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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_HUMAN              Reviewed;         523 AA.
P35398; P35397; P35399; P45445; Q495X4; Q96H83;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 2.
25-OCT-2017, entry version 184.
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;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION AS
TRANSCRIPTION ACTIVATOR, DNA-BINDING, AND SUBUNIT.
TISSUE=Retina, and Testis;
PubMed=7926749; DOI=10.1101/gad.8.5.538;
Giguere V., Tini M., Flock G., Ong E., Evans R.M., Otulakowski G.;
"Isoform-specific amino-terminal domains dictate DNA-binding
properties of ROR alpha, a novel family of orphan hormone nuclear
receptors.";
Genes Dev. 8:538-553(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND TISSUE SPECIFICITY.
TISSUE=Umbilical vein endothelial cell;
PubMed=7916608; DOI=10.1006/bbrc.1993.1976;
Becker-Andre M., Andre E., Delamarter J.F.;
"Identification of nuclear receptor mRNAs by RT-PCR amplification of
conserved zinc-finger motif sequences.";
Biochem. Biophys. Res. Commun. 194:1371-1379(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
TISSUE=Kidney;
Kaighin V.A., Martin A.L., Aronstam R.S.;
"Isolation of cDNA coding for multiple human nuclear receptor
clones.";
Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
TISSUE=Muscle;
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).
[7]
FUNCTION AS TRANSCRIPTION ACTIVATOR, INTERACTION WITH NCOR1,
DNA-BINDING, AND SUBUNIT.
PubMed=9328355; DOI=10.1210/mend.11.11.0002;
Harding H.P., Atkins G.B., Jaffe A.B., Seo W.J., Lazar M.A.;
"Transcriptional activation and repression by RORalpha, an orphan
nuclear receptor required for cerebellar development.";
Mol. Endocrinol. 11:1737-1746(1997).
[8]
FUNCTION AS TRANSCRIPTION ACTIVATOR, INTERACTION WITH MED1 AND NCOA2,
AND MUTAGENESIS OF VAL-335 AND 510-LEU-PHE-511.
PubMed=10478845; DOI=10.1210/mend.13.9.0343;
Atkins G.B., Hu X., Guenther M.G., Rachez C., Freedman L.P.,
Lazar M.A.;
"Coactivators for the orphan nuclear receptor RORalpha.";
Mol. Endocrinol. 13:1550-1557(1999).
[9]
FUNCTION IN MYOGENESIS, AND INTERACTION WITH EP300.
PubMed=9862959; DOI=10.1093/nar/27.2.411;
Lau P., Bailey P., Dowhan D.H., Muscat G.E.;
"Exogenous expression of a dominant negative RORalpha1 vector in
muscle cells impairs differentiation: RORalpha1 directly interacts
with p300 and myoD.";
Nucleic Acids Res. 27:411-420(1999).
[10]
FUNCTION AS TRANSCRIPTION ACTIVATOR, AND DNA-BINDING.
PubMed=11554739; DOI=10.1006/bbrc.2001.5602;
Sundvold H., Lien S.;
"Identification of a novel peroxisome proliferator-activated receptor
(PPAR) gamma promoter in man and transactivation by the nuclear
receptor RORalpha1.";
Biochem. Biophys. Res. Commun. 287:383-390(2001).
[11]
FUNCTION IN INFLAMMATION.
PubMed=11252722; DOI=10.1093/embo-reports/kve007;
Delerive P., Monte D., Dubois G., Trottein F., Fruchart-Najib J.,
Mariani J., Fruchart J.C., Staels B.;
"The orphan nuclear receptor ROR alpha is a negative regulator of the
inflammatory response.";
EMBO Rep. 2:42-48(2001).
[12]
FUNCTION IN TRIGLYCERIDE METABOLISM, AND DNA-BINDING.
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).
[13]
FUNCTION AS TRANSCRIPTION ACTIVATOR, UBIQUITINATION, AND MUTAGENESIS
OF LYS-357; LEU-361; VAL-364 AND GLU-509.
PubMed=14570920; DOI=10.1074/jbc.M308152200;
Moraitis A.N., Giguere V.;
"The co-repressor hairless protects RORalpha orphan nuclear receptor
from proteasome-mediated degradation.";
J. Biol. Chem. 278:52511-52518(2003).
[14]
INDUCTION BY HYPOXIA (ISOFORM 4).
PubMed=14742449; DOI=10.1074/jbc.M313186200;
Miki N., Ikuta M., Matsui T.;
"Hypoxia-induced activation of the retinoic acid receptor-related
orphan receptor alpha4 gene by an interaction between hypoxia-
inducible factor-1 and Sp1.";
J. Biol. Chem. 279:15025-15031(2004).
[15]
FUNCTION IN TRIGLYCERIDE METABOLISM, AND DNA-BINDING.
PubMed=15790933; DOI=10.1161/01.ATV.0000163841.85333.83;
Genoux A., Dehondt H., Helleboid-Chapman A., Duhem C., Hum D.W.,
Martin G., Pennacchio L.A., Staels B., Fruchart-Najib J.,
Fruchart J.C.;
"Transcriptional regulation of apolipoprotein A5 gene expression by
the nuclear receptor RORalpha.";
Arterioscler. Thromb. Vasc. Biol. 25:1186-1192(2005).
[16]
FUNCTION IN TRIGLYCERIDE METABOLISM, AND DNA-BINDING.
PubMed=15781255; DOI=10.1016/j.bbrc.2005.02.151;
Lind U., Nilsson T., McPheat J., Stroemstedt P.E., Bamberg K.,
Balendran C., Kang D.;
"Identification of the human ApoAV gene as a novel RORalpha target
gene.";
Biochem. Biophys. Res. Commun. 330:233-241(2005).
[17]
FUNCTION IN CELL GROWTH, AND INDUCTION BY CELLULAR STRESS.
PubMed=16462772; DOI=10.1038/sj.onc.1209314;
Zhu Y., McAvoy S., Kuhn R., Smith D.I.;
"RORA, a large common fragile site gene, is involved in cellular
stress response.";
Oncogene 25:2901-2908(2006).
[18]
PHOSPHORYLATION AT THR-183, FUNCTION, AND MUTAGENESIS OF THR-183.
PubMed=17512500; DOI=10.1016/j.bbrc.2007.05.016;
Lechtken A., Hoernig M., Werz O., Corvey N., Zoendorf I.,
Dingermann T., Brandes R., Steinhilber D.;
"Extracellular signal-regulated kinase-2 phosphorylates RORalpha4 in
vitro.";
Biochem. Biophys. Res. Commun. 358:890-896(2007).
[19]
FUNCTION IN HYPOXIA SIGNALING, INTERACTION WITH HIF1A, INDUCTION BY
HYPOXIA, AND SUBCELLULAR LOCATION.
PubMed=18658046; DOI=10.1161/ATVBAHA.108.171546;
Kim E.J., Yoo Y.G., Yang W.K., Lim Y.S., Na T.Y., Lee I.K., Lee M.O.;
"Transcriptional activation of HIF-1 by RORalpha and its role in
hypoxia signaling.";
Arterioscler. Thromb. Vasc. Biol. 28:1796-1802(2008).
[20]
FUNCTION, INTERACTION WITH FOXP3, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND MUTAGENESIS OF 510-LEU-PHE-511.
PubMed=18354202; DOI=10.4049/jimmunol.180.7.4785;
Du J., Huang C., Zhou B., Ziegler S.F.;
"Isoform-specific inhibition of ROR alpha-mediated transcriptional
activation by human FOXP3.";
J. Immunol. 180:4785-4792(2008).
[21]
FUNCTION AS TRANSCRIPTION ACTIVATOR, PHOSPHORYLATION, AND SUBCELLULAR
LOCATION.
PubMed=18005000; DOI=10.1111/j.1471-4159.2007.05074.x;
Duplus E., Gras C., Soubeyre V., Vodjdani G., Lemaigre-Dubreuil Y.,
Brugg B.;
"Phosphorylation and transcriptional activity regulation of retinoid-
related orphan receptor alpha 1 by protein kinases C.";
J. Neurochem. 104:1321-1332(2008).
[22]
SUMOYLATION AT LYS-240, AND MUTAGENESIS OF LYS-240 AND LYS-441.
PubMed=19041634; DOI=10.1016/j.bbrc.2008.11.072;
Hwang E.J., Lee J.M., Jeong J., Park J.H., Yang Y., Lim J.S.,
Kim J.H., Baek S.H., Kim K.I.;
"SUMOylation of RORalpha potentiates transcriptional activation
function.";
Biochem. Biophys. Res. Commun. 378:513-517(2009).
[23]
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).
[24]
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).
[25]
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).
[26]
FUNCTION IN T(H)17 CELLS DIFFERENTIATION, 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).
[27]
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).
[28]
METHYLATION AT LYS-38.
PubMed=23063525; DOI=10.1016/j.molcel.2012.09.004;
Lee J.M., Lee J.S., Kim H., Kim K., Park H., Kim J.Y., Lee S.H.,
Kim I.S., Kim J., Lee M., Chung C.H., Seo S.B., Yoon J.B., Ko E.,
Noh D.Y., Kim K.I., Kim K.K., Baek S.H.;
"EZH2 generates a methyl degron that is recognized by the
DCAF1/DDB1/CUL4 E3 ubiquitin ligase complex.";
Mol. Cell 48:572-586(2012).
[29]
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).
[30]
VARIANT [LARGE SCALE ANALYSIS] SER-18 (ISOFORM 2).
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[31]
X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 271-523 IN COMPLEX WITH
CHOLESTEROL, FUNCTION AS TRANSCRIPTION ACTIVATOR, IDENTIFICATION OF
LIGANDS, MUTAGENESIS OF CYS-323; ALA-330; ALA-371; PHE-399; HIS-484
AND TYR-507, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=12467577; DOI=10.1016/S0969-2126(02)00912-7;
Kallen J.A., Schlaeppi J.-M., Bitsch F., Geisse S., Geiser M.,
Delhon I., Fournier B.;
"X-ray structure of the hRORalpha LBD at 1.63 A: structural and
functional data that cholesterol or a cholesterol derivative is the
natural ligand of RORalpha.";
Structure 10:1697-1707(2002).
[32]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 271-523 IN COMPLEX WITH
CHOLESTEROL SULFATE, MUTAGENESIS OF CYS-288; CYS-323; ALA-330; LYS-339
AND GLU-509, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=14722075; DOI=10.1074/jbc.M400302200;
Kallen J., Schlaeppi J.-M., Bitsch F., Delhon I., Fournier B.;
"Crystal structure of the human RORalpha Ligand binding domain in
complex with cholesterol sulfate at 2.2 A.";
J. Biol. Chem. 279:14033-14038(2004).
-!- 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:10478845,
ECO:0000269|PubMed:11053433, ECO:0000269|PubMed:11252722,
ECO:0000269|PubMed:11554739, ECO:0000269|PubMed:12467577,
ECO:0000269|PubMed:14570920, ECO:0000269|PubMed:15781255,
ECO:0000269|PubMed:15790933, ECO:0000269|PubMed:16462772,
ECO:0000269|PubMed:17512500, ECO:0000269|PubMed:18005000,
ECO:0000269|PubMed:18354202, ECO:0000269|PubMed:18658046,
ECO:0000269|PubMed:19965867, ECO:0000269|PubMed:21499262,
ECO:0000269|PubMed:7926749, ECO:0000269|PubMed:9328355,
ECO:0000269|PubMed:9862959}.
-!- 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 (By similarity). Interacts with NRIP1. Isoform 4
interacts (via AF-2 motif) with isoform 1 of FOXP3 (via LXXLL
motif). {ECO:0000250|UniProtKB:P51448,
ECO:0000269|PubMed:10478845, ECO:0000269|PubMed:12467577,
ECO:0000269|PubMed:14722075, ECO:0000269|PubMed:18354202,
ECO:0000269|PubMed:18658046, ECO:0000269|PubMed:21628546,
ECO:0000269|PubMed:22170608, ECO:0000269|PubMed:7926749,
ECO:0000269|PubMed:9328355, ECO:0000269|PubMed:9862959}.
-!- INTERACTION:
Q9BZS1:FOXP3; NbExp=5; IntAct=EBI-11295807, EBI-983719;
P14136:GFAP; NbExp=3; IntAct=EBI-748689, EBI-744302;
P51843:NR0B1; NbExp=2; IntAct=EBI-748689, EBI-946109;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00407, ECO:0000269|PubMed:18005000,
ECO:0000269|PubMed:18354202, ECO:0000269|PubMed:18658046}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=4;
Name=1; Synonyms=Alpha-1;
IsoId=P35398-2; Sequence=Displayed;
Name=2; Synonyms=Alpha-2;
IsoId=P35398-1; Sequence=VSP_053973;
Note=Produced by alternative promoter usage. Region from 23 to
71 inhibits DNA-binding and transactivation activity. Variant in
position: 18:P->S (in a colorectal cancer sample, somatic
mutation).;
Name=3; Synonyms=Alpha-3;
IsoId=P35398-3; Sequence=VSP_053975;
Note=Produced by alternative splicing.;
Name=4; Synonyms=Alpha-4;
IsoId=P35398-4; Sequence=VSP_053974;
Note=Produced by alternative promoter usage. Ref.2 (AAA02963)
sequence is in conflict in position: 7:A->E. {ECO:0000305};
-!- TISSUE SPECIFICITY: Widely expressed in a number of tissues.
Expressed in both regulatory T-cells (Treg) and effector T-cells
(Teff). {ECO:0000269|PubMed:18354202, ECO:0000269|PubMed:7916608}.
-!- INDUCTION: Induced by oxidative stress and DNA damage. Isoform 4
is induced by hypoxia (through transactivation by HIF1A and SP1),
but not isoform 1. {ECO:0000269|PubMed:16462772,
ECO:0000269|PubMed:18658046}.
-!- DOMAIN: The AF-2 (activation function-2) motif is required for
recruiting coregulators containing LXXLL motifs. {ECO:0000250}.
-!- PTM: Phosphorylation by conventional PKCs in neurons inhibits
transcriptional activity. Phosphorylated on Thr-183 by MAPK1/ERK1
in vitro. {ECO:0000269|PubMed:17512500,
ECO:0000269|PubMed:18005000}.
-!- PTM: Sumoylated by SENP1 and SENP2. Sumoylation, promoted by
PIAS2, PIAS3, PIAS4 but not PIAS1, enhances the transcriptional
activity. Desumoylated by SENP1. {ECO:0000269|PubMed:19041634}.
-!- PTM: Ubiquitinated, leading to its degradation by the proteasome.
Proteasomal degradation is required for efficient transcriptional
activity and is prevented by HR. {ECO:0000269|PubMed:14570920}.
-!- 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:0000269|PubMed:14570920}.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
subfamily. {ECO:0000305}.
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EMBL; U04897; AAA62658.1; -; mRNA.
EMBL; U04898; AAA62659.1; -; mRNA.
EMBL; U04899; AAA62660.1; -; mRNA.
EMBL; L14611; AAA02963.1; -; mRNA.
EMBL; HQ692818; ADZ17329.1; -; mRNA.
EMBL; AC009560; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC012404; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC022898; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC079068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC087385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC107241; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC107905; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471082; EAW77594.1; -; Genomic_DNA.
EMBL; BC008831; AAH08831.1; -; mRNA.
EMBL; BC100987; AAI00988.1; -; mRNA.
EMBL; BC100988; AAI00989.1; -; mRNA.
EMBL; BC100989; AAI00990.1; -; mRNA.
EMBL; BC100990; AAI00991.1; -; mRNA.
CCDS; CCDS10177.1; -. [P35398-2]
CCDS; CCDS10179.1; -. [P35398-1]
CCDS; CCDS45271.1; -. [P35398-4]
PIR; A53196; A53196.
PIR; A56856; A56856.
PIR; B53196; B53196.
PIR; C53196; C53196.
RefSeq; NP_002934.1; NM_002943.3.
RefSeq; NP_599022.1; NM_134260.2. [P35398-1]
RefSeq; NP_599023.1; NM_134261.2. [P35398-2]
RefSeq; NP_599024.1; NM_134262.2.
UniGene; Hs.560343; -.
PDB; 1N83; X-ray; 1.63 A; A=271-523.
PDB; 1S0X; X-ray; 2.20 A; A=271-523.
PDB; 4S15; X-ray; 1.90 A; A/B=269-523.
PDBsum; 1N83; -.
PDBsum; 1S0X; -.
PDBsum; 4S15; -.
ProteinModelPortal; P35398; -.
SMR; P35398; -.
BioGrid; 112022; 24.
DIP; DIP-29938N; -.
IntAct; P35398; 9.
MINT; MINT-2855668; -.
STRING; 9606.ENSP00000261523; -.
BindingDB; P35398; -.
ChEMBL; CHEMBL5868; -.
DrugBank; DB04540; Cholesterol.
DrugBank; DB01990; Cholesterol-Sulfate.
GuidetoPHARMACOLOGY; 598; -.
iPTMnet; P35398; -.
PhosphoSitePlus; P35398; -.
BioMuta; RORA; -.
DMDM; 548814; -.
PaxDb; P35398; -.
PeptideAtlas; P35398; -.
PRIDE; P35398; -.
Ensembl; ENST00000261523; ENSP00000261523; ENSG00000069667. [P35398-1]
Ensembl; ENST00000335670; ENSP00000335087; ENSG00000069667. [P35398-2]
GeneID; 6095; -.
KEGG; hsa:6095; -.
UCSC; uc002agt.5; human. [P35398-2]
CTD; 6095; -.
DisGeNET; 6095; -.
EuPathDB; HostDB:ENSG00000069667.15; -.
GeneCards; RORA; -.
HGNC; HGNC:10258; RORA.
HPA; CAB009861; -.
MIM; 600825; gene.
neXtProt; NX_P35398; -.
OpenTargets; ENSG00000069667; -.
PharmGKB; PA34630; -.
eggNOG; KOG4216; Eukaryota.
eggNOG; ENOG410XUGR; LUCA.
GeneTree; ENSGT00870000136388; -.
HOGENOM; HOG000010200; -.
HOVERGEN; HBG106848; -.
InParanoid; P35398; -.
KO; K08532; -.
OMA; YQNKPRE; -.
OrthoDB; EOG091G0649; -.
TreeFam; TF319910; -.
Reactome; R-HSA-1368082; RORA activates gene expression.
Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
Reactome; R-HSA-400253; Circadian Clock.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
SignaLink; P35398; -.
SIGNOR; P35398; -.
ChiTaRS; RORA; human.
EvolutionaryTrace; P35398; -.
GeneWiki; RAR-related_orphan_receptor_alpha; -.
GenomeRNAi; 6095; -.
PRO; PR:P35398; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000069667; -.
CleanEx; HS_RORA; -.
ExpressionAtlas; P35398; baseline and differential.
Genevisible; P35398; HS.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0008013; F:beta-catenin binding; IEA:Ensembl.
GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0008142; F:oxysterol binding; IDA:UniProtKB.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:MGI.
GO; GO:0004879; F:RNA polymerase II transcription factor activity, ligand-activated sequence-specific DNA binding; IEA:InterPro.
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; IPI:UniProtKB.
GO; GO:0098531; F:transcription factor activity, direct ligand regulated sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; IC:NTNU_SB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0001525; P:angiogenesis; IMP:UniProtKB.
GO; GO:0071456; P:cellular response to hypoxia; IMP:UniProtKB.
GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
GO; GO:0036315; P:cellular response to sterol; IDA:UniProtKB.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
GO; GO:0021930; P:cerebellar granule cell precursor proliferation; ISS:UniProtKB.
GO; GO:0021702; P:cerebellar Purkinje cell differentiation; IEA:Ensembl.
GO; GO:0046068; P:cGMP metabolic process; IEA:Ensembl.
GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
GO; GO:0030522; P:intracellular receptor signaling pathway; IDA:UniProtKB.
GO; GO:0042692; P:muscle cell differentiation; IMP:UniProtKB.
GO; GO:0045599; P:negative regulation of fat cell differentiation; ISS:UniProtKB.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0050728; P:negative regulation of inflammatory response; IMP:UniProtKB.
GO; GO:0006809; P:nitric oxide biosynthetic process; IEA:Ensembl.
GO; GO:0042753; P:positive regulation of circadian rhythm; ISS: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; IMP:UniProtKB.
GO; GO:2000188; P:regulation of cholesterol homeostasis; ISS:UniProtKB.
GO; GO:0010906; P:regulation of glucose metabolic process; ISS:UniProtKB.
GO; GO:0043030; P:regulation of macrophage activation; IEA:Ensembl.
GO; GO:0008589; P:regulation of smoothened signaling pathway; ISS:UniProtKB.
GO; GO:0019218; P:regulation of steroid metabolic process; ISS:UniProtKB.
GO; GO:0060850; P:regulation of transcription involved in cell fate commitment; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0072539; P:T-helper 17 cell differentiation; ISS:UniProtKB.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0070328; P:triglyceride homeostasis; IMP:UniProtKB.
GO; GO:0006805; P:xenobiotic metabolic process; ISS:UniProtKB.
Gene3D; 1.10.565.10; -; 1.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR035500; NHR_like_domain.
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; PS00031; NUCLEAR_REC_DBD_1; 1.
PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative promoter usage;
Alternative splicing; Biological rhythms; Complete proteome;
DNA-binding; Isopeptide bond; Metal-binding; Methylation; Nucleus;
Phosphoprotein; Polymorphism; Receptor; Reference proteome;
Transcription; Transcription regulation; Ubl conjugation; Zinc;
Zinc-finger.
CHAIN 1 523 Nuclear receptor ROR-alpha.
/FTId=PRO_0000053512.
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.
REGION 272 523 Ligand-binding.
MOTIF 506 523 AF-2.
COMPBIAS 166 169 Poly-Gln.
MOD_RES 38 38 N6-methyllysine.
{ECO:0000269|PubMed:23063525}.
MOD_RES 183 183 Phosphothreonine; by MAPK1.
{ECO:0000269|PubMed:17512500}.
CROSSLNK 240 240 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:19041634}.
VAR_SEQ 1 66 MESAPAAPDPAASEPGSSGADAAAGSRETPLNQESARKSEP
PAPVRRQSYSSTSRGISVTKKTHTS -> MNEGAPGDSDLE
TEARVPWSIMGHCLRTGQARMSATPTPAGEGARRDELFGIL
QILHQCILSSGDAFVLTGVCCSWRQNGKPPYSQKEDKEVQT
GYMNA (in isoform 2).
{ECO:0000303|PubMed:7926749}.
/FTId=VSP_053973.
VAR_SEQ 1 65 MESAPAAPDPAASEPGSSGADAAAGSRETPLNQESARKSEP
PAPVRRQSYSSTSRGISVTKKTHT -> MMYFVIAAMK
(in isoform 4).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7916608,
ECO:0000303|Ref.3}.
/FTId=VSP_053974.
VAR_SEQ 38 65 KSEPPAPVRRQSYSSTSRGISVTKKTHT -> SSSTCSSLS
RLFWSQLEHINWDGATAKNFINLREFFSFLLPALRK (in
isoform 3). {ECO:0000303|PubMed:7926749}.
/FTId=VSP_053975.
MUTAGEN 183 183 T->A: Greatly increased transcriptional
activity. Decrease in repression by
NR1D1. {ECO:0000269|PubMed:17512500}.
MUTAGEN 183 183 T->D,E: Some increase in transcriptional
activity. No change in repression by
NR1D1. {ECO:0000269|PubMed:17512500}.
MUTAGEN 183 183 T->R: Attenuates transcriptional
activity. {ECO:0000269|PubMed:17512500}.
MUTAGEN 183 183 T->V,I: Some increase in transcriptional
activity. {ECO:0000269|PubMed:17512500}.
MUTAGEN 240 240 K->R: Loss of sumoylation.
{ECO:0000269|PubMed:19041634}.
MUTAGEN 288 288 C->Q: Less effect on transcriptional
activity with cholesterol sulfate as
substrate as compared to cholesterol as
substrate. {ECO:0000269|PubMed:14722075}.
MUTAGEN 323 323 C->L: About 60% loss of transcriptional
activity. {ECO:0000269|PubMed:12467577,
ECO:0000269|PubMed:14722075}.
MUTAGEN 330 330 A->L: About 80% loss of transcriptional
activity. {ECO:0000269|PubMed:12467577,
ECO:0000269|PubMed:14722075}.
MUTAGEN 335 335 V->R: Strongly decreases interaction with
NCOA2 and MED1.
{ECO:0000269|PubMed:10478845}.
MUTAGEN 339 339 K->A: Complete loss of transcriptional
activity; when associated with A-507.
{ECO:0000269|PubMed:14722075}.
MUTAGEN 357 357 K->A: Increased transcriptional activity.
No effect on protein degradation.
{ECO:0000269|PubMed:14570920}.
MUTAGEN 361 361 L->F: Small reduction in transcriptional
activity. No protein degradation.
{ECO:0000269|PubMed:14570920}.
MUTAGEN 364 364 V->G: Greatly reduced transcriptional
activity. Protects from protein
degradation.
{ECO:0000269|PubMed:14570920}.
MUTAGEN 371 371 A->Q: Almost total loss of
transcriptional activity.
{ECO:0000269|PubMed:12467577}.
MUTAGEN 399 399 F->W: Slight loss of transcriptional
activity. {ECO:0000269|PubMed:12467577}.
MUTAGEN 441 441 K->R: No effect on sumoylation.
{ECO:0000269|PubMed:19041634}.
MUTAGEN 484 484 H->W: Almost total loss of
transcriptional activity.
{ECO:0000269|PubMed:12467577}.
MUTAGEN 507 507 Y->A: Complete loss of transcriptional
activity; when associated with A-339.
{ECO:0000269|PubMed:12467577}.
MUTAGEN 507 507 Y->F: About 40% loss of transcriptional
activity. {ECO:0000269|PubMed:12467577}.
MUTAGEN 509 509 E->K: Abolishes transcriptional activity.
Protects from protein degradation.
{ECO:0000269|PubMed:14570920,
ECO:0000269|PubMed:14722075}.
MUTAGEN 510 511 LF->AA: Decreases interaction with NCOA2.
Loss of interaction with FOXP3.
{ECO:0000269|PubMed:10478845,
ECO:0000269|PubMed:18354202}.
CONFLICT 368 368 M -> V (in Ref. 2; AAA02963).
{ECO:0000305}.
CONFLICT 466 466 I -> M (in Ref. 2; AAA02963).
{ECO:0000305}.
HELIX 271 286 {ECO:0000244|PDB:1N83}.
HELIX 292 297 {ECO:0000244|PDB:1N83}.
TURN 298 300 {ECO:0000244|PDB:1N83}.
HELIX 305 313 {ECO:0000244|PDB:1N83}.
HELIX 316 340 {ECO:0000244|PDB:1N83}.
TURN 342 346 {ECO:0000244|PDB:1N83}.
HELIX 349 367 {ECO:0000244|PDB:1N83}.
HELIX 368 371 {ECO:0000244|PDB:1N83}.
TURN 374 377 {ECO:0000244|PDB:1N83}.
STRAND 378 381 {ECO:0000244|PDB:1N83}.
STRAND 384 386 {ECO:0000244|PDB:1N83}.
HELIX 388 394 {ECO:0000244|PDB:1N83}.
HELIX 397 411 {ECO:0000244|PDB:1N83}.
TURN 412 414 {ECO:0000244|PDB:4S15}.
HELIX 417 428 {ECO:0000244|PDB:1N83}.
HELIX 439 460 {ECO:0000244|PDB:1N83}.
HELIX 466 494 {ECO:0000244|PDB:1N83}.
HELIX 496 502 {ECO:0000244|PDB:1N83}.
HELIX 505 510 {ECO:0000244|PDB:1N83}.
SEQUENCE 523 AA; 58975 MW; 0FA43BBCE6E28DC7 CRC64;
MESAPAAPDP AASEPGSSGA DAAAGSRETP LNQESARKSE PPAPVRRQSY SSTSRGISVT
KKTHTSQIEI IPCKICGDKS SGIHYGVITC EGCKGFFRRS QQSNATYSCP RQKNCLIDRT
SRNRCQHCRL QKCLAVGMSR DAVKFGRMSK KQRDSLYAEV QKHRMQQQQR DHQQQPGEAE
PLTPTYNISA NGLTELHDDL SNYIDGHTPE 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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