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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.
22-NOV-2017, entry version 167.
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).
-!- 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). Interacts with the
corepressor NCOR1. Interacts with CRY1. Interacts (via AF-2 motif)
with PROX1. Interacts with FOXP3. {ECO:0000269|PubMed:16148126,
ECO:0000269|PubMed:17476214, ECO:0000269|PubMed:18368049,
ECO:0000269|PubMed:21499262, ECO:0000269|PubMed:22170608,
ECO:0000269|PubMed:23723244}.
-!- INTERACTION:
Q61656:Ddx5; NbExp=3; IntAct=EBI-4422044, EBI-643076;
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;
Note=Produced by alternative promoter usage.;
Name=2; Synonyms=RORgT;
IsoId=P51450-2; Sequence=VSP_003659, VSP_003660;
Note=Produced by alternative promoter usage.;
Name=3 {ECO:0000305};
IsoId=P51450-3; Sequence=VSP_056787, VSP_056788;
Note=Produced by alternative splicing of isoform 1.
{ECO:0000305};
-!- 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 E12.5. At E16.5,
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}.
-!- 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.
UniGene; Mm.4372; -.
ProteinModelPortal; P51450; -.
SMR; P51450; -.
BioGrid; 202957; 4.
DIP; DIP-59439N; -.
IntAct; P51450; 8.
STRING; 10090.ENSMUSP00000029795; -.
BindingDB; P51450; -.
ChEMBL; CHEMBL1293231; -.
iPTMnet; P51450; -.
PhosphoSitePlus; 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; ENSGT00870000136388; -.
HOGENOM; HOG000010200; -.
HOVERGEN; HBG106848; -.
InParanoid; P51450; -.
KO; K08534; -.
PhylomeDB; P51450; -.
TreeFam; TF319910; -.
Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
PRO; PR:P51450; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000028150; -.
CleanEx; MM_RORC; -.
ExpressionAtlas; P51450; baseline and differential.
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:0004879; F:nuclear receptor activity; IEA:InterPro.
GO; GO:0008142; F:oxysterol binding; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II core promoter proximal 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:0098531; F:transcription factor activity, direct ligand regulated sequence-specific DNA binding; ISO:MGI.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; ISO:MGI.
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 from RNA polymerase II promoter; 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:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
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; 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; Complete proteome; Developmental protein;
DNA-binding; Metal-binding; Nucleus; Receptor; Reference proteome;
Transcription; Transcription regulation; Zinc; Zinc-finger.
CHAIN 1 516 Nuclear receptor ROR-gamma.
/FTId=PRO_0000053518.
DNA_BIND 31 96 Nuclear receptor. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 31 51 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 67 91 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
REGION 1 30 Modulating. {ECO:0000255}.
REGION 97 266 Hinge. {ECO:0000255}.
REGION 267 516 Ligand-binding. {ECO:0000255}.
MOTIF 499 504 AF-2.
COMPBIAS 119 130 Poly-Gln.
VAR_SEQ 1 24 MDRAPQRHHRTSRELLAAKKTHTS -> MAGSYLHCA (in
isoform 3). {ECO:0000305}.
/FTId=VSP_056787.
VAR_SEQ 1 21 Missing (in isoform 2).
{ECO:0000303|PubMed:10602018,
ECO:0000303|PubMed:9881970}.
/FTId=VSP_003659.
VAR_SEQ 22 24 HTS -> MRT (in isoform 2).
{ECO:0000303|PubMed:10602018,
ECO:0000303|PubMed:9881970}.
/FTId=VSP_003660.
VAR_SEQ 310 463 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_056788.
MUTAGEN 31 31 C->A: Loss of adipogenesis inhibition,
when associated with A-48.
{ECO:0000269|PubMed:21853531}.
MUTAGEN 48 48 C->A: Loss of adipogenesis inhibition,
when associated with A-31.
{ECO:0000269|PubMed:21853531}.
MUTAGEN 56 57 RR->AG: Abolishes DNA-binding. No effect
neither on interaction with NCOA1 and
NCOA2 nor on inhibition of NFATC1
expression.
{ECO:0000269|PubMed:16148126}.
MUTAGEN 500 500 Y->F: Abolishes interaction with NCOA1
and NCOA2. {ECO:0000269|PubMed:16148126}.
MUTAGEN 502 502 E->Q: Loss of transactivation function.
{ECO:0000269|PubMed:22753030}.
CONFLICT 70 71 QQ -> HR (in Ref. 6; BAE32267).
{ECO:0000305}.
CONFLICT 142 142 A -> R (in Ref. 6; BAE32267).
{ECO:0000305}.
CONFLICT 181 181 G -> A (in Ref. 6; BAE32267).
{ECO:0000305}.
CONFLICT 181 181 G -> D (in Ref. 3; AAB02582).
{ECO:0000305}.
CONFLICT 186 186 N -> H (in Ref. 6; BAE32267).
{ECO:0000305}.
CONFLICT 207 207 G -> C (in Ref. 6; BAE32267).
{ECO:0000305}.
CONFLICT 352 352 T -> K (in Ref. 3; AAB02582, 4; AAD46913
and 8; AAH14804). {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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