222 and D-223."
FT /evidence="ECO:0000269|PubMed:12554770"
FT MUTAGEN 365
FT /note="K->E: As a heterodimer with RXRA, reduces
FT transcriptional repression on DR1 and reduces
FT transcriptional activation on DR5. Reduces transcriptional
FT repression on DR1 and reduces transcriptional activation on
FT DR5; when associated with E-366 and E-367."
FT /evidence="ECO:0000269|PubMed:29021580"
FT MUTAGEN 366
FT /note="R->E: As a heterodimer with RXRA, reduces binding
FT affinity for DR5 DNA element and no change in binding to
FT DR1. Reduces transcriptional repression on DR1 and reduces
FT transcriptional activation on DR5; when associated with E-
FT 365 and E-367. Reduces binding affinity for DR1 and DR5 DNA
FT elements; when associated with E-120."
FT /evidence="ECO:0000269|PubMed:29021580"
FT MUTAGEN 367
FT /note="R->E: As a heterodimer with RXRA, reduces
FT transcriptional repression on DR1 and reduces
FT transcriptional activation on DR5. Reduces transcriptional
FT repression on DR1 and reduces transcriptional activation on
FT DR5; when associated with E-365 and E-366."
FT /evidence="ECO:0000269|PubMed:29021580"
FT MUTAGEN 369
FT /note="S->E: Reduces transcriptional repression on DR1 and
FT reduces transcriptional activation on DR5; when associated
FT with V-123 and E-370."
FT MUTAGEN 370
FT /note="K->E: Reduces transcriptional repression on DR1 and
FT reduced transcriptional activation on DR5; when associated
FT with V-123 and E-369."
FT CONFLICT 206
FT /note="G -> A (in Ref. 2; CAA68398)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="L -> Q (in Ref. 1; CAA30262)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="L -> M (in Ref. 2; CAA68398)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="V -> L (in Ref. 1; CAA30262)"
FT /evidence="ECO:0000305"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:1HRA"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:1HRA"
FT HELIX 107..118
FT /evidence="ECO:0007829|PDB:1HRA"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:1HRA"
FT HELIX 141..148
FT /evidence="ECO:0007829|PDB:1HRA"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:1HRA"
FT HELIX 182..198
FT /evidence="ECO:0007829|PDB:4DM6"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:4DM6"
FT HELIX 222..244
FT /evidence="ECO:0007829|PDB:4DM6"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:4DM6"
FT HELIX 254..274
FT /evidence="ECO:0007829|PDB:4DM6"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:4JYG"
FT TURN 279..282
FT /evidence="ECO:0007829|PDB:4DM6"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:4DM6"
FT STRAND 289..293
FT /evidence="ECO:0007829|PDB:4DM6"
FT HELIX 294..300
FT /evidence="ECO:0007829|PDB:4DM6"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:4DM6"
FT HELIX 306..316
FT /evidence="ECO:0007829|PDB:4DM6"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:4DM6"
FT HELIX 323..334
FT /evidence="ECO:0007829|PDB:4DM6"
FT HELIX 345..366
FT /evidence="ECO:0007829|PDB:4DM6"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:4JYG"
FT HELIX 373..401
FT /evidence="ECO:0007829|PDB:4DM6"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:4DM6"
FT HELIX 408..414
FT /evidence="ECO:0007829|PDB:4DM6"
SQ SEQUENCE 455 AA; 50489 MW; 8813263AD0495D5A CRC64;
MTTSGHACPV PAVNGHMTHY PATPYPLLFP PVIGGLSLPP LHGLHGHPPP SGCSTPSPAT
IETQSTSSEE LVPSPPSPLP PPRVYKPCFV CQDKSSGYHY GVSACEGCKG FFRRSIQKNM
IYTCHRDKNC VINKVTRNRC QYCRLQKCFE VGMSKESVRN DRNKKKKETS KQECTESYEM
TAELDDLTEK IRKAHQETFP SLCQLGKYTT NSSADHRVRL DLGLWDKFSE LATKCIIKIV
EFAKRLPGFT GLTIADQITL LKAACLDILI LRICTRYTPE QDTMTFSDGL TLNRTQMHNA
GFGPLTDLVF TFANQLLPLE MDDTETGLLS AICLICGDRQ DLEEPTKVDK LQEPLLEALK
IYIRKRRPSK PHMFPKILMK ITDLRSISAK GAERVITLKM EIPGSMPPLI QEMLENSEGH
EPLTPSSSGN TAEHSPSISP SSVENSGVSQ SPLVQ
