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Database: UniProt
Entry: P10826
LinkDB: P10826
Original site: P10826 
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   07-OCT-2020, entry version 239.
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:0000244|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 mutations 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};
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   SMR; P10826; -.
DR   BioGRID; 111850; 25.
DR   IntAct; P10826; 20.
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, 1 O-linked glycan (1 site).
DR   iPTMnet; P10826; -.
DR   PhosphoSitePlus; P10826; -.
DR   BioMuta; RARB; -.
DR   DMDM; 17380507; -.
DR   jPOST; P10826; -.
DR   MassIVE; 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; 504 antibodies.
DR   DNASU; 5915; -.
DR   Ensembl; ENST00000330688; ENSP00000332296; ENSG00000077092. [P10826-2]
DR   Ensembl; ENST00000437042; ENSP00000398840; ENSG00000077092. [P10826-3]
DR   Ensembl; ENST00000458646; ENSP00000391391; ENSG00000077092. [P10826-3]
DR   GeneID; 5915; -.
DR   KEGG; hsa:5915; -.
DR   UCSC; uc003cdh.4; human. [P10826-1]
DR   CTD; 5915; -.
DR   DisGeNET; 5915; -.
DR   EuPathDB; HostDB:ENSG00000077092.18; -.
DR   GeneCards; RARB; -.
DR   GeneReviews; RARB; -.
DR   HGNC; HGNC:9865; RARB.
DR   HPA; ENSG00000077092; Tissue enhanced (retina).
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   eggNOG; KOG3575; Eukaryota.
DR   GeneTree; ENSGT00940000156196; -.
DR   HOGENOM; CLU_007368_18_0_1; -.
DR   InParanoid; P10826; -.
DR   KO; K08528; -.
DR   OMA; FTENYEM; -.
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; 7 hits in 899 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 forebrain and 170 other tissues.
DR   ExpressionAtlas; P10826; baseline and differential.
DR   Genevisible; P10826; HS.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000790; C:nuclear chromatin; ISA:NTNU_SB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
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:0008144; F:drug binding; IEA:Ensembl.
DR   GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR   GO; GO:0046965; F:retinoid X receptor binding; IEA:Ensembl.
DR   GO; GO:0000977; F:RNA polymerase II transcription 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:0038023; F:signaling receptor activity; IBA:GO_Central.
DR   GO; GO:0008134; F:transcription factor binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0003148; P:outflow tract septum morphogenesis; IEA:Ensembl.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0031641; P:regulation of myelination; IEA:Ensembl.
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:0021756; P:striatum development; IEA:Ensembl.
DR   GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
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 mutation;
KW   DNA-binding; Metal-binding; Microphthalmia; Nucleus; Phosphoprotein;
KW   Polymorphism; 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          154..182
FT                   /note="Hinge"
FT   MOD_RES         77
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|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:0000244|PDB:1HRA"
FT   STRAND          100..102
FT                   /evidence="ECO:0000244|PDB:1HRA"
FT   HELIX           107..118
FT                   /evidence="ECO:0000244|PDB:1HRA"
FT   STRAND          133..135
FT                   /evidence="ECO:0000244|PDB:1HRA"
FT   HELIX           141..148
FT                   /evidence="ECO:0000244|PDB:1HRA"
FT   HELIX           149..151
FT                   /evidence="ECO:0000244|PDB:1HRA"
FT   HELIX           182..198
FT                   /evidence="ECO:0000244|PDB:4DM6"
FT   STRAND          202..205
FT                   /evidence="ECO:0000244|PDB:4DM6"
FT   HELIX           222..244
FT                   /evidence="ECO:0000244|PDB:4DM6"
FT   HELIX           249..251
FT                   /evidence="ECO:0000244|PDB:4DM6"
FT   HELIX           254..274
FT                   /evidence="ECO:0000244|PDB:4DM6"
FT   STRAND          276..278
FT                   /evidence="ECO:0000244|PDB:4JYG"
FT   TURN            279..282
FT                   /evidence="ECO:0000244|PDB:4DM6"
FT   STRAND          283..285
FT                   /evidence="ECO:0000244|PDB:4DM6"
FT   STRAND          289..293
FT                   /evidence="ECO:0000244|PDB:4DM6"
FT   HELIX           294..300
FT                   /evidence="ECO:0000244|PDB:4DM6"
FT   HELIX           303..305
FT                   /evidence="ECO:0000244|PDB:4DM6"
FT   HELIX           306..316
FT                   /evidence="ECO:0000244|PDB:4DM6"
FT   HELIX           317..319
FT                   /evidence="ECO:0000244|PDB:4DM6"
FT   HELIX           323..334
FT                   /evidence="ECO:0000244|PDB:4DM6"
FT   HELIX           345..366
FT                   /evidence="ECO:0000244|PDB:4DM6"
FT   STRAND          368..370
FT                   /evidence="ECO:0000244|PDB:4JYG"
FT   HELIX           373..401
FT                   /evidence="ECO:0000244|PDB:4DM6"
FT   STRAND          402..404
FT                   /evidence="ECO:0000244|PDB:4DM6"
FT   HELIX           408..414
FT                   /evidence="ECO:0000244|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
//
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