RORB_MOUSE
ID RORB_MOUSE Reviewed; 470 AA.
AC Q8R1B8; Q0PQZ2; Q0PQZ3; Q1MVR9;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Nuclear receptor ROR-beta;
DE AltName: Full=Nuclear receptor RZR-beta;
DE AltName: Full=Nuclear receptor subfamily 1 group F member 2;
DE AltName: Full=Retinoid-related orphan receptor-beta;
GN Name=Rorb; Synonyms=Nr1f2;
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 [MRNA] (ISOFORMS 1 AND 2), FUNCTION IN CONE
RP PHOTORECEPTOR DEVELOPMENT, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND DNA-BINDING.
RC STRAIN=C57BL/6J; TISSUE=Embryonic eye;
RX PubMed=16574740; DOI=10.1210/me.2005-0505;
RA Srinivas M., Ng L., Liu H., Jia L., Forrest D.;
RT "Activation of the blue opsin gene in cone photoreceptor development by
RT retinoid-related orphan receptor beta.";
RL Mol. Endocrinol. 20:1728-1741(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Takano A., Katsuyama Y.;
RT "Mouse ROR beta partial cDNA.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Retina;
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 FUNCTION IN CIRCADIAN RHYTHMS AND DEVELOPMENT, DISRUPTION PHENOTYPE, AND
RP TISSUE SPECIFICITY.
RX PubMed=9670004; DOI=10.1093/emboj/17.14.3867;
RA Andre E., Conquet F., Steinmayr M., Stratton S.C., Porciatti V.,
RA Becker-Andre M.;
RT "Disruption of retinoid-related orphan receptor beta changes circadian
RT behavior, causes retinal degeneration and leads to vacillans phenotype in
RT mice.";
RL EMBO J. 17:3867-3877(1998).
RN [5]
RP FUNCTION IN CIRCADIAN RHYTHMS, AND DISRUPTION PHENOTYPE.
RX PubMed=17303680; DOI=10.1152/ajpregu.00687.2006;
RA Masana M.I., Sumaya I.C., Becker-Andre M., Dubocovich M.L.;
RT "Behavioral characterization and modulation of circadian rhythms by light
RT and melatonin in C3H/HeN mice homozygous for the RORbeta knockout.";
RL Am. J. Physiol. 292:R2357-R2367(2007).
RN [6]
RP FUNCTION IN ROD DIFFERENTIATION, AND DISRUPTION PHENOTYPE.
RX PubMed=19805139; DOI=10.1073/pnas.0902425106;
RA Jia L., Oh E.C., Ng L., Srinivas M., Brooks M., Swaroop A., Forrest D.;
RT "Retinoid-related orphan nuclear receptor RORbeta is an early-acting factor
RT in rod photoreceptor development.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:17534-17539(2009).
RN [7]
RP FUNCTION IN NEUROGENESIS, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=21799210; DOI=10.1093/cercor/bhr182;
RA Jabaudon D., Shnider S.J., Tischfield D.J., Galazo M.J., Macklis J.D.;
RT "RORbeta induces barrel-like neuronal clusters in the developing
RT neocortex.";
RL Cereb. Cortex 22:996-1006(2012).
RN [8]
RP FUNCTION IN OSTEOGENESIS, TISSUE SPECIFICITY, AND INDUCTION BY AGING.
RX PubMed=22189870; DOI=10.1002/jbmr.1502;
RA Roforth M.M., Liu G., Khosla S., Monroe D.G.;
RT "Examination of nuclear receptor expression in osteoblasts reveals Rorbeta
RT as an important regulator of osteogenesis.";
RL J. Bone Miner. Res. 27:891-901(2012).
RN [9]
RP FUNCTION IN RETINA DEVELOPMENT (ISOFORM 1), DISRUPTION PHENOTYPE (ISOFORM
RP 1), TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE (ISOFORMS 1 AND 2).
RX PubMed=23652001; DOI=10.1038/ncomms2793;
RA Liu H., Kim S.Y., Fu Y., Wu X., Ng L., Swaroop A., Forrest D.;
RT "An isoform of retinoid-related orphan receptor beta directs
RT differentiation of retinal amacrine and horizontal interneurons.";
RL Nat. Commun. 4:1813-1813(2013).
CC -!- FUNCTION: Nuclear receptor that binds DNA as a monomer to ROR response
CC elements (RORE) containing a single core motif half-site 5'-AGGTCA-3'
CC preceded by a short A-T-rich sequence. Considered to have intrinsic
CC transcriptional activity, have some natural ligands such as all-trans
CC retinoic acid (ATRA) and other retinoids which act as inverse agonists
CC repressing the transcriptional activity. Required for normal postnatal
CC development of rod and cone photoreceptor cells. Modulates rod
CC photoreceptors differentiation at least by inducing the transcription
CC factor NRL-mediated pathway. In cone photoreceptor cells, regulates
CC transcription of OPN1SW. Involved in the regulation of the period
CC length and stability of the circadian rhythm. May control
CC cytoarchitectural patterning of neocortical neurons during development.
CC May act in a dose-dependent manner to regulate barrel formation upon
CC innervation of layer IV neurons by thalamocortical axons. May play a
CC role in the suppression of osteoblastic differentiation through the
CC inhibition of RUNX2 transcriptional activity.
CC {ECO:0000250|UniProtKB:P45446}.
CC -!- FUNCTION: Isoform 1 is critical for hindlimb motor control and for the
CC differentiation of amacrine and horizontal cells in the retina.
CC Regulates the expression of PTF1A synergistically with FOXN4.
CC {ECO:0000269|PubMed:23652001}.
CC -!- SUBUNIT: Monomer. Interacts with CRX. {ECO:0000250|UniProtKB:P45446}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16574740}. Nucleus,
CC nucleoplasm {ECO:0000250|UniProtKB:Q92753}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=2;
CC IsoId=Q8R1B8-2; Sequence=Displayed;
CC Name=1;
CC IsoId=Q8R1B8-1; Sequence=VSP_022576;
CC -!- TISSUE SPECIFICITY: Expressed in inner and outer neuroblastic layer as
CC well as in the ganglion cell layer of the developing retina. Expressed
CC in bone marrow osteoprogenitor cells. {ECO:0000269|PubMed:16574740,
CC ECO:0000269|PubMed:21799210, ECO:0000269|PubMed:22189870,
CC ECO:0000269|PubMed:23652001, ECO:0000269|PubMed:9670004}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the lateral cortical plate at 18.5
CC dpc and only very weakly expressed by cortical neurons at 15.5 dpc.
CC Expression progressively increases in layer IV neurons of the
CC prospective somatosensory, visual and auditory cortices. At much lower
CC levels, also expressed by scattered neurons in layer V in these areas.
CC By P4, expression is striking in the whisker barrel cortex of the
CC somatosensory cortex. During retinal development, isoform 1 is broadly
CC expressed in between 13.5 dpc and P5 then declines and is maintained at
CC lower levels into adulthood. At 15.5 dpc, is expressed in the immature
CC cochlea, brainstem, spinal cord and cerebral cortex. Isoform 2 is first
CC detected at low levels at late embryonic stages (18.5 dpc), the
CC expression highly increases during the first postnatal week and is
CC maintained during the adulthood. {ECO:0000269|PubMed:16574740,
CC ECO:0000269|PubMed:21799210}.
CC -!- INDUCTION: Induced by aging in bone marrow.
CC {ECO:0000269|PubMed:22189870}.
CC -!- DOMAIN: AF-2 (activation function-2) motif is required for recruiting
CC coregulators containing the LXXLL motif, such as NCOA1, and control the
CC transactivational activity. {ECO:0000250|UniProtKB:P45446}.
CC -!- DISRUPTION PHENOTYPE: Mice are blind, show juvenile ataxia, duck gait,
CC hind paw clasping reflex as well as delayed onset of male fertility.
CC They suffer a degeneration of the retina during postnatal development
CC with severe defects in photoreceptor cell morphology. Mice display
CC reduced anxiety and learned helplessness-related behaviors. They also
CC show a significant increase of the circadian period. Knockouts for
CC isoform 1 display duck gait and lack amacrine and horizontal cells with
CC an excess of ganglion cells in the retina (PubMed:23652001).
CC {ECO:0000269|PubMed:16574740, ECO:0000269|PubMed:17303680,
CC ECO:0000269|PubMed:19805139, ECO:0000269|PubMed:23652001,
CC ECO:0000269|PubMed:9670004}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH24842.2; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=AAH58269.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; BC024842; AAH24842.2; ALT_SEQ; mRNA.
DR EMBL; BC058269; AAH58269.1; ALT_SEQ; mRNA.
DR EMBL; DQ779923; ABG77269.1; -; mRNA.
DR EMBL; DQ779924; ABG77270.1; -; mRNA.
DR EMBL; AB258405; BAE93688.1; -; mRNA.
DR CCDS; CCDS37932.1; -. [Q8R1B8-1]
DR CCDS; CCDS37933.1; -. [Q8R1B8-2]
DR RefSeq; NP_001036819.1; NM_001043354.2. [Q8R1B8-1]
DR RefSeq; NP_001276850.1; NM_001289921.1.
DR RefSeq; NP_666207.3; NM_146095.4. [Q8R1B8-2]
DR AlphaFoldDB; Q8R1B8; -.
DR SMR; Q8R1B8; -.
DR BioGRID; 230457; 8.
DR IntAct; Q8R1B8; 5.
DR STRING; 10090.ENSMUSP00000047597; -.
DR iPTMnet; Q8R1B8; -.
DR PhosphoSitePlus; Q8R1B8; -.
DR PaxDb; Q8R1B8; -.
DR PRIDE; Q8R1B8; -.
DR ProteomicsDB; 301593; -. [Q8R1B8-2]
DR ProteomicsDB; 301594; -. [Q8R1B8-1]
DR Antibodypedia; 1699; 413 antibodies from 31 providers.
DR DNASU; 225998; -.
DR Ensembl; ENSMUST00000040153; ENSMUSP00000047597; ENSMUSG00000036192. [Q8R1B8-2]
DR Ensembl; ENSMUST00000112832; ENSMUSP00000108451; ENSMUSG00000036192. [Q8R1B8-1]
DR GeneID; 225998; -.
DR KEGG; mmu:225998; -.
DR UCSC; uc008gyc.2; mouse. [Q8R1B8-2]
DR UCSC; uc008gye.2; mouse. [Q8R1B8-1]
DR CTD; 6096; -.
DR MGI; MGI:1343464; Rorb.
DR VEuPathDB; HostDB:ENSMUSG00000036192; -.
DR eggNOG; KOG4216; Eukaryota.
DR GeneTree; ENSGT00940000157708; -.
DR HOGENOM; CLU_007368_2_0_1; -.
DR InParanoid; Q8R1B8; -.
DR OMA; TIACKIC; -.
DR OrthoDB; 583704at2759; -.
DR PhylomeDB; Q8R1B8; -.
DR TreeFam; TF319910; -.
DR Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
DR BioGRID-ORCS; 225998; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Rorb; mouse.
DR PRO; PR:Q8R1B8; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8R1B8; protein.
DR Bgee; ENSMUSG00000036192; Expressed in cortical layer IV and 127 other tissues.
DR ExpressionAtlas; Q8R1B8; baseline and differential.
DR Genevisible; Q8R1B8; MM.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:GO_Central.
DR GO; GO:0008502; F:melatonin receptor activity; ISO:MGI.
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; IDA:NTNU_SB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0035881; P:amacrine cell differentiation; IMP:UniProtKB.
DR GO; GO:0071300; P:cellular response to retinoic acid; ISS:UniProtKB.
DR GO; GO:0042462; P:eye photoreceptor cell development; IMP:UniProtKB.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:UniProtKB.
DR GO; GO:0046549; P:retinal cone cell development; IDA:UniProtKB.
DR GO; GO:0046548; P:retinal rod cell development; IMP:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd06968; NR_DBD_ROR; 1.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR044101; NR_DBD_ROR.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR003079; ROR_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; PR01293; RORNUCRECPTR.
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 Activator; Alternative promoter usage; Biological rhythms;
KW Developmental protein; DNA-binding; Metal-binding; Nucleus; Receptor;
KW Reference proteome; Sensory transduction; Transcription;
KW Transcription regulation; Vision; Zinc; Zinc-finger.
FT CHAIN 1..470
FT /note="Nuclear receptor ROR-beta"
FT /id="PRO_0000053515"
FT DOMAIN 222..460
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 18..93
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 21..41
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 57..81
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 104..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 456..461
FT /note="AF-2"
FT VAR_SEQ 1..13
FT /note="MCENQPKTKADGT -> MR (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:16574740, ECO:0000303|Ref.2"
FT /id="VSP_022576"
FT CONFLICT 107
FT /note="E -> G (in Ref. 2; BAE93688)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="M -> L (in Ref. 2; BAE93688)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="Q -> H (in Ref. 2; BAE93688)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 470 AA; 53118 MW; 6E2F30DB56E94B86 CRC64;
MCENQPKTKA DGTAQIEVIP CKICGDKSSG IHYGVITCEG CKGFFRRSQQ NNASYSCPRQ
RNCLIDRTNR NRCQHCRLQK CLALGMSRDA VKFGRMSKKQ RDSLYAEVQK HQQRLQEQRQ
QQSGEAEALA RVYSSSISNG LSNLNTETGG TYANGHVIDL PKSEGYYSID SGQPSPDQSG
LDMTGIKQIK QEPIYDLTSV PNLFTYSSFN NGQLAPGITM SEIDRIAQNI IKSHLETCQY
TMEELHQLAW QTHTYEEIKA YQSKSREALW QQCAIQITHA IQYVVEFAKR ITGFMELCQN
DQILLLKSGC LEVVLVRMCR AFNPLNNTVL FEGKYGGMQM FKALGSDDLV NEAFDFAKNL
CSLQLTEEEI ALFSSAVLIS PDRAWLIEPR KVQKLQEKIY FALQHVIQKN HLDDETLAKL
IAKIPTITAV CNLHGEKLQV FKQSHPDIVN TLFPPLYKEL FNPDCAAVCK