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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)

 RORG_MOUSE              Reviewed;         516 AA.
P51450; E9Q8I1; Q3U513; Q61027; Q91YT5; Q9QXD9; Q9R177;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
11-DEC-2019, entry version 180.
RecName: Full=Nuclear receptor ROR-gamma;
AltName: Full=Nuclear receptor RZR-gamma;
AltName: Full=Nuclear receptor subfamily 1 group F member 3;
AltName: Full=RAR-related orphan receptor C;
AltName: Full=Retinoid-related orphan receptor-gamma;
AltName: Full=Thymus orphan receptor;
Short=TOR;
Name=Rorc; Synonyms=Nr1f3, Rorg, Thor;
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 [GENOMIC DNA / MRNA] (ISOFORM 1).
PubMed=8973331; DOI=10.1016/s0378-1119(96)00504-5;
Medvedev A., Yan Z.H., Hirose T., Giguere V., Jetten A.M.;
"Cloning of a cDNA encoding the murine orphan receptor RZR/ROR gamma and
characterization of its response element.";
Gene 181:199-206(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
STRAIN=129;
PubMed=9403063; DOI=10.1006/geno.1997.4980;
Medvedev A., Chistokhina A., Hirose A., Jetten A.M.;
"Genomic structure and chromosomal mapping of the nuclear orphan receptor
ROR gamma (RORC) gene.";
Genomics 46:93-102(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=CD-1; TISSUE=Thymus;
PubMed=8614404; DOI=10.1210/mend.9.12.8614404;
Ortiz M.A., Piedrafita F.J., Pfahl M., Maki R.;
"TOR: a new orphan receptor expressed in the thymus that can modulate
retinoid and thyroid hormone signals.";
Mol. Endocrinol. 9:1679-1691(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION IN T-CELLS (ISOFORM 2),
AND TISSUE SPECIFICITY.
TISSUE=Thymus;
PubMed=9881970; DOI=10.1016/s1074-7613(00)80645-7;
He Y.-W., Deftos M.L., Ojala E.W., Bevan M.J.;
"RORgamma t, a novel isoform of an orphan receptor, negatively regulates
Fas ligand expression and IL-2 production in T cells.";
Immunity 9:797-806(1998).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION IN PRE-TCR ACTIVATION
(ISOFORM 2), AND TISSUE SPECIFICITY.
TISSUE=Thymus;
PubMed=10602018;
DOI=10.1002/(sici)1521-4141(199912)29:12<4072::aid-immu4072>3.0.co;2-e;
Villey I., De Chasseval R., De Villartay J.-P.;
"RORgammaT, a thymus-specific isoform of the orphan nuclear receptor
RORg/TOR, is up-regulated by signaling through the pre-T cell receptor
(TCR) and binds to the TEA promoter.";
Eur. J. Immunol. 29:4072-4080(1999).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
STRAIN=NOD {ECO:0000312|EMBL:BAE32267.1};
TISSUE=Thymus {ECO:0000312|EMBL:BAE32267.1};
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of the
mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[9]
FUNCTION IN THYMOPOIESIS (ISOFORM 2), DISRUPTION PHENOTYPE (ISOFORM 2),
DEVELOPMENTAL STAGE (ISOFORM 2), AND TISSUE SPECIFICITY (ISOFORM 2).
PubMed=14691482; DOI=10.1038/ni1022;
Eberl G., Marmon S., Sunshine M.J., Rennert P.D., Choi Y., Littman D.R.;
"An essential function for the nuclear receptor RORgamma(t) in the
generation of fetal lymphoid tissue inducer cells.";
Nat. Immunol. 5:64-73(2004).
[10]
FUNCTION IN THYMOCYTE SURVIVAL (ISOFORM 2), INTERACTION WITH NCOA1 AND
NCOA2, DISRUPTION PHENOTYPE, DNA-BINDING, MUTAGENESIS OF 56-ARG-ARG-57 AND
TYR-500, AND DOMAIN.
PubMed=16148126; DOI=10.4049/jimmunol.175.6.3800;
Xie H., Sadim M.S., Sun Z.;
"RORgammat recruits steroid receptor coactivators to ensure thymocyte
survival.";
J. Immunol. 175:3800-3809(2005).
[11]
FUNCTION IN T(H)17 CELLS DIFFERENTIATION (ISOFORM 2), DISRUPTION PHENOTYPE
(ISOFORM 2), INDUCTION BY IL6 AND TGFB1 (ISOFORM 2), AND TISSUE SPECIFICITY
(ISOFORM 2).
PubMed=16990136; DOI=10.1016/j.cell.2006.07.035;
Ivanov I.I., McKenzie B.S., Zhou L., Tadokoro C.E., Lepelley A.,
Lafaille J.J., Cua D.J., Littman D.R.;
"The orphan nuclear receptor RORgammat directs the differentiation program
of proinflammatory IL-17+ T helper cells.";
Cell 126:1121-1133(2006).
[12]
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).
[13]
FUNCTION IN METABOLISM REGULATION, DEVELOPMENTAL STAGE, DISRUPTION
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).
[14]
FUNCTION IN T(H)17 CELLS DIFFERENTIATION (ISOFORM 2), INDUCTION BY IL6 AND
TGB1 (ISOFORM 2), AND TISSUE SPECIFICITY (ISOFORM 2).
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]
SUBCELLULAR LOCATION, INTERACTION WITH FOXP3, AND INDUCTION.
PubMed=18368049; DOI=10.1038/nature06878;
Zhou L., Lopes J.E., Chong M.M., Ivanov I.I., Min R., Victora G.D.,
Shen Y., Du J., Rubtsov Y.P., Rudensky A.Y., Ziegler S.F., Littman D.R.;
"TGF-beta-induced Foxp3 inhibits T(H)17 cell differentiation by
antagonizing RORgammat function.";
Nature 453:236-240(2008).
[16]
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).
[17]
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).
[18]
FUNCTION IN ADIPOGENESIS, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION,
DEVELOPMENTAL STAGE, AND MUTAGENESIS OF CYS-31 AND CYS-48.
PubMed=21853531; DOI=10.1002/emmm.201100172;
Meissburger B., Ukropec J., Roeder E., Beaton N., Geiger M., Teupser D.,
Civan B., Langhans W., Nawroth P.P., Gasperikova D., Rudofsky G.,
Wolfrum C.;
"Adipogenesis and insulin sensitivity in obesity are regulated by retinoid-
related orphan receptor gamma.";
EMBO Mol. Med. 3:637-651(2011).
[19]
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).
[20]
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).
[21]
FUNCTION IN CIRCADIAN RHYTHMS, TISSUE SPECIFICITY, INDUCTION, SUBCELLULAR
LOCATION, DNA-BINDING, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-502.
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).
[22]
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).
[23]
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).
[24]
FUNCTION (ISOFORM 2).
PubMed=26607793; DOI=10.1016/j.cell.2015.10.068;
Wang C., Yosef N., Gaublomme J., Wu C., Lee Y., Clish C.B., Kaminski J.,
Xiao S., Meyer Zu Horste G., Pawlak M., Kishi Y., Joller N., Karwacz K.,
Zhu C., Ordovas-Montanes M., Madi A., Wortman I., Miyazaki T., Sobel R.A.,
Park H., Regev A., Kuchroo V.K.;
"CD5L/AIM regulates lipid biosynthesis and restrains Th17 cell
pathogenicity.";
Cell 163:1413-1427(2015).
[25]
INTERACTION WITH NR0B2.
PubMed=25212631; DOI=10.1002/hep.27437;
Lee S.M., Zhang Y., Tsuchiya H., Smalling R., Jetten A.M., Wang L.;
"Small heterodimer partner/neuronal PAS domain protein 2 axis regulates the
oscillation of liver lipid metabolism.";
Hepatology 61:497-505(2015).
-!- 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 cellular
differentiation, immunity, peripheral 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 gene regulatory regions to modulate their
transcriptional expression, depending on the tissue, time and promoter
contexts (PubMed:17666523, PubMed:19381306, PubMed:19965867,
PubMed:21853531, PubMed:22789990, PubMed:23723244). Regulates the
circadian expression of clock genes such as CRY1, ARNTL/BMAL1 and NR1D1
in peripheral tissues and in a tissue-selective manner
(PubMed:22753030). 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 RORC-mediated
activation of the expression, leading to the circadian pattern of clock
genes expression. Therefore influences the period length and stability
of the clock (PubMed:22753030). Involved in the regulation of the
rhythmic expression of genes involved in glucose and lipid metabolism,
including PLIN2 and AVPR1A. Negative regulator of adipocyte
differentiation through the regulation of early phase genes expression,
such as MMP3. Controls adipogenesis as well as adipocyte size and
modulates insulin sensitivity in obesity. In liver, has specific and
redundant functions with RORA 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 SULT1E1
(PubMed:21853531). Also plays also a role in the regulation of
hepatocyte glucose metabolism through the regulation of G6PC and PCK1.
Regulates the rhythmic expression of PROX1 and promotes its nuclear
localization. {ECO:0000269|PubMed:17666523,
ECO:0000269|PubMed:19381306, ECO:0000269|PubMed:19965867,
ECO:0000269|PubMed:21853531, ECO:0000269|PubMed:22753030,
ECO:0000269|PubMed:22789990, ECO:0000269|PubMed:23723244}.
-!- FUNCTION: [Isoform 2]: Essential for thymopoiesis and the development
of several secondary lymphoid tissues, including lymph nodes and
Peyer's patches (PubMed:10602018, PubMed:14691482, PubMed:16148126).
Required for the generation of LTi (lymphoid tissue inducer) cells.
Regulates thymocyte survival through DNA-binding on ROREs of target
gene promoter regions and recruitment of coactivaros via the AF-2. Also
plays a key role, downstream of IL6 and TGFB and synergistically with
RORA, for 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
(PubMed:16990136, PubMed:18164222, PubMed:26607793). May also play a
role in the pre-TCR activation cascade leading to the maturation of
alpha/beta T-cells and may participate in the regulation of DNA
accessibility in the TCR-J(alpha) locus (PubMed:9881970,
PubMed:10602018, PubMed:14691482, PubMed:16148126, PubMed:16990136,
PubMed:18164222). Plays an indispensable role in the induction of IFN-
gamma dependent anti-mycobacterial systemic immunity (By similarity).
{ECO:0000250|UniProtKB:P51449, ECO:0000269|PubMed:10602018,
ECO:0000269|PubMed:14691482, ECO:0000269|PubMed:16148126,
ECO:0000269|PubMed:16990136, ECO:0000269|PubMed:18164222,
ECO:0000269|PubMed:26607793, ECO:0000269|PubMed:9881970}.
-!- SUBUNIT: Interacts (via AF-2 motif) with the coactivators NCOA1, NCOA2
and PPARGC1A (via LXXLL motif) (PubMed:16148126, PubMed:17476214,
PubMed:21499262). Interacts with the corepressor NCOR1
(PubMed:21499262). Interacts with CRY1 (PubMed:22170608). Interacts
(via AF-2 motif) with PROX1 (PubMed:23723244). Interacts with FOXP3
(PubMed:18368049). Interacts with NR0B2 (PubMed:25212631).
{ECO:0000269|PubMed:16148126, ECO:0000269|PubMed:17476214,
ECO:0000269|PubMed:18368049, ECO:0000269|PubMed:21499262,
ECO:0000269|PubMed:22170608, ECO:0000269|PubMed:23723244,
ECO:0000269|PubMed:25212631}.
-!- INTERACTION:
Q9R1E0:Foxo1; NbExp=2; IntAct=EBI-4422078, EBI-1371343;
Q16665:HIF1A (xeno); NbExp=2; IntAct=EBI-4422078, EBI-447269;
Q61221:Hif1a; NbExp=2; IntAct=EBI-4422078, EBI-298954;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407,
ECO:0000269|PubMed:18368049, ECO:0000269|PubMed:21853531,
ECO:0000269|PubMed:22753030}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P51450-1; Sequence=Displayed;
Name=2; Synonyms=RORgT;
IsoId=P51450-2; Sequence=VSP_003659, VSP_003660;
Name=3 {ECO:0000305};
IsoId=P51450-3; Sequence=VSP_056787, VSP_056788;
-!- TISSUE SPECIFICITY: Isoform 1 is widely expressed with highest levels
in muscle, kidney and liver. Isoform 2 is expressed primarily in
immature thymocytes and the subset of mature T(H)17 cells. Neither
isoform is expressed in spleen or bone marrow.
{ECO:0000269|PubMed:10602018, ECO:0000269|PubMed:17666523,
ECO:0000269|PubMed:22753030, ECO:0000269|PubMed:9881970}.
-!- DEVELOPMENTAL STAGE: In 3T3-L1 cells, sharp decline at mRNA and protein
levels upon induction of adipocyte differentiation. Isoform 2 is
detected in the immediate vicinity of vessels among small clusters of
CD45(+) cells as early as 12.5 dpc. At 16.5 dpc, isoform 2 is expressed
exclusively in tight clusters of cells found in lymph node anlagen, in
the submucosal region of the intestine and around central vessels in
the spleen. {ECO:0000269|PubMed:17666523, ECO:0000269|PubMed:21853531}.
-!- INDUCTION: Isoform 1 expression oscillates diurnally in peripheral
tissues such as liver, brown adipose tissue (BAT), kidney and small
intestines. Isoform 2 is induced upon antigen receptor ligation in the
presence of IL6 and TGB1 (via STAT3). Induced by TGFB1 in T-cells.
{ECO:0000269|PubMed:18368049, ECO:0000269|PubMed:22753030}.
-!- DOMAIN: The AF-2 (activation function-2) motif is required for
recruiting coregulators containing LXXLL motifs such as NCOA1 and
NCOA2. {ECO:0000269|PubMed:16148126}.
-!- DISRUPTION PHENOTYPE: Mice show decreased adipocytes size and highly
insulin sensitivity, leading to an improved control of circulating
fatty acids. Mutants are protected from hyperglycemia and insulin
resistance in the state of obesity. Loss of circadian pattern of some
clock genes expression in the peripheral tissues and massive apoptosis
of thymocytes. Knockout mice for isoform 2 lack all lymph nodes and
Peyer's patches, as well as LTi cells. They also show a reduction of
T(H)17 cells in the lamina propria by at least 10-fold to less than 1%
of the T(H) cells. Mice are less susceptible to autoimmune inflammatory
diseases. {ECO:0000269|PubMed:16148126, ECO:0000269|PubMed:17666523,
ECO:0000269|PubMed:21853531, ECO:0000269|PubMed:22753030}.
-!- MISCELLANEOUS: [Isoform 1]: Produced by alternative promoter usage.
-!- MISCELLANEOUS: [Isoform 2]: Produced by alternative promoter usage.
{ECO:0000305}.
-!- MISCELLANEOUS: [Isoform 3]: Produced by alternative splicing of isoform
1. {ECO:0000305}.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
subfamily. {ECO:0000305}.
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EMBL; U43508; AAB40709.1; -; mRNA.
EMBL; AF019660; AAC53501.1; -; Genomic_DNA.
EMBL; AF019655; AAC53501.1; JOINED; Genomic_DNA.
EMBL; AF019656; AAC53501.1; JOINED; Genomic_DNA.
EMBL; AF019657; AAC53501.1; JOINED; Genomic_DNA.
EMBL; AF019658; AAC53501.1; JOINED; Genomic_DNA.
EMBL; AF019659; AAC53501.1; JOINED; Genomic_DNA.
EMBL; U39071; AAB02582.1; -; mRNA.
EMBL; AF163668; AAD46913.1; -; mRNA.
EMBL; AJ132394; CAA10661.1; -; mRNA.
EMBL; AK153941; BAE32267.1; -; mRNA.
EMBL; AC164562; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC014804; AAH14804.1; -; mRNA.
CCDS; CCDS17591.1; -. [P51450-1]
CCDS; CCDS79971.1; -. [P51450-2]
PIR; JC5375; JC5375.
RefSeq; NP_001280663.1; NM_001293734.1.
RefSeq; NP_035411.2; NM_011281.3.
SMR; P51450; -.
BioGrid; 202957; 4.
DIP; DIP-59439N; -.
IntAct; P51450; 7.
STRING; 10090.ENSMUSP00000029795; -.
BindingDB; P51450; -.
ChEMBL; CHEMBL1293231; -.
DrugCentral; P51450; -.
iPTMnet; P51450; -.
PhosphoSitePlus; P51450; -.
jPOST; P51450; -.
MaxQB; P51450; -.
PaxDb; P51450; -.
PeptideAtlas; P51450; -.
PRIDE; P51450; -.
Ensembl; ENSMUST00000200009; ENSMUSP00000143610; ENSMUSG00000028150. [P51450-3]
GeneID; 19885; -.
KEGG; mmu:19885; -.
UCSC; uc008qfy.3; mouse. [P51450-1]
UCSC; uc008qfz.3; mouse. [P51450-2]
UCSC; uc012ctn.2; mouse. [P51450-3]
CTD; 6097; -.
MGI; MGI:104856; Rorc.
eggNOG; KOG4216; Eukaryota.
eggNOG; ENOG410XUGR; LUCA.
GeneTree; ENSGT00940000161521; -.
HOGENOM; HOG000010200; -.
InParanoid; P51450; -.
KO; K08534; -.
OrthoDB; 583704at2759; -.
PhylomeDB; P51450; -.
TreeFam; TF319910; -.
Reactome; R-MMU-383280; Nuclear Receptor transcription pathway. [P51450-2]
ChiTaRS; Rorc; mouse.
PRO; PR:P51450; -.
Proteomes; UP000000589; Chromosome 3.
RNAct; P51450; protein.
Bgee; ENSMUSG00000028150; Expressed in 109 organ(s), highest expression level in thymus.
ExpressionAtlas; P51450; baseline and differential.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0016604; C:nuclear body; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
GO; GO:0098531; F:ligand-activated transcription factor activity; ISO:MGI.
GO; GO:0004879; F:nuclear receptor activity; IEA:InterPro.
GO; GO:0008142; F:oxysterol binding; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II cis-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:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0060612; P:adipose tissue development; IMP:UniProtKB.
GO; GO:0046632; P:alpha-beta T cell differentiation; IMP:MGI.
GO; GO:0030154; P:cell differentiation; IMP:MGI.
GO; GO:0036315; P:cellular response to sterol; ISO:MGI.
GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
GO; GO:0032620; P:interleukin-17 production; IDA:UniProtKB.
GO; GO:0072615; P:interleukin-17 secretion; IMP:MGI.
GO; GO:0048535; P:lymph node development; IMP:UniProtKB.
GO; GO:0048537; P:mucosal-associated lymphoid tissue development; IMP:MGI.
GO; GO:0070244; P:negative regulation of thymocyte apoptotic process; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0048541; P:Peyer's patch development; IMP:UniProtKB.
GO; GO:0042753; P:positive regulation of circadian rhythm; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IMP:MGI.
GO; GO:0045598; P:regulation of fat cell differentiation; IMP:UniProtKB.
GO; GO:0045586; P:regulation of gamma-delta T cell differentiation; IDA:MGI.
GO; GO:0010906; P:regulation of glucose metabolic process; 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:0033077; P:T cell differentiation in thymus; IMP:MGI.
GO; GO:0072539; P:T-helper 17 cell differentiation; IDA:MGI.
GO; GO:0042093; P:T-helper cell differentiation; 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; Alternative splicing;
Biological rhythms; Developmental protein; DNA-binding; Metal-binding;
Nucleus; Receptor; Reference proteome; Transcription;
Transcription regulation; Zinc; Zinc-finger.
CHAIN 1..516
/note="Nuclear receptor ROR-gamma"
/id="PRO_0000053518"
DOMAIN 267..506
/note="NR LBD"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
DNA_BIND 31..96
/note="Nuclear receptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
ZN_FING 31..51
/note="NR C4-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
ZN_FING 67..91
/note="NR C4-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
REGION 1..30
/note="Modulating"
/evidence="ECO:0000255"
MOTIF 499..504
/note="AF-2"
COMPBIAS 119..130
/note="Poly-Gln"
VAR_SEQ 1..24
/note="MDRAPQRHHRTSRELLAAKKTHTS -> MAGSYLHCA (in isoform
3)"
/evidence="ECO:0000305"
/id="VSP_056787"
VAR_SEQ 1..21
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:10602018,
ECO:0000303|PubMed:9881970"
/id="VSP_003659"
VAR_SEQ 22..24
/note="HTS -> MRT (in isoform 2)"
/evidence="ECO:0000303|PubMed:10602018,
ECO:0000303|PubMed:9881970"
/id="VSP_003660"
VAR_SEQ 310..463
/note="Missing (in isoform 3)"
/evidence="ECO:0000305"
/id="VSP_056788"
MUTAGEN 31
/note="C->A: Loss of adipogenesis inhibition, when
associated with A-48."
/evidence="ECO:0000269|PubMed:21853531"
MUTAGEN 48
/note="C->A: Loss of adipogenesis inhibition, when
associated with A-31."
/evidence="ECO:0000269|PubMed:21853531"
MUTAGEN 56..57
/note="RR->AG: Abolishes DNA-binding. No effect neither on
interaction with NCOA1 and NCOA2 nor on inhibition of
NFATC1 expression."
/evidence="ECO:0000269|PubMed:16148126"
MUTAGEN 500
/note="Y->F: Abolishes interaction with NCOA1 and NCOA2."
/evidence="ECO:0000269|PubMed:16148126"
MUTAGEN 502
/note="E->Q: Loss of transactivation function."
/evidence="ECO:0000269|PubMed:22753030"
CONFLICT 70..71
/note="QQ -> HR (in Ref. 6; BAE32267)"
/evidence="ECO:0000305"
CONFLICT 142
/note="A -> R (in Ref. 6; BAE32267)"
/evidence="ECO:0000305"
CONFLICT 181
/note="G -> A (in Ref. 6; BAE32267)"
/evidence="ECO:0000305"
CONFLICT 181
/note="G -> D (in Ref. 3; AAB02582)"
/evidence="ECO:0000305"
CONFLICT 186
/note="N -> H (in Ref. 6; BAE32267)"
/evidence="ECO:0000305"
CONFLICT 207
/note="G -> C (in Ref. 6; BAE32267)"
/evidence="ECO:0000305"
CONFLICT 352
/note="T -> K (in Ref. 3; AAB02582, 4; AAD46913 and 8;
AAH14804)"
/evidence="ECO:0000305"
SEQUENCE 516 AA; 58117 MW; 218068AF4598A93B CRC64;
MDRAPQRHHR TSRELLAAKK THTSQIEVIP CKICGDKSSG IHYGVITCEG CKGFFRRSQQ
CNVAYSCTRQ QNCPIDRTSR NRCQHCRLQK CLALGMSRDA VKFGRMSKKQ RDSLHAEVQK
QLQQQQQQEQ VAKTPPAGSR GADTLTYTLG LSDGQLPLGA SPDLPEASAC PPGLLRASGS
GPPYSNTLAK TEVQGASCHL EYSPERGKAE GRDSIYSTDG QLTLGRCGLR FEETRHPELG
EPEQGPDSHC IPSFCSAPEV PYASLTDIEY LVQNVCKSFR ETCQLRLEDL LRQRTNLFSR
EEVTSYQRKS MWEMWERCAH HLTEAIQYVV EFAKRLSGFM ELCQNDQIIL LTAGAMEVVL
VRMCRAYNAN NHTVFFEGKY GGVELFRALG CSELISSIFD FSHFLSALCF SEDEIALYTA
LVLINANRPG LQEKRRVEHL QYNLELAFHH HLCKTHRQGL LAKLPPKGKL RSLCSQHVEK
LQIFQHLHPI VVQAAFPPLY KELFSTDVES PEGLSK


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[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)
[RORC NR1F3 RORG RZRG] 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)
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[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)
[RORB NR1F2 RZRB] Nuclear receptor ROR-beta (Nuclear receptor RZR-beta) (Nuclear receptor subfamily 1 group F member 2) (Retinoid-related orphan receptor-beta)
[RORC NR1F3] Nuclear receptor ROR-gamma (Nuclear receptor RZR-gamma) (Nuclear receptor subfamily 1 group F member 3) (Retinoid-related orphan receptor-gamma)
[Nr2c2 Mtr2r1 Tak1 Tr4] Nuclear receptor subfamily 2 group C member 2 (Orphan nuclear receptor TAK1) (Orphan nuclear receptor TR4) (Testicular receptor 4)
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[PPARG NR1C3] Peroxisome proliferator-activated receptor gamma (PPAR-gamma) (Nuclear receptor subfamily 1 group C member 3)
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[rarga nr1b3a rarg rarg2 si:dkey-148f24.2] Retinoic acid receptor gamma-A (RAR-gamma-A) (zRAR gamma) (Nuclear receptor subfamily 1 group B member 3-A) (RAR-gamma-2)
[Rarg Nr1b3] Retinoic acid receptor gamma (RAR-gamma) (Nuclear receptor subfamily 1 group B member 3)
[Rxrg Nr2b3] Retinoic acid receptor RXR-gamma (Nuclear receptor subfamily 2 group B member 3) (Retinoid X receptor gamma)
[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)
[RARG NR1B3] Retinoic acid receptor gamma (RAR-gamma) (Nuclear receptor subfamily 1 group B member 3)
[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)
[Nr1h2 Lxrb] Oxysterols receptor LXR-beta (Liver X receptor beta) (Nuclear receptor subfamily 1 group H member 2) (Orphan nuclear receptor OR-1) (Ubiquitously-expressed nuclear receptor) (UR)
[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)
[rargb nr1b3b] Retinoic acid receptor gamma-B (RAR-gamma-B) (Nuclear receptor subfamily 1 group B member 3-B)
[Rxrg Nr2b3] Retinoic acid receptor RXR-gamma (Nuclear receptor subfamily 2 group B member 3) (Retinoid X receptor gamma)
[RXRG NR2B3] Retinoic acid receptor RXR-gamma (Nuclear receptor subfamily 2 group B member 3) (Retinoid X receptor gamma)
[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)
[ESRRA ERR1 ESRL1 NR3B1] Steroid hormone receptor ERR1 (Estrogen receptor-like 1) (Estrogen-related receptor alpha) (ERR-alpha) (Nuclear receptor subfamily 3 group B member 1)
[NR3C1 GRL] Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)
[Nr1h4 Bar Fxr 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)

Bibliography :