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Nuclear receptor ROR-alpha (Nuclear receptor RZR-alpha) (Nuclear receptor subfamily 1 group F member 1) (RAR-related orphan receptor A) (Retinoid-related orphan receptor-alpha)

 RORA_MOUSE              Reviewed;         523 AA.
P51448; P70283; P97741; P97773; Q923G1;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
17-JUN-2020, entry version 193.
RecName: Full=Nuclear receptor ROR-alpha;
AltName: Full=Nuclear receptor RZR-alpha;
AltName: Full=Nuclear receptor subfamily 1 group F member 1;
AltName: Full=RAR-related orphan receptor A;
AltName: Full=Retinoid-related orphan receptor-alpha;
Name=Rora; Synonyms=Nr1f1, Rzra;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Cerebellum;
PubMed=8602221; DOI=10.1038/379736a0;
Hamilton B.A., Frankel W.N., Kerrebrock A.W., Hawkins T.L., Fitzhugh W.,
Kusumi K., Russell L.B., Mueller K.L., Vanberkel V., Birren B.W.,
Kruglyak L., Lander E.S.;
"Disruption of the nuclear hormone receptor RORalpha in staggerer mice.";
Nature 379:736-739(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
STRAIN=C57BL/6J; TISSUE=Skin;
PubMed=7935491; DOI=10.1210/mend.8.6.7935491;
Carlberg C., Hooft van Huijsduijnen R., Staple J.K., Delamarter J.F.,
Becker-Andre M.;
"RZRs, a new family of retinoid-related orphan receptors that function as
both monomers and homodimers.";
Mol. Endocrinol. 8:757-770(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND VARIANT SG 275-HIS--LYS-314
DEL.
STRAIN=C57BL/6J; TISSUE=Cerebellum;
PubMed=9226375; DOI=10.1006/geno.1997.4757;
Matysiak-Scholze U., Nehls M.C.;
"The structural integrity of ROR alpha isoforms is mutated in staggerer
mice: cerebellar coexpression of ROR alpha1 and ROR alpha4.";
Genomics 43:78-84(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
TISSUE=Brain;
PubMed=8750880; DOI=10.1016/0169-328x(95)00126-d;
Matsui T., Sashihara S., Oh Y., Waxman S.G.;
"An orphan nuclear receptor, mROR alpha, and its spatial expression in
adult mouse brain.";
Brain Res. Mol. Brain Res. 33:217-226(1995).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
STRAIN=FVB/N; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 39-61, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[7]
FUNCTION IN TRIGLYCERIDE METABOLISM, DNA-BINDING, AND CHARACTERIZATION OF
VARIANT SG PHENOTYPE.
PubMed=11053433; DOI=10.1074/jbc.m004982200;
Raspe E., Duez H., Gervois P., Fievet C., Fruchart J.C., Besnard S.,
Mariani J., Tedgui A., Staels B.;
"Transcriptional regulation of apolipoprotein C-III gene expression by the
orphan nuclear receptor RORalpha.";
J. Biol. Chem. 276:2865-2871(2001).
[8]
FUNCTION IN CEREBELLAR DEVELOPMENT, DEVELOPMENTAL STAGE, INTERACTION WITH
CTNNB1, AND CHARACTERIZATION OF VARIANT SG PHENOTYPE.
PubMed=14687547; DOI=10.1016/s0896-6273(03)00769-4;
Gold D.A., Baek S.H., Schork N.J., Rose D.W., Larsen D.D., Sachs B.D.,
Rosenfeld M.G., Hamilton B.A.;
"RORalpha coordinates reciprocal signaling in cerebellar development
through sonic hedgehog and calcium-dependent pathways.";
Neuron 40:1119-1131(2003).
[9]
FUNCTION IN CIRCADIAN RHYTHMS, AND CHARACTERIZATION OF VARIANT SG
PHENOTYPE.
PubMed=15821743; DOI=10.1038/nsmb925;
Akashi M., Takumi T.;
"The orphan nuclear receptor RORalpha regulates circadian transcription of
the mammalian core-clock Bmal1.";
Nat. Struct. Mol. Biol. 12:441-448(2005).
[10]
INTERACTION WITH PPARGC1A.
PubMed=17476214; DOI=10.1038/nature05767;
Liu C., Li S., Liu T., Borjigin J., Lin J.D.;
"Transcriptional coactivator PGC-1alpha integrates the mammalian clock and
energy metabolism.";
Nature 447:477-481(2007).
[11]
FUNCTION IN METABOLISM REGULATION, CHARACTERIZATION OF VARIANT SG
PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=17666523; DOI=10.1152/physiolgenomics.00098.2007;
Kang H.S., Angers M., Beak J.Y., Wu X., Gimble J.M., Wada T., Xie W.,
Collins J.B., Grissom S.F., Jetten A.M.;
"Gene expression profiling reveals a regulatory role for ROR alpha and ROR
gamma in phase I and phase II metabolism.";
Physiol. Genomics 31:281-294(2007).
[12]
FUNCTION IN METABOLISM REGULATION, CHARACTERIZATION OF VARIANT SG
PHENOTYPE, AND DNA-BINDING.
PubMed=18055760; DOI=10.1124/mol.107.040741;
Wada T., Kang H.S., Angers M., Gong H., Bhatia S., Khadem S., Ren S.,
Ellis E., Strom S.C., Jetten A.M., Xie W.;
"Identification of oxysterol 7alpha-hydroxylase (Cyp7b1) as a novel
retinoid-related orphan receptor alpha (RORalpha) (NR1F1) target gene and a
functional cross-talk between RORalpha and liver X receptor (NR1H3).";
Mol. Pharmacol. 73:891-899(2008).
[13]
REVIEW OF FUNCTION IN METABOLISM REGULATION.
PubMed=18535165; DOI=10.3181/0802-mr-50;
Wada T., Kang H.S., Jetten A.M., Xie W.;
"The emerging role of nuclear receptor RORalpha and its crosstalk with LXR
in xeno- and endobiotic gene regulation.";
Exp. Biol. Med. 233:1191-1201(2008).
[14]
FUNCTION IN T(H)17 CELLS DIFFERENTIATION, INDUCTION BY IL6 AND TGFB1, AND
TISSUE SPECIFICITY.
PubMed=18164222; DOI=10.1016/j.immuni.2007.11.016;
Yang X.O., Pappu B.P., Nurieva R., Akimzhanov A., Kang H.S., Chung Y.,
Ma L., Shah B., Panopoulos A.D., Schluns K.S., Watowich S.S., Tian Q.,
Jetten A.M., Dong C.;
"T helper 17 lineage differentiation is programmed by orphan nuclear
receptors ROR alpha and ROR gamma.";
Immunity 28:29-39(2008).
[15]
FUNCTION IN LIPID METABOLISM REGULATION, TISSUE SPECIFICITY, AND
CHARACTERIZATION OF VARIANT SG PHENOTYPE.
PubMed=18441015; DOI=10.1074/jbc.m710526200;
Lau P., Fitzsimmons R.L., Raichur S., Wang S.C., Lechtken A., Muscat G.E.;
"The orphan nuclear receptor, RORalpha, regulates gene expression that
controls lipid metabolism: staggerer (SG/SG) mice are resistant to diet-
induced obesity.";
J. Biol. Chem. 283:18411-18421(2008).
[16]
INTERACTION WITH NCOA2.
PubMed=19039140; DOI=10.1126/science.1164847;
Chopra A.R., Louet J.F., Saha P., An J., Demayo F., Xu J., York B.,
Karpen S., Finegold M., Moore D., Chan L., Newgard C.B., O'Malley B.W.;
"Absence of the SRC-2 coactivator results in a glycogenopathy resembling
Von Gierke's disease.";
Science 322:1395-1399(2008).
[17]
FUNCTION, DEVELOPMENTAL STAGE, AND CHARACTERIZATION OF VARIANT SG.
PubMed=19014374; DOI=10.1111/j.1471-4159.2008.05739.x;
Fujieda H., Bremner R., Mears A.J., Sasaki H.;
"Retinoic acid receptor-related orphan receptor alpha regulates a subset of
cone genes during mouse retinal development.";
J. Neurochem. 108:91-101(2009).
[18]
FUNCTION IN ADIPOGENESIS, INTERACTION WITH CEBPB, AND DEVELOPMENTAL STAGE.
PubMed=19324970; DOI=10.1210/me.2008-0277;
Ohoka N., Kato S., Takahashi Y., Hayashi H., Sato R.;
"The orphan nuclear receptor RORalpha restrains adipocyte differentiation
through a reduction of C/EBPbeta activity and perilipin gene expression.";
Mol. Endocrinol. 23:759-771(2009).
[19]
REVIEW ON FUNCTION.
PubMed=19381306; DOI=10.1621/nrs.07003;
Jetten A.M.;
"Retinoid-related orphan receptors (RORs): critical roles in development,
immunity, circadian rhythm, and cellular metabolism.";
Nucl. Recept. Signal. 7:3-35(2009).
[20]
INTERACTION WITH MAGED1.
PubMed=20300063; DOI=10.1038/emboj.2010.34;
Wang X., Tang J., Xing L., Shi G., Ruan H., Gu X., Liu Z., Wu X., Gao X.,
Xu Y.;
"Interaction of MAGED1 with nuclear receptors affects circadian clock
function.";
EMBO J. 29:1389-1400(2010).
[21]
INTERACTION WITH PER2.
PubMed=20159955; DOI=10.1101/gad.564110;
Schmutz I., Ripperger J.A., Baeriswyl-Aebischer S., Albrecht U.;
"The mammalian clock component PERIOD2 coordinates circadian output by
interaction with nuclear receptors.";
Genes Dev. 24:345-357(2010).
[22]
FUNCTION IN GLUCOSE METABOLISM REGULATION, AND IDENTIFICATION OF LIGANDS.
PubMed=19965867; DOI=10.1074/jbc.m109.080614;
Wang Y., Kumar N., Solt L.A., Richardson T.I., Helvering L.M., Crumbley C.,
Garcia-Ordonez R.D., Stayrook K.R., Zhang X., Novick S., Chalmers M.J.,
Griffin P.R., Burris T.P.;
"Modulation of retinoic acid receptor-related orphan receptor alpha and
gamma activity by 7-oxygenated sterol ligands.";
J. Biol. Chem. 285:5013-5025(2010).
[23]
FUNCTION, AND INTERACTION WITH NRIP1.
PubMed=21628546; DOI=10.1177/0748730411401579;
Poliandri A.H., Gamsby J.J., Christian M., Spinella M.J., Loros J.J.,
Dunlap J.C., Parker M.G.;
"Modulation of clock gene expression by the transcriptional coregulator
receptor interacting protein 140 (RIP140).";
J. Biol. Rhythms 26:187-199(2011).
[24]
FUNCTION IN T(H)17 CELLS DIFFERENTIATION, INDUCTION BY IL6 AND TGFB1,
INTERACTION WITH NCOR1 AND NCOA2, AND IDENTIFICATION OF LIGANDS.
PubMed=21499262; DOI=10.1038/nature10075;
Solt L.A., Kumar N., Nuhant P., Wang Y., Lauer J.L., Liu J., Istrate M.A.,
Kamenecka T.M., Roush W.R., Vidovic D., Schuerer S.C., Xu J., Wagoner G.,
Drew P.D., Griffin P.R., Burris T.P.;
"Suppression of TH17 differentiation and autoimmunity by a synthetic ROR
ligand.";
Nature 472:491-494(2011).
[25]
INTERACTION WITH CRY1.
PubMed=22170608; DOI=10.1038/nature10700;
Lamia K.A., Papp S.J., Yu R.T., Barish G.D., Uhlenhaut N.H., Jonker J.W.,
Downes M., Evans R.M.;
"Cryptochromes mediate rhythmic repression of the glucocorticoid
receptor.";
Nature 480:552-556(2011).
[26]
FUNCTION IN CIRCADIAN RHYTHMS, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
DNA-BINDING, AND INDUCTION.
PubMed=22753030; DOI=10.1093/nar/gks630;
Takeda Y., Jothi R., Birault V., Jetten A.M.;
"RORgamma directly regulates the circadian expression of clock genes and
downstream targets in vivo.";
Nucleic Acids Res. 40:8519-8535(2012).
[27]
REVIEW ON FUNCTION AND LIGANDS.
PubMed=22789990; DOI=10.1016/j.tem.2012.05.012;
Solt L.A., Burris T.P.;
"Action of RORs and their ligands in (patho)physiology.";
Trends Endocrinol. Metab. 23:619-627(2012).
[28]
FUNCTION, AND INDUCTION.
PubMed=23172836; DOI=10.1161/circulationaha.112.135608;
Saito T., Hirano M., Ide T., Ichiki T., Koibuchi N., Sunagawa K.,
Hirano K.;
"Pivotal role of Rho-associated kinase 2 in generating the intrinsic
circadian rhythm of vascular contractility.";
Circulation 127:104-114(2013).
[29]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PROX1.
PubMed=23723244; DOI=10.1093/nar/gkt447;
Takeda Y., Jetten A.M.;
"Prospero-related homeobox 1 (Prox1) functions as a novel modulator of
retinoic acid-related orphan receptors alpha- and gamma-mediated
transactivation.";
Nucleic Acids Res. 41:6992-7008(2013).
-!- FUNCTION: Nuclear receptor that binds DNA as a monomer to ROR response
elements (RORE) containing a single core motif half-site 5'-AGGTCA-3'
preceded by a short A-T-rich sequence. Key regulator of embryonic
development, cellular differentiation, immunity, circadian rhythm as
well as lipid, steroid, xenobiotics and glucose metabolism. Considered
to have intrinsic transcriptional activity, have some natural ligands
like oxysterols that act as agonists (25-hydroxycholesterol) or inverse
agonists (7-oxygenated sterols), enhancing or repressing the
transcriptional activity, respectively. Recruits distinct combinations
of cofactors to target genes regulatory regions to modulate their
transcriptional expression, depending on the tissue, time and promoter
contexts. Regulates genes involved in photoreceptor development
including OPN1SW, OPN1SM and ARR3 and skeletal muscle development with
MYOD1. Required for proper cerebellum development, regulates SHH gene
expression, among others, to induce granule cells proliferation as well
as expression of genes involved in calcium-mediated signal
transduction. Regulates the circadian expression of several clock
genes, including CLOCK, ARNTL/BMAL1, NPAS2 and CRY1. Competes with
NR1D1 for binding to their shared DNA response element on some clock
genes such as ARNTL/BMAL1, CRY1 and NR1D1 itself, resulting in NR1D1-
mediated repression or RORA-mediated activation of clock genes
expression, leading to the circadian pattern of clock genes expression.
Therefore influences the period length and stability of the clock.
Regulates genes involved in lipid metabolism such as apolipoproteins
APOA1, APOA5, APOC3 and PPARG. In liver, has specific and redundant
functions with RORC as positive or negative modulator of expression of
genes encoding phase I and phase II proteins involved in the metabolism
of lipids, steroids and xenobiotics, such as CYP7B1 and SULT2A1.
Induces a rhythmic expression of some of these genes. In addition,
interplays functionally with NR1H2 and NR1H3 for the regulation of
genes involved in cholesterol metabolism. Also involved in the
regulation of hepatic glucose metabolism through the modulation of G6PC
and PCK1. In adipose tissue, plays a role as negative regulator of
adipocyte differentiation, probably acting through dual mechanisms. May
suppress CEBPB-dependent adipogenesis through direct interaction and
PPARG-dependent adipogenesis through competition for DNA-binding.
Downstream of IL6 and TGFB and synergistically with RORC isoform 2, is
implicated in the lineage specification of uncommitted CD4(+) T-helper
(T(H)) cells into T(H)17 cells, antagonizing the T(H)1 program.
Probably regulates IL17 and IL17F expression on T(H) by binding to the
essential enhancer conserved non-coding sequence 2 (CNS2) in the IL17-
IL17F locus. Involved in hypoxia signaling by interacting with and
activating the transcriptional activity of HIF1A. May inhibit cell
growth in response to cellular stress. May exert an anti-inflammatory
role by inducing CHUK expression and inhibiting NF-kappa-B signaling.
{ECO:0000269|PubMed:11053433, ECO:0000269|PubMed:14687547,
ECO:0000269|PubMed:15821743, ECO:0000269|PubMed:17666523,
ECO:0000269|PubMed:18055760, ECO:0000269|PubMed:18164222,
ECO:0000269|PubMed:18441015, ECO:0000269|PubMed:19014374,
ECO:0000269|PubMed:19324970, ECO:0000269|PubMed:19965867,
ECO:0000269|PubMed:21499262, ECO:0000269|PubMed:21628546,
ECO:0000269|PubMed:22753030, ECO:0000269|PubMed:23172836,
ECO:0000269|PubMed:23723244}.
-!- SUBUNIT: Monomer. Interacts (via the DNA-binding domain) with HIF1A;
the interaction enhances HIF1A transcription under hypoxia through
increasing protein stability. Interacts with CEBPB; the interaction
disrupts the interaction CEBPB:EP300. Interacts with the coactivators
NCOA2, PPARGC1A (via LXXLL motif), EP300 and MED1. Interacts with the
corepressor NCOR1. Interacts with MAGED1 and CTNNB1. Interacts with
CRY1 and PER2. Interacts (via AF-2 motif) with PROX1. Interacts with
NRIP1. Isoform 4 interacts (via AF-2 motif) with isoform 1 of FOXP3
(via LXXLL motif) (By similarity). {ECO:0000250|UniProtKB:P35398,
ECO:0000269|PubMed:14687547, ECO:0000269|PubMed:17476214,
ECO:0000269|PubMed:19039140, ECO:0000269|PubMed:19324970,
ECO:0000269|PubMed:20159955, ECO:0000269|PubMed:20300063,
ECO:0000269|PubMed:21499262, ECO:0000269|PubMed:21628546,
ECO:0000269|PubMed:22170608, ECO:0000269|PubMed:23723244}.
-!- INTERACTION:
P51448; P54254: Atxn1; NbExp=3; IntAct=EBI-1169722, EBI-1169713;
P51448; Q9QYH6: Maged1; NbExp=5; IntAct=EBI-1169722, EBI-1801274;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407,
ECO:0000269|PubMed:22753030, ECO:0000269|PubMed:23723244}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage; Named isoforms=4;
Name=1; Synonyms=Alpha-1;
IsoId=P51448-1; Sequence=Displayed;
Name=2; Synonyms=Alpha-2;
IsoId=P51448-3; Sequence=Not described;
Name=3; Synonyms=Alpha-3;
IsoId=P51448-4; Sequence=Not described;
Name=4; Synonyms=Alpha-4;
IsoId=P51448-2; Sequence=VSP_003658;
-!- TISSUE SPECIFICITY: Expressed in cerebellum, heart, liver, lung,
kidney, retina and brown and white adipose tissues. Expressed in the
subset of mature Th17 cells. {ECO:0000269|PubMed:17666523,
ECO:0000269|PubMed:18164222, ECO:0000269|PubMed:18441015,
ECO:0000269|PubMed:22753030}.
-!- DEVELOPMENTAL STAGE: In cerebellum, expression begins at 12.5 dpc. In
the developing retina, first expressed at 17 dpc in the ganglion cell
layer. At P3, expressed in the inner border of the neuroblasitic border
(presumptive amacrine cells). By P6, levels increase in developing
cones. Expression found in the presumptive bipolar cells by P9. During
adipocyte differentiation, expression gradually increases.
{ECO:0000269|PubMed:14687547, ECO:0000269|PubMed:19014374,
ECO:0000269|PubMed:19324970}.
-!- INDUCTION: In T(H) cells, induced upon antigen receptor ligation in the
presence of IL6 and TGB1 (via STAT3). Oscillates diurnally in central
nervous system. In liver, Isoform 1 oscillates diurnally but not
isoform 4. {ECO:0000269|PubMed:18164222, ECO:0000269|PubMed:21499262,
ECO:0000269|PubMed:22753030, ECO:0000269|PubMed:23172836}.
-!- DOMAIN: The AF-2 (activation function-2) motif is required for
recruiting coregulators containing LXXLL motifs.
{ECO:0000250|UniProtKB:P35398}.
-!- PTM: Phosphorylation by conventional PKCs in neurons inhibits
transcriptional activity. Phosphorylated on Thr-183 by MAPK1/ERK1 in
vitro. {ECO:0000250|UniProtKB:P35398}.
-!- PTM: Sumoylated by SENP1 and SENP2. Sumoylation, promoted by PIAS2,
PIAS3, PIAS4 but not PIAS1, enhances the transcriptional activity.
Desumoylated by SENP1. {ECO:0000250|UniProtKB:P35398}.
-!- PTM: Ubiquitinated, leading to its degradation by the proteasome.
Proteasomal degradation is required for efficient transcriptional
activity and is prevented by HR. {ECO:0000250|UniProtKB:P35398}.
-!- PTM: [Isoform 1]: monomethylated at Lys-38 by EZH2, this creates a
degron recognized by a DCX (DDB1-DCAF1/VPRBP-CUL4A-RBX1) E3 ubiquitin
ligase complex. {ECO:0000250|UniProtKB:P35398}.
-!- DISEASE: Note=Defects in Rora are the cause of the staggerer (SG)
mutant phenotype which is characterized by disturbance of Purkinje cell
development and immune system functioning. This phenotype exhibits
lower body weight, reduced adiposity, decreased plasma cholesterol,
triglyceride and apolipoprotein CIII levels, and is resistant to diet-
induced obesity. Also has abnormal circadian rhythms.
{ECO:0000269|PubMed:11053433, ECO:0000269|PubMed:14687547,
ECO:0000269|PubMed:15821743, ECO:0000269|PubMed:17666523,
ECO:0000269|PubMed:18055760, ECO:0000269|PubMed:18441015,
ECO:0000269|PubMed:19014374, ECO:0000269|PubMed:9226375}.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH03757.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
Sequence=CAA69930.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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EMBL; U53228; AAC52513.1; -; mRNA.
EMBL; Y08640; CAA69930.1; ALT_INIT; mRNA.
EMBL; Z82994; CAB05396.1; -; mRNA.
EMBL; S82720; AAB46801.2; -; mRNA.
EMBL; D45910; BAA22970.1; -; mRNA.
EMBL; BC003757; AAH03757.2; ALT_INIT; mRNA.
CCDS; CCDS23314.1; -. [P51448-1]
CCDS; CCDS72268.1; -. [P51448-2]
PIR; S68517; S68517.
RefSeq; NP_001276845.1; NM_001289916.1. [P51448-2]
RefSeq; NP_038674.1; NM_013646.2. [P51448-1]
SMR; P51448; -.
BioGRID; 202956; 1.
CORUM; P51448; -.
DIP; DIP-35351N; -.
IntAct; P51448; 3.
MINT; P51448; -.
STRING; 10090.ENSMUSP00000034766; -.
ChEMBL; CHEMBL3217403; -.
iPTMnet; P51448; -.
PhosphoSitePlus; P51448; -.
PaxDb; P51448; -.
PeptideAtlas; P51448; -.
PRIDE; P51448; -.
Antibodypedia; 4080; 542 antibodies.
Ensembl; ENSMUST00000034766; ENSMUSP00000034766; ENSMUSG00000032238. [P51448-1]
Ensembl; ENSMUST00000113624; ENSMUSP00000109254; ENSMUSG00000032238. [P51448-2]
GeneID; 19883; -.
KEGG; mmu:19883; -.
UCSC; uc009qmx.2; mouse. [P51448-1]
CTD; 6095; -.
MGI; MGI:104661; Rora.
eggNOG; KOG4216; Eukaryota.
eggNOG; ENOG410XUGR; LUCA.
GeneTree; ENSGT00940000157387; -.
HOGENOM; CLU_007368_2_0_1; -.
InParanoid; P51448; -.
KO; K08532; -.
OMA; FKSLAGC; -.
PhylomeDB; P51448; -.
TreeFam; TF319910; -.
Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
Reactome; R-MMU-4090294; SUMOylation of intracellular receptors.
BioGRID-ORCS; 19883; 0 hits in 12 CRISPR screens.
ChiTaRS; Rora; mouse.
PRO; PR:P51448; -.
Proteomes; UP000000589; Chromosome 9.
RNAct; P51448; protein.
Bgee; ENSMUSG00000032238; Expressed in medial geniculate body and 334 other tissues.
ExpressionAtlas; P51448; baseline and differential.
Genevisible; P51448; MM.
GO; GO:0042025; C:host cell nucleus; IEA:InterPro.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0008013; F:beta-catenin binding; IPI:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
GO; GO:0098531; F:ligand-activated transcription factor activity; ISS:UniProtKB.
GO; GO:0004879; F:nuclear receptor activity; IEA:InterPro.
GO; GO:0008142; F:oxysterol binding; ISS:UniProtKB.
GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0003707; F:steroid hormone receptor activity; IEA:InterPro.
GO; GO:0001223; F:transcription coactivator binding; IPI:UniProtKB.
GO; GO:0001222; F:transcription corepressor binding; ISO:MGI.
GO; GO:0008134; F:transcription factor binding; ISO:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
GO; GO:0071456; P:cellular response to hypoxia; ISS:UniProtKB.
GO; GO:0071347; P:cellular response to interleukin-1; IDA:MGI.
GO; GO:0036315; P:cellular response to sterol; ISS:UniProtKB.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:MGI.
GO; GO:0021930; P:cerebellar granule cell precursor proliferation; IMP:UniProtKB.
GO; GO:0021702; P:cerebellar Purkinje cell differentiation; IMP:MGI.
GO; GO:0046068; P:cGMP metabolic process; IMP:MGI.
GO; GO:0042632; P:cholesterol homeostasis; IMP:UniProtKB.
GO; GO:0032922; P:circadian regulation of gene expression; IDA:UniProtKB.
GO; GO:0030522; P:intracellular receptor signaling pathway; ISS:UniProtKB.
GO; GO:0042692; P:muscle cell differentiation; ISS:UniProtKB.
GO; GO:0045599; P:negative regulation of fat cell differentiation; IMP:UniProtKB.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
GO; GO:0050728; P:negative regulation of inflammatory response; ISS:UniProtKB.
GO; GO:0006809; P:nitric oxide biosynthetic process; IMP:MGI.
GO; GO:0042753; P:positive regulation of circadian rhythm; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; ISS:UniProtKB.
GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
GO; GO:0010906; P:regulation of glucose metabolic process; IMP:UniProtKB.
GO; GO:0043030; P:regulation of macrophage activation; IMP:MGI.
GO; GO:0008589; P:regulation of smoothened signaling pathway; IMP:UniProtKB.
GO; GO:0019218; P:regulation of steroid metabolic process; IMP:UniProtKB.
GO; GO:0060850; P:regulation of transcription involved in cell fate commitment; IDA:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0072539; P:T-helper 17 cell differentiation; IMP:UniProtKB.
GO; GO:0070328; P:triglyceride homeostasis; IMP:UniProtKB.
GO; GO:0006805; P:xenobiotic metabolic process; IMP:UniProtKB.
Gene3D; 1.10.565.10; -; 1.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR035500; NHR-like_dom_sf.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
InterPro; IPR003079; ROR_rcpt.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF00105; zf-C4; 1.
PRINTS; PR01293; RORNUCRECPTR.
PRINTS; PR00398; STRDHORMONER.
PRINTS; PR00047; STROIDFINGER.
SMART; SM00430; HOLI; 1.
SMART; SM00399; ZnF_C4; 1.
SUPFAM; SSF48508; SSF48508; 1.
PROSITE; PS51843; NR_LBD; 1.
PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
1: Evidence at protein level;
Activator; Alternative promoter usage; Biological rhythms;
Developmental protein; Direct protein sequencing; Disease mutation;
DNA-binding; Isopeptide bond; Metal-binding; Methylation; Nucleus;
Phosphoprotein; Receptor; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1..523
/note="Nuclear receptor ROR-alpha"
/id="PRO_0000053513"
DOMAIN 272..510
/note="NR LBD"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
DNA_BIND 73..138
/note="Nuclear receptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
ZN_FING 73..93
/note="NR C4-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
ZN_FING 109..133
/note="NR C4-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
MOTIF 506..511
/note="AF-2"
COMPBIAS 101..175
/note="Gln-rich"
MOD_RES 38
/note="N6-methyllysine"
/evidence="ECO:0000250|UniProtKB:P35398"
MOD_RES 183
/note="Phosphothreonine; by MAPK1"
/evidence="ECO:0000250|UniProtKB:P35398"
CROSSLNK 240
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO)"
/evidence="ECO:0000250"
VAR_SEQ 1..66
/note="MESAPAAPDPAASEPGSSGSEAAAGSRETPLTQDTGRKSEAPGAGRRQSYAS
SSRGISVTKKTHTS -> MYFVIAAMKA (in isoform 4)"
/evidence="ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7935491, ECO:0000303|PubMed:8750880,
ECO:0000303|PubMed:9226375"
/id="VSP_003658"
VARIANT 275..314
/note="Missing (in SG; disturbance of Purkinje cell and
muscle development, lipid metabolism, circadian behavior
and immune system functioning)"
/evidence="ECO:0000269|PubMed:9226375"
CONFLICT 163
/note="H -> R (in Ref. 2; CAA69930)"
/evidence="ECO:0000305"
CONFLICT 180..181
/note="EP -> T (in Ref. 2; CAA69930)"
/evidence="ECO:0000305"
CONFLICT 182
/note="L -> I (in Ref. 4; AAB46801/BAA22970)"
/evidence="ECO:0000305"
CONFLICT 193..194
/note="LT -> SA (in Ref. 2; CAA69930)"
/evidence="ECO:0000305"
CONFLICT 304
/note="L -> W (in Ref. 2; CAA69930)"
/evidence="ECO:0000305"
CONFLICT 315
/note="Missing (in Ref. 4; AAB46801/BAA22970)"
/evidence="ECO:0000305"
CONFLICT 362
/note="E -> G (in Ref. 2; CAA69930)"
/evidence="ECO:0000305"
CONFLICT 433
/note="R -> P (in Ref. 2; CAA69930)"
/evidence="ECO:0000305"
CONFLICT 450..451
/note="QL -> HM (in Ref. 2; CAA69930)"
/evidence="ECO:0000305"
CONFLICT 487
/note="K -> N (in Ref. 4; AAB46801/BAA22970)"
/evidence="ECO:0000305"
SEQUENCE 523 AA; 58845 MW; A194E02E4D9D177E CRC64;
MESAPAAPDP AASEPGSSGS EAAAGSRETP LTQDTGRKSE APGAGRRQSY ASSSRGISVT
KKTHTSQIEI IPCKICGDKS SGIHYGVITC EGCKGFFRRS QQSNATYSCP RQKNCLIDRT
SRNRCQHCRL QKCLAVGMSR DAVKFGRMSK KQRDSLYAEV QKHRMQQQQR DHQQQPGEAE
PLTPTYNISA NGLTELHDDL STYMDGHTPE GSKADSAVSS FYLDIQPSPD QSGLDINGIK
PEPICDYTPA SGFFPYCSFT NGETSPTVSM AELEHLAQNI SKSHLETCQY LREELQQITW
QTFLQEEIEN YQNKQREVMW QLCAIKITEA IQYVVEFAKR IDGFMELCQN DQIVLLKAGS
LEVVFIRMCR AFDSQNNTVY FDGKYASPDV FKSLGCEDFI SFVFEFGKSL CSMHLTEDEI
ALFSAFVLMS ADRSWLQEKV KIEKLQQKIQ LALQHVLQKN HREDGILTKL ICKVSTLRAL
CGRHTEKLMA FKAIYPDIVR LHFPPLYKEL FTSEFEPAMQ IDG


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Related Genes :
[RORA NR1F1 RZRA] Nuclear receptor ROR-alpha (Nuclear receptor RZR-alpha) (Nuclear receptor subfamily 1 group F member 1) (RAR-related orphan receptor A) (Retinoid-related orphan receptor-alpha)
[Rora Nr1f1 Rzra] Nuclear receptor ROR-alpha (Nuclear receptor RZR-alpha) (Nuclear receptor subfamily 1 group F member 1) (RAR-related orphan receptor A) (Retinoid-related orphan receptor-alpha)
[Rorc Nr1f3 Rorg Thor] Nuclear receptor ROR-gamma (Nuclear receptor RZR-gamma) (Nuclear receptor subfamily 1 group F member 3) (RAR-related orphan receptor C) (Retinoid-related orphan receptor-gamma) (Thymus orphan receptor) (TOR)
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[RORB NR1F2 RZRB] Nuclear receptor ROR-beta (Nuclear receptor RZR-beta) (Nuclear receptor subfamily 1 group F member 2) (Retinoid-related orphan receptor-beta)
[NR1D2] Nuclear receptor subfamily 1 group D member 2 (Orphan nuclear hormone receptor BD73) (Rev-erb alpha-related receptor) (RVR) (Rev-erb-beta) (V-erbA-related protein 1-related) (EAR-1R)
[NR4A1 GFRP1 HMR NAK1] Nuclear receptor subfamily 4 group A member 1 (Early response protein NAK1) (Nuclear hormone receptor NUR/77) (Nur77) (Orphan nuclear receptor HMR) (Orphan nuclear receptor TR3) (ST-59) (Testicular receptor 3)
[Nr2c2 Mtr2r1 Tak1 Tr4] Nuclear receptor subfamily 2 group C member 2 (Orphan nuclear receptor TAK1) (Orphan nuclear receptor TR4) (Testicular receptor 4)
[NR2C2 TAK1 TR4] Nuclear receptor subfamily 2 group C member 2 (Orphan nuclear receptor TAK1) (Orphan nuclear receptor TR4) (Testicular receptor 4)
[RORC NR1F3] Nuclear receptor ROR-gamma (Nuclear receptor RZR-gamma) (Nuclear receptor subfamily 1 group F member 3) (Retinoid-related orphan receptor-gamma)
[RXRA NR2B1] Retinoic acid receptor RXR-alpha (Nuclear receptor subfamily 2 group B member 1) (Retinoid X receptor alpha)
[THRA EAR7 ERBA1 NR1A1 THRA1 THRA2] Thyroid hormone receptor alpha (Nuclear receptor subfamily 1 group A member 1) (V-erbA-related protein 7) (EAR-7) (c-erbA-1) (c-erbA-alpha)
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[RARA NR1B1] Retinoic acid receptor alpha (RAR-alpha) (Nuclear receptor subfamily 1 group B member 1)
[NR1D1 EAR1 HREV THRAL] Nuclear receptor subfamily 1 group D member 1 (Rev-erbA-alpha) (V-erbA-related protein 1) (EAR-1)
[Esrra Err1 Estrra Nr3b1] Steroid hormone receptor ERR1 (Estrogen receptor-like 1) (Estrogen-related receptor alpha) (ERR-alpha) (Nuclear receptor subfamily 3 group B member 1)
[Rxra Nr2b1] Retinoic acid receptor RXR-alpha (Nuclear receptor subfamily 2 group B member 1) (Retinoid X receptor alpha)
[Nr2c1 Tr2 Tr2-11] Nuclear receptor subfamily 2 group C member 1 (Orphan nuclear receptor TR2) (Testicular receptor 2) (mTR2)
[Nr1d2] Nuclear receptor subfamily 1 group D member 2 (Orphan nuclear receptor RVR) (Rev-erb-beta)
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[Nr4a1 Gfrp Hmr N10 Nur77] Nuclear receptor subfamily 4 group A member 1 (Nuclear hormone receptor NUR/77) (Nuclear protein N10) (Orphan nuclear receptor HMR)
[rxrga nr2b1 nr2b3a rxr rxra rxrg] Retinoic acid receptor RXR-gamma-A (Nuclear receptor subfamily 2 group B member 3-A) (Retinoic acid receptor RXR-alpha) (Retinoid X receptor alpha) (Retinoid X receptor gamma-A)
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[Nr4a1 Hmr Ngfib] Nuclear receptor subfamily 4 group A member 1 (NUR77) (Nerve growth factor-induced protein I-B) (NGFI-B) (Orphan nuclear receptor HMR)
[Nr1d1 Ear1] Nuclear receptor subfamily 1 group D member 1 (Rev-erbA-alpha) (V-erbA-related protein 1) (EAR-1)
[Rxra Nr2b1] Retinoic acid receptor RXR-alpha (Nuclear receptor subfamily 2 group B member 1) (Retinoid X receptor alpha)
[rarab nr1b1b rara2b] Retinoic acid receptor alpha-B (RAR-alpha-B) (Nuclear receptor subfamily 1 group B member 1-B) (Retinoic acid receptor alpha-2.B) (RAR-alpha-2.B)
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[NR1H4 BAR FXR HRR1 RIP14] Bile acid receptor (Farnesoid X-activated receptor) (Farnesol receptor HRR-1) (Nuclear receptor subfamily 1 group H member 4) (Retinoid X receptor-interacting protein 14) (RXR-interacting protein 14)
[NR5A2 B1F CPF FTF] Nuclear receptor subfamily 5 group A member 2 (Alpha-1-fetoprotein transcription factor) (B1-binding factor) (hB1F) (CYP7A promoter-binding factor) (Hepatocytic transcription factor) (Liver receptor homolog 1) (LRH-1)

Bibliography :
[32061868] Melatonin inhibits apoptosis in mouse Leydig cells via the retinoic acid-related orphan nuclear receptor α/p53 pathway.
[31924695] Ser100-Phosphorylated ROR Orchestrates CAR and HNF4 to Form Active Chromatin Complex in Response to Phenobarbital to Regulate Induction of CYP2B6.
[31805036] Mediator MED23 regulates inflammatory responses and liver fibrosis.
[31676672] The Transcription Factor RORα Preserves ILC3 Lineage Identity and Function during Chronic Intestinal Infection.
[31668395] MicroRNA-10a-5p regulates macrophage polarization and promotes therapeutic adipose tissue remodeling.
[31661301] Declining Pulmonary Function in Interstitial Lung Disease Linked to Lymphocyte Dysfunction.
[31524147] MiR-652 serves as a prognostic biomarker in gastric cancer and promotes tumor proliferation, migration, and invasion via targeting RORA.
[31462679] Nobiletin fortifies mitochondrial respiration in skeletal muscle to promote healthy aging against metabolic challenge.
[31409890] Retinoid-related orphan nuclear receptor alpha (RORα)-deficient mice display morphological testicular defects.
[31340215] RORA Overexpression Alleviates Nasal Mucosal Injury and Enhances Red Blood Cell Immune Adhesion Function in a Mouse Model of Allergic Rhinitis via Inactivation of the Wnt/β-Catenin Signaling Pathway.