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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)

 RORG_HUMAN              Reviewed;         518 AA.
P51449; Q5SZR9; Q8N5V7; Q8NCY8;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
21-JUN-2004, sequence version 2.
05-DEC-2018, entry version 182.
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;
Name=RORC; Synonyms=NR1F3, RORG, RZRG;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Skeletal muscle;
PubMed=7811290; DOI=10.1006/bbrc.1994.2902;
Hirose T., Smith R.J., Jetten A.M.;
"ROR gamma: the third member of ROR/RZR orphan receptor subfamily that
is highly expressed in skeletal muscle.";
Biochem. Biophys. Res. Commun. 205:1976-1983(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Lymph node;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon, and Kidney;
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).
[5]
INTERACTION WITH FOXP3.
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).
[6]
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).
[7]
ACTIVITY REGULATION, AND INTERACTION WITH NCOA2.
PubMed=20211758; DOI=10.1016/j.bbalip.2010.02.012;
Wang Y., Kumar N., Crumbley C., Griffin P.R., Burris T.P.;
"A second class of nuclear receptors for oxysterols: Regulation of
RORalpha and RORgamma activity by 24S-hydroxycholesterol
(cerebrosterol).";
Biochim. Biophys. Acta 1801:917-923(2010).
[8]
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).
[9]
INDUCTION BY OBESITY.
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).
[10]
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).
[11]
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).
[12]
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).
[13]
FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN IMD42, VARIANT IMD42
LEU-38, AND CHARACTERIZATION OF VARIANT IMD42 LEU-38.
PubMed=26160376; DOI=10.1126/science.aaa4282;
Okada S., Markle J.G., Deenick E.K., Mele F., Averbuch D., Lagos M.,
Alzahrani M., Al-Muhsen S., Halwani R., Ma C.S., Wong N., Soudais C.,
Henderson L.A., Marzouqa H., Shamma J., Gonzalez M.,
Martinez-Barricarte R., Okada C., Avery D.T., Latorre D., Deswarte C.,
Jabot-Hanin F., Torrado E., Fountain J., Belkadi A., Itan Y.,
Boisson B., Migaud M., Arlehamn C.S., Sette A., Breton S.,
McCluskey J., Rossjohn J., de Villartay J.P., Moshous D.,
Hambleton S., Latour S., Arkwright P.D., Picard C., Lantz O.,
Engelhard D., Kobayashi M., Abel L., Cooper A.M., Notarangelo L.D.,
Boisson-Dupuis S., Puel A., Sallusto F., Bustamante J., Tangye S.G.,
Casanova J.L.;
"Impairment of immunity to Candida and Mycobacterium in humans with
bi-allelic RORC mutations.";
Science 349:606-613(2015).
[14]
X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 260-507 IN COMPLEX WITH
HYDROXYCHOLESTEROLS, FUNCTION TRANSCRIPTION ACTIVATOR, AND MUTAGENESIS
OF ALA-327; PHE-378 AND ILE-397.
PubMed=20203100; DOI=10.1210/me.2009-0507;
Jin L., Martynowski D., Zheng S., Wada T., Xie W., Li Y.;
"Structural basis for hydroxycholesterols as natural ligands of orphan
nuclear receptor RORgamma.";
Mol. Endocrinol. 24:923-929(2010).
-!- 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
(PubMed:19381306, PubMed:19965867, PubMed:22789990,
PubMed:26160376, PubMed:20203100). 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 (PubMed:19965867,
PubMed:22789990). Recruits distinct combinations of cofactors to
target gene regulatory regions to modulate their transcriptional
expression, depending on the tissue, time and promoter contexts.
Regulates the circadian expression of clock genes such as CRY1,
ARNTL/BMAL1 and NR1D1 in peripheral tissues and in a tissue-
selective manner. 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. Involved in the regulation of
the rhythmic expression of genes involved in glucose and lipid
metabolism, including PLIN2 and AVPR1A (PubMed:19965867). 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. Also plays also
a role in the regulation of hepatocyte glucose metabolism through
the regulation of G6PC and PCK1 (PubMed:19965867). Regulates the
rhythmic expression of PROX1 and promotes its nuclear localization
(PubMed:19381306, PubMed:19965867, PubMed:22789990,
PubMed:26160376, PubMed:20203100). Plays an indispensable role in
the induction of IFN-gamma dependent anti-mycobacterial systemic
immunity (PubMed:26160376). {ECO:0000250|UniProtKB:P51450,
ECO:0000269|PubMed:19381306, ECO:0000269|PubMed:19965867,
ECO:0000269|PubMed:20203100, ECO:0000269|PubMed:22789990,
ECO:0000269|PubMed:26160376}.
-!- FUNCTION: Isoform 2: Essential for thymopoiesis and the
development of several secondary lymphoid tissues, including lymph
nodes and Peyer's patches. 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. 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. {ECO:0000269|PubMed:21499262}.
-!- SUBUNIT: Interacts (via AF-2 motif) with the coactivator NCOA2
(via LXXLL motif). Interacts with the corepressor NCOR1. Interacts
with CRY1. Interacts (via AF-2 motif) with the coactivators NCOA1
and PPARGC1A (via LXXLL motif) (By similarity). Interacts (via AF-
2 motif) with PROX1 (By similarity). Interacts with FOXP3.
{ECO:0000250|UniProtKB:P51450, ECO:0000269|PubMed:18368049,
ECO:0000269|PubMed:20203100, ECO:0000269|PubMed:20211758,
ECO:0000269|PubMed:22170608}.
-!- INTERACTION:
Q9WTL8:Arntl (xeno); NbExp=2; IntAct=EBI-3908771, EBI-644534;
O08785:Clock (xeno); NbExp=2; IntAct=EBI-3908771, EBI-79859;
Q15788:NCOA1; NbExp=2; IntAct=EBI-3908771, EBI-455189;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26160376}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage; Named isoforms=2;
Name=1;
IsoId=P51449-1; Sequence=Displayed;
Name=2; Synonyms=RORgT;
IsoId=P51449-2; Sequence=VSP_010632, VSP_010633;
-!- TISSUE SPECIFICITY: Isoform 1 is widely expressed in many tissues,
including liver and adipose, and highly expressed in skeletal
muscle. Isoform 2 is primarily expressed in immature thymocytes.
-!- INDUCTION: Up-regulated in the state of obesity.
{ECO:0000269|PubMed:21853531}.
-!- DOMAIN: The AF-2 (activation function-2) motif is required for
recruiting coregulators containing LXXLL motifs such as NCOA1 and
NCOA2. {ECO:0000250|UniProtKB:P51450}.
-!- DISEASE: Immunodeficiency 42 (IMD42) [MIM:616622]: An autosomal
recessive primary immunodeficiency characterized by increased
susceptibility to concomitant candidiasis and mycobacteriosis.
Candidiasis is characterized by persistent and/or recurrent
infections of the skin, nails and mucous membranes caused by
organisms of the genus Candida. Mycobacteriosis is characterized
by infections caused by moderately virulent mycobacterial species,
such as Bacillus Calmette-Guerin (BCG) vaccine, environmental non-
tuberculous mycobacteria, and by the more virulent Mycobacterium
tuberculosis. IMD42 patients vaccinated with BCG are particularly
at risk for developing disseminated mycobacterial infections.
{ECO:0000269|PubMed:26160376}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA64751.1; Type=Frameshift; Positions=516; Evidence={ECO:0000305};
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EMBL; U16997; AAA64751.1; ALT_FRAME; mRNA.
EMBL; AL834219; CAD38900.1; -; mRNA.
EMBL; AL589765; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC031554; AAH31554.1; -; mRNA.
CCDS; CCDS1004.1; -. [P51449-1]
CCDS; CCDS30856.1; -. [P51449-2]
PIR; JC2494; JC2494.
RefSeq; NP_001001523.1; NM_001001523.1. [P51449-2]
RefSeq; NP_005051.2; NM_005060.3. [P51449-1]
UniGene; Hs.256022; -.
UniGene; Hs.607993; -.
PDB; 3B0W; X-ray; 2.20 A; A/B=265-507.
PDB; 3KYT; X-ray; 2.35 A; A=265-507.
PDB; 3L0J; X-ray; 2.40 A; A=265-507.
PDB; 3L0L; X-ray; 1.74 A; A/B=260-507.
PDB; 4NB6; X-ray; 2.85 A; A/B=262-507.
PDB; 4NIE; X-ray; 2.01 A; A/B=263-509.
PDB; 4QM0; X-ray; 2.20 A; A/C=262-507.
PDB; 4S14; X-ray; 3.54 A; A=262-518.
PDB; 4WLB; X-ray; 1.70 A; A/B=262-507.
PDB; 4WPF; X-ray; 2.20 A; A/D=262-509.
PDB; 4WQP; X-ray; 1.99 A; A/B=262-507, P=480-492.
PDB; 4XT9; X-ray; 2.25 A; A=265-507.
PDB; 4YMQ; X-ray; 2.00 A; A=260-507.
PDB; 4YPQ; X-ray; 2.32 A; A=265-507.
PDB; 4ZJR; X-ray; 2.70 A; A/B/C/D=265-487.
PDB; 4ZJW; X-ray; 2.50 A; A/B=265-487.
PDB; 4ZOM; X-ray; 2.27 A; A/B/C/D=265-487.
PDB; 5APH; X-ray; 1.54 A; A=265-507.
PDB; 5APJ; X-ray; 2.08 A; A=265-507.
PDB; 5APK; X-ray; 2.10 A; A/B=265-507, D=480-492.
PDB; 5AYG; X-ray; 2.60 A; A/B=261-518.
PDB; 5C4O; X-ray; 2.24 A; A=267-507.
PDB; 5C4S; X-ray; 2.23 A; A=267-507.
PDB; 5C4T; X-ray; 1.77 A; A=267-507.
PDB; 5C4U; X-ray; 2.08 A; A=267-507.
PDB; 5EJV; X-ray; 2.58 A; A/B=259-518.
PDB; 5ETH; X-ray; 2.80 A; A/B=267-487.
PDB; 5G42; X-ray; 1.72 A; A=265-507.
PDB; 5G43; X-ray; 2.58 A; A=265-507.
PDB; 5G44; X-ray; 1.84 A; A=265-507.
PDB; 5G45; X-ray; 2.07 A; A=265-507.
PDB; 5G46; X-ray; 1.76 A; A=265-507.
PDB; 5IXK; X-ray; 2.35 A; A/B=268-487.
PDB; 5IZ0; X-ray; 2.63 A; A/B/D/G=259-518.
PDB; 5K38; X-ray; 2.05 A; A/B=265-507.
PDB; 5K3L; X-ray; 2.75 A; A/B/C/D=265-507.
PDB; 5K3M; X-ray; 2.89 A; A/B=265-507.
PDB; 5K3N; X-ray; 2.67 A; A/B/C/D=265-507.
PDB; 5K6E; X-ray; 2.80 A; A/B=265-507.
PDB; 5K74; X-ray; 2.75 A; A/B=265-507.
PDB; 5LWP; X-ray; 2.40 A; A=265-506.
PDB; 5M96; X-ray; 1.77 A; A/B=263-491.
PDB; 5NI5; X-ray; 2.30 A; A=265-507.
PDB; 5NI7; X-ray; 2.45 A; A=265-507.
PDB; 5NI8; X-ray; 1.94 A; A=265-507.
PDB; 5NIB; X-ray; 1.82 A; A=265-507.
PDB; 5NTI; X-ray; 2.40 A; A/B/C/D=263-518.
PDB; 5NTK; X-ray; 1.90 A; A/B=263-491.
PDB; 5NTN; X-ray; 1.90 A; A/B/C/D=263-518.
PDB; 5NTP; X-ray; 1.70 A; A=263-499.
PDB; 5NTQ; X-ray; 2.26 A; A/B=263-499.
PDB; 5NTW; X-ray; 1.64 A; A/B/C/D=263-518.
PDB; 5NU1; X-ray; 1.85 A; A/B=263-518.
PDB; 5UFO; X-ray; 2.80 A; A=265-507.
PDB; 5UFR; X-ray; 2.07 A; A/B=265-507.
PDB; 5UHI; X-ray; 3.20 A; A/B=265-507.
PDB; 5VB3; X-ray; 1.95 A; A=260-507.
PDB; 5VB5; X-ray; 2.23 A; A=260-507.
PDB; 5VB6; X-ray; 2.04 A; A=260-507.
PDB; 5VB7; X-ray; 2.33 A; A=260-507.
PDB; 5VQK; X-ray; 3.10 A; A=260-507.
PDB; 5VQL; X-ray; 2.70 A; A=260-507.
PDB; 5W4R; X-ray; 3.00 A; A/B=265-481.
PDB; 5W4V; X-ray; 2.65 A; A/B/C/D/E/F=266-475.
PDB; 5X8Q; X-ray; 2.20 A; A/C/E/G=261-518.
PDB; 5YP5; X-ray; 2.65 A; A=265-507.
PDB; 5YP6; X-ray; 2.20 A; A=265-507.
PDB; 6B30; X-ray; 2.69 A; A/B=265-479.
PDB; 6B31; X-ray; 3.18 A; A/B=265-492.
PDB; 6BN6; X-ray; 2.40 A; A/B=265-508.
PDB; 6BR2; X-ray; 3.18 A; A/B=265-479.
PDB; 6BR3; X-ray; 3.00 A; A/B=265-480.
PDB; 6CN5; X-ray; 2.30 A; A/B=259-518.
PDB; 6CN6; X-ray; 2.45 A; A=259-517.
PDB; 6CVH; X-ray; 3.50 A; A=265-489.
PDB; 6ESN; X-ray; 1.84 A; A=265-507.
PDB; 6FGQ; X-ray; 2.37 A; A/B=265-507.
PDB; 6FZU; X-ray; 1.80 A; A/B=263-518.
PDB; 6G05; X-ray; 1.90 A; A/B=263-518.
PDB; 6G07; X-ray; 1.66 A; A/B/C/D=263-518.
PDBsum; 3B0W; -.
PDBsum; 3KYT; -.
PDBsum; 3L0J; -.
PDBsum; 3L0L; -.
PDBsum; 4NB6; -.
PDBsum; 4NIE; -.
PDBsum; 4QM0; -.
PDBsum; 4S14; -.
PDBsum; 4WLB; -.
PDBsum; 4WPF; -.
PDBsum; 4WQP; -.
PDBsum; 4XT9; -.
PDBsum; 4YMQ; -.
PDBsum; 4YPQ; -.
PDBsum; 4ZJR; -.
PDBsum; 4ZJW; -.
PDBsum; 4ZOM; -.
PDBsum; 5APH; -.
PDBsum; 5APJ; -.
PDBsum; 5APK; -.
PDBsum; 5AYG; -.
PDBsum; 5C4O; -.
PDBsum; 5C4S; -.
PDBsum; 5C4T; -.
PDBsum; 5C4U; -.
PDBsum; 5EJV; -.
PDBsum; 5ETH; -.
PDBsum; 5G42; -.
PDBsum; 5G43; -.
PDBsum; 5G44; -.
PDBsum; 5G45; -.
PDBsum; 5G46; -.
PDBsum; 5IXK; -.
PDBsum; 5IZ0; -.
PDBsum; 5K38; -.
PDBsum; 5K3L; -.
PDBsum; 5K3M; -.
PDBsum; 5K3N; -.
PDBsum; 5K6E; -.
PDBsum; 5K74; -.
PDBsum; 5LWP; -.
PDBsum; 5M96; -.
PDBsum; 5NI5; -.
PDBsum; 5NI7; -.
PDBsum; 5NI8; -.
PDBsum; 5NIB; -.
PDBsum; 5NTI; -.
PDBsum; 5NTK; -.
PDBsum; 5NTN; -.
PDBsum; 5NTP; -.
PDBsum; 5NTQ; -.
PDBsum; 5NTW; -.
PDBsum; 5NU1; -.
PDBsum; 5UFO; -.
PDBsum; 5UFR; -.
PDBsum; 5UHI; -.
PDBsum; 5VB3; -.
PDBsum; 5VB5; -.
PDBsum; 5VB6; -.
PDBsum; 5VB7; -.
PDBsum; 5VQK; -.
PDBsum; 5VQL; -.
PDBsum; 5W4R; -.
PDBsum; 5W4V; -.
PDBsum; 5X8Q; -.
PDBsum; 5YP5; -.
PDBsum; 5YP6; -.
PDBsum; 6B30; -.
PDBsum; 6B31; -.
PDBsum; 6BN6; -.
PDBsum; 6BR2; -.
PDBsum; 6BR3; -.
PDBsum; 6CN5; -.
PDBsum; 6CN6; -.
PDBsum; 6CVH; -.
PDBsum; 6ESN; -.
PDBsum; 6FGQ; -.
PDBsum; 6FZU; -.
PDBsum; 6G05; -.
PDBsum; 6G07; -.
ProteinModelPortal; P51449; -.
SMR; P51449; -.
BioGrid; 112024; 34.
DIP; DIP-60622N; -.
IntAct; P51449; 28.
MINT; P51449; -.
STRING; 9606.ENSP00000327025; -.
BindingDB; P51449; -.
ChEMBL; CHEMBL1741186; -.
GuidetoPHARMACOLOGY; 600; -.
iPTMnet; P51449; -.
PhosphoSitePlus; P51449; -.
BioMuta; RORC; -.
DMDM; 49066040; -.
PaxDb; P51449; -.
PeptideAtlas; P51449; -.
PRIDE; P51449; -.
ProteomicsDB; 56305; -.
ProteomicsDB; 56306; -. [P51449-2]
DNASU; 6097; -.
Ensembl; ENST00000318247; ENSP00000327025; ENSG00000143365. [P51449-1]
Ensembl; ENST00000356728; ENSP00000349164; ENSG00000143365. [P51449-2]
GeneID; 6097; -.
KEGG; hsa:6097; -.
UCSC; uc001ezg.4; human. [P51449-1]
CTD; 6097; -.
DisGeNET; 6097; -.
EuPathDB; HostDB:ENSG00000143365.16; -.
GeneCards; RORC; -.
HGNC; HGNC:10260; RORC.
HPA; HPA065620; -.
MalaCards; RORC; -.
MIM; 602943; gene.
MIM; 616622; phenotype.
neXtProt; NX_P51449; -.
OpenTargets; ENSG00000143365; -.
Orphanet; 477857; Autosomal recessive mendelian susceptibility to mycobacterial diseases due to complete RORgamma receptor deficiency.
PharmGKB; PA34632; -.
eggNOG; KOG4216; Eukaryota.
eggNOG; ENOG410XUGR; LUCA.
GeneTree; ENSGT00940000161521; -.
HOVERGEN; HBG106848; -.
InParanoid; P51449; -.
KO; K08534; -.
OMA; MDRAPQR; -.
OrthoDB; EOG091G0649; -.
PhylomeDB; P51449; -.
TreeFam; TF319910; -.
Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
Reactome; R-HSA-8949275; RUNX3 Regulates Immune Response and Cell Migration.
SIGNOR; P51449; -.
EvolutionaryTrace; P51449; -.
GeneWiki; RAR-related_orphan_receptor_gamma; -.
GenomeRNAi; 6097; -.
PRO; PR:P51449; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000143365; Expressed in 101 organ(s), highest expression level in gastrocnemius.
CleanEx; HS_RORC; -.
ExpressionAtlas; P51449; baseline and differential.
Genevisible; P51449; HS.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
GO; GO:0004879; F:nuclear receptor activity; TAS:ProtInc.
GO; GO:0008142; F:oxysterol binding; IDA:UniProtKB.
GO; GO:0001078; F:proximal promoter DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0003707; F:steroid hormone receptor activity; IEA:InterPro.
GO; GO:0001223; F:transcription coactivator binding; IBA:GO_Central.
GO; GO:0098531; F:transcription factor activity, direct ligand regulated sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0060612; P:adipose tissue development; ISS:UniProtKB.
GO; GO:0036315; P:cellular response to sterol; IDA:UniProtKB.
GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0048535; P:lymph node development; ISS:UniProtKB.
GO; GO:0070244; P:negative regulation of thymocyte apoptotic process; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
GO; GO:0048541; P:Peyer's patch development; ISS:UniProtKB.
GO; GO:0042753; P:positive regulation of circadian rhythm; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0045598; P:regulation of fat cell differentiation; ISS:UniProtKB.
GO; GO:0010906; P:regulation of glucose metabolic process; 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:0072539; P:T-helper 17 cell differentiation; ISS:UniProtKB.
GO; GO:0042093; P:T-helper cell differentiation; ISS:UniProtKB.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0006805; P:xenobiotic metabolic process; ISS:UniProtKB.
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;
3D-structure; Activator; Alternative promoter usage;
Biological rhythms; Complete proteome; Developmental protein;
Disease mutation; DNA-binding; Metal-binding; Nucleus; Receptor;
Reference proteome; Transcription; Transcription regulation; Zinc;
Zinc-finger.
CHAIN 1 518 Nuclear receptor ROR-gamma.
/FTId=PRO_0000053517.
DOMAIN 269 508 NR LBD. {ECO:0000255|PROSITE-
ProRule:PRU01189}.
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}.
MOTIF 501 506 AF-2.
COMPBIAS 121 130 Poly-Gln.
VAR_SEQ 1 21 Missing (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_010632.
VAR_SEQ 22 24 HTS -> MRT (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_010633.
VARIANT 38 38 S -> L (in IMD42; does not affect nuclear
localization; loss of transcription
regulatory region sequence-specific DNA
binding; loss of transcriptional
activity; dbSNP:rs774357869).
{ECO:0000269|PubMed:26160376}.
/FTId=VAR_073725.
MUTAGEN 327 327 A->F: Completely abolishes
transcriptional activity.
{ECO:0000269|PubMed:20203100}.
MUTAGEN 378 378 F->Q: Completely abolishes
transcriptional activity.
{ECO:0000269|PubMed:20203100}.
MUTAGEN 397 397 I->N: Nearly abolishes transcriptional
activity. {ECO:0000269|PubMed:20203100}.
HELIX 267 282 {ECO:0000244|PDB:5APH}.
STRAND 285 287 {ECO:0000244|PDB:5X8Q}.
HELIX 289 294 {ECO:0000244|PDB:5APH}.
HELIX 295 297 {ECO:0000244|PDB:5APH}.
HELIX 302 310 {ECO:0000244|PDB:5APH}.
HELIX 313 337 {ECO:0000244|PDB:5APH}.
HELIX 341 343 {ECO:0000244|PDB:5APH}.
HELIX 346 364 {ECO:0000244|PDB:5APH}.
HELIX 365 368 {ECO:0000244|PDB:5APH}.
TURN 371 374 {ECO:0000244|PDB:5APH}.
STRAND 375 378 {ECO:0000244|PDB:5APH}.
STRAND 381 383 {ECO:0000244|PDB:5APH}.
HELIX 385 391 {ECO:0000244|PDB:5APH}.
HELIX 394 408 {ECO:0000244|PDB:5APH}.
TURN 409 411 {ECO:0000244|PDB:5APH}.
HELIX 414 425 {ECO:0000244|PDB:5APH}.
STRAND 430 432 {ECO:0000244|PDB:5K3N}.
HELIX 436 456 {ECO:0000244|PDB:5APH}.
HELIX 460 465 {ECO:0000244|PDB:5APH}.
HELIX 469 489 {ECO:0000244|PDB:5APH}.
HELIX 491 497 {ECO:0000244|PDB:5APH}.
HELIX 500 506 {ECO:0000244|PDB:5APH}.
SEQUENCE 518 AA; 58195 MW; 7F423140BD7922BE CRC64;
MDRAPQRQHR ASRELLAAKK THTSQIEVIP CKICGDKSSG IHYGVITCEG CKGFFRRSQR
CNAAYSCTRQ QNCPIDRTSR NRCQHCRLQK CLALGMSRDA VKFGRMSKKQ RDSLHAEVQK
QLQQRQQQQQ EPVVKTPPAG AQGADTLTYT LGLPDGQLPL GSSPDLPEAS ACPPGLLKAS
GSGPSYSNNL AKAGLNGASC HLEYSPERGK AEGRESFYST GSQLTPDRCG LRFEEHRHPG
LGELGQGPDS YGSPSFRSTP EAPYASLTEI EHLVQSVCKS YRETCQLRLE DLLRQRSNIF
SREEVTGYQR KSMWEMWERC AHHLTEAIQY VVEFAKRLSG FMELCQNDQI VLLKAGAMEV
VLVRMCRAYN ADNRTVFFEG KYGGMELFRA LGCSELISSI FDFSHSLSAL HFSEDEIALY
TALVLINAHR PGLQEKRKVE QLQYNLELAF HHHLCKTHRQ SILAKLPPKG KLRSLCSQHV
ERLQIFQHLH PIVVQAAFPP LYKELFSTET ESPVGLSK


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