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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.
20-DEC-2017, entry version 175.
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:
P54254:Atxn1; NbExp=3; IntAct=EBI-1169722, EBI-1169713;
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 E12.5. In
the developing retina, first expressed at E17 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=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAA69930.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; 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]
UniGene; Mm.378450; -.
UniGene; Mm.391890; -.
UniGene; Mm.427266; -.
UniGene; Mm.445802; -.
UniGene; Mm.491288; -.
ProteinModelPortal; P51448; -.
SMR; P51448; -.
BioGrid; 202956; 1.
DIP; DIP-35351N; -.
IntAct; P51448; 3.
STRING; 10090.ENSMUSP00000034766; -.
ChEMBL; CHEMBL3217403; -.
iPTMnet; P51448; -.
PhosphoSitePlus; P51448; -.
PaxDb; P51448; -.
PeptideAtlas; P51448; -.
PRIDE; P51448; -.
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; ENSGT00870000136388; -.
HOGENOM; HOG000010200; -.
HOVERGEN; HBG106848; -.
InParanoid; P51448; -.
KO; K08532; -.
OMA; YQNKPRE; -.
OrthoDB; EOG091G0649; -.
PhylomeDB; P51448; -.
TreeFam; TF319910; -.
Reactome; R-MMU-1368092; Rora activates gene expression.
Reactome; R-MMU-1368110; Bmal1:Clock,Npas2 activates circadian gene expression.
Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
ChiTaRS; Rora; mouse.
PRO; PR:P51448; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000032238; -.
CleanEx; MM_RORA; -.
ExpressionAtlas; P51448; baseline and differential.
Genevisible; P51448; MM.
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:0001046; F:core promoter sequence-specific DNA binding; ISO:MGI.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0004879; F:nuclear receptor activity; IEA:InterPro.
GO; GO:0008142; F:oxysterol binding; ISS:UniProtKB.
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:0098531; F:transcription factor activity, direct ligand regulated sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
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:0032922; P:circadian regulation of gene expression; IDA:UniProtKB.
GO; GO:0007623; P:circadian rhythm; TAS:Reactome.
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 from RNA polymerase II promoter; 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:2000188; P:regulation of cholesterol homeostasis; IMP: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:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
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;
Complete proteome; 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 Nuclear receptor ROR-alpha.
/FTId=PRO_0000053513.
DOMAIN 272 510 NR LBD. {ECO:0000255|PROSITE-
ProRule:PRU01189}.
DNA_BIND 73 138 Nuclear receptor. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 73 93 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 109 133 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
REGION 139 271 Hinge.
MOTIF 506 511 AF-2.
COMPBIAS 101 175 Gln-rich.
MOD_RES 38 38 N6-methyllysine.
{ECO:0000250|UniProtKB:P35398}.
MOD_RES 183 183 Phosphothreonine; by MAPK1.
{ECO:0000250|UniProtKB:P35398}.
CROSSLNK 240 240 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
VAR_SEQ 1 66 MESAPAAPDPAASEPGSSGSEAAAGSRETPLTQDTGRKSEA
PGAGRRQSYASSSRGISVTKKTHTS -> MYFVIAAMKA
(in isoform 4).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7935491,
ECO:0000303|PubMed:8750880,
ECO:0000303|PubMed:9226375}.
/FTId=VSP_003658.
VARIANT 275 314 Missing (in SG; disturbance of Purkinje
cell and muscle development, lipid
metabolism, circadian behavior and immune
system functioning).
{ECO:0000269|PubMed:9226375}.
CONFLICT 163 163 H -> R (in Ref. 2; CAA69930).
{ECO:0000305}.
CONFLICT 180 181 EP -> T (in Ref. 2; CAA69930).
{ECO:0000305}.
CONFLICT 182 182 L -> I (in Ref. 4; AAB46801/BAA22970).
{ECO:0000305}.
CONFLICT 193 194 LT -> SA (in Ref. 2; CAA69930).
{ECO:0000305}.
CONFLICT 304 304 L -> W (in Ref. 2; CAA69930).
{ECO:0000305}.
CONFLICT 315 315 Missing (in Ref. 4; AAB46801/BAA22970).
{ECO:0000305}.
CONFLICT 362 362 E -> G (in Ref. 2; CAA69930).
{ECO:0000305}.
CONFLICT 433 433 R -> P (in Ref. 2; CAA69930).
{ECO:0000305}.
CONFLICT 450 451 QL -> HM (in Ref. 2; CAA69930).
{ECO:0000305}.
CONFLICT 487 487 K -> N (in Ref. 4; AAB46801/BAA22970).
{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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