RORG_HUMAN
ID RORG_HUMAN Reviewed; 518 AA.
AC P51449; Q5SZR9; Q8N5V7; Q8NCY8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2004, sequence version 2.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Nuclear receptor ROR-gamma;
DE AltName: Full=Nuclear receptor RZR-gamma;
DE AltName: Full=Nuclear receptor subfamily 1 group F member 3;
DE AltName: Full=RAR-related orphan receptor C;
DE AltName: Full=Retinoid-related orphan receptor-gamma;
GN Name=RORC; Synonyms=NR1F3, RORG, RZRG;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Skeletal muscle;
RX PubMed=7811290; DOI=10.1006/bbrc.1994.2902;
RA Hirose T., Smith R.J., Jetten A.M.;
RT "ROR gamma: the third member of ROR/RZR orphan receptor subfamily that is
RT highly expressed in skeletal muscle.";
RL Biochem. Biophys. Res. Commun. 205:1976-1983(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon, and Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH FOXP3.
RX PubMed=18368049; DOI=10.1038/nature06878;
RA Zhou L., Lopes J.E., Chong M.M., Ivanov I.I., Min R., Victora G.D.,
RA Shen Y., Du J., Rubtsov Y.P., Rudensky A.Y., Ziegler S.F., Littman D.R.;
RT "TGF-beta-induced Foxp3 inhibits T(H)17 cell differentiation by
RT antagonizing RORgammat function.";
RL Nature 453:236-240(2008).
RN [6]
RP REVIEW ON FUNCTION.
RX PubMed=19381306; DOI=10.1621/nrs.07003;
RA Jetten A.M.;
RT "Retinoid-related orphan receptors (RORs): critical roles in development,
RT immunity, circadian rhythm, and cellular metabolism.";
RL Nucl. Recept. Signal. 7:3-35(2009).
RN [7]
RP ACTIVITY REGULATION, AND INTERACTION WITH NCOA2.
RX PubMed=20211758; DOI=10.1016/j.bbalip.2010.02.012;
RA Wang Y., Kumar N., Crumbley C., Griffin P.R., Burris T.P.;
RT "A second class of nuclear receptors for oxysterols: Regulation of RORalpha
RT and RORgamma activity by 24S-hydroxycholesterol (cerebrosterol).";
RL Biochim. Biophys. Acta 1801:917-923(2010).
RN [8]
RP FUNCTION IN GLUCOSE METABOLISM REGULATION, AND IDENTIFICATION OF LIGANDS.
RX PubMed=19965867; DOI=10.1074/jbc.m109.080614;
RA Wang Y., Kumar N., Solt L.A., Richardson T.I., Helvering L.M., Crumbley C.,
RA Garcia-Ordonez R.D., Stayrook K.R., Zhang X., Novick S., Chalmers M.J.,
RA Griffin P.R., Burris T.P.;
RT "Modulation of retinoic acid receptor-related orphan receptor alpha and
RT gamma activity by 7-oxygenated sterol ligands.";
RL J. Biol. Chem. 285:5013-5025(2010).
RN [9]
RP INDUCTION BY OBESITY.
RX PubMed=21853531; DOI=10.1002/emmm.201100172;
RA Meissburger B., Ukropec J., Roeder E., Beaton N., Geiger M., Teupser D.,
RA Civan B., Langhans W., Nawroth P.P., Gasperikova D., Rudofsky G.,
RA Wolfrum C.;
RT "Adipogenesis and insulin sensitivity in obesity are regulated by retinoid-
RT related orphan receptor gamma.";
RL EMBO Mol. Med. 3:637-651(2011).
RN [10]
RP FUNCTION IN T(H)17 CELLS DIFFERENTIATION, AND IDENTIFICATION OF LIGANDS.
RX PubMed=21499262; DOI=10.1038/nature10075;
RA Solt L.A., Kumar N., Nuhant P., Wang Y., Lauer J.L., Liu J., Istrate M.A.,
RA Kamenecka T.M., Roush W.R., Vidovic D., Schuerer S.C., Xu J., Wagoner G.,
RA Drew P.D., Griffin P.R., Burris T.P.;
RT "Suppression of TH17 differentiation and autoimmunity by a synthetic ROR
RT ligand.";
RL Nature 472:491-494(2011).
RN [11]
RP INTERACTION WITH CRY1.
RX PubMed=22170608; DOI=10.1038/nature10700;
RA Lamia K.A., Papp S.J., Yu R.T., Barish G.D., Uhlenhaut N.H., Jonker J.W.,
RA Downes M., Evans R.M.;
RT "Cryptochromes mediate rhythmic repression of the glucocorticoid
RT receptor.";
RL Nature 480:552-556(2011).
RN [12]
RP REVIEW ON FUNCTION AND LIGANDS.
RX PubMed=22789990; DOI=10.1016/j.tem.2012.05.012;
RA Solt L.A., Burris T.P.;
RT "Action of RORs and their ligands in (patho)physiology.";
RL Trends Endocrinol. Metab. 23:619-627(2012).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN IMD42, VARIANT IMD42 LEU-38,
RP AND CHARACTERIZATION OF VARIANT IMD42 LEU-38.
RX PubMed=26160376; DOI=10.1126/science.aaa4282;
RA Okada S., Markle J.G., Deenick E.K., Mele F., Averbuch D., Lagos M.,
RA Alzahrani M., Al-Muhsen S., Halwani R., Ma C.S., Wong N., Soudais C.,
RA Henderson L.A., Marzouqa H., Shamma J., Gonzalez M.,
RA Martinez-Barricarte R., Okada C., Avery D.T., Latorre D., Deswarte C.,
RA Jabot-Hanin F., Torrado E., Fountain J., Belkadi A., Itan Y., Boisson B.,
RA Migaud M., Arlehamn C.S., Sette A., Breton S., McCluskey J., Rossjohn J.,
RA de Villartay J.P., Moshous D., Hambleton S., Latour S., Arkwright P.D.,
RA Picard C., Lantz O., Engelhard D., Kobayashi M., Abel L., Cooper A.M.,
RA Notarangelo L.D., Boisson-Dupuis S., Puel A., Sallusto F., Bustamante J.,
RA Tangye S.G., Casanova J.L.;
RT "Impairment of immunity to Candida and Mycobacterium in humans with bi-
RT allelic RORC mutations.";
RL Science 349:606-613(2015).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 260-507 IN COMPLEX WITH
RP HYDROXYCHOLESTEROLS, FUNCTION TRANSCRIPTION ACTIVATOR, AND MUTAGENESIS OF
RP ALA-327; PHE-378 AND ILE-397.
RX PubMed=20203100; DOI=10.1210/me.2009-0507;
RA Jin L., Martynowski D., Zheng S., Wada T., Xie W., Li Y.;
RT "Structural basis for hydroxycholesterols as natural ligands of orphan
RT nuclear receptor RORgamma.";
RL Mol. Endocrinol. 24:923-929(2010).
CC -!- FUNCTION: Nuclear receptor that binds DNA as a monomer to ROR response
CC elements (RORE) containing a single core motif half-site 5'-AGGTCA-3'
CC preceded by a short A-T-rich sequence. Key regulator of cellular
CC differentiation, immunity, peripheral circadian rhythm as well as
CC lipid, steroid, xenobiotics and glucose metabolism (PubMed:19381306,
CC PubMed:19965867, PubMed:22789990, PubMed:26160376, PubMed:20203100).
CC Considered to have intrinsic transcriptional activity, have some
CC natural ligands like oxysterols that act as agonists (25-
CC hydroxycholesterol) or inverse agonists (7-oxygenated sterols),
CC enhancing or repressing the transcriptional activity, respectively
CC (PubMed:19965867, PubMed:22789990). Recruits distinct combinations of
CC cofactors to target gene regulatory regions to modulate their
CC transcriptional expression, depending on the tissue, time and promoter
CC contexts. Regulates the circadian expression of clock genes such as
CC CRY1, ARNTL/BMAL1 and NR1D1 in peripheral tissues and in a tissue-
CC selective manner. Competes with NR1D1 for binding to their shared DNA
CC response element on some clock genes such as ARNTL/BMAL1, CRY1 and
CC NR1D1 itself, resulting in NR1D1-mediated repression or RORC-mediated
CC activation of the expression, leading to the circadian pattern of clock
CC genes expression. Therefore influences the period length and stability
CC of the clock. Involved in the regulation of the rhythmic expression of
CC genes involved in glucose and lipid metabolism, including PLIN2 and
CC AVPR1A (PubMed:19965867). Negative regulator of adipocyte
CC differentiation through the regulation of early phase genes expression,
CC such as MMP3. Controls adipogenesis as well as adipocyte size and
CC modulates insulin sensitivity in obesity. In liver, has specific and
CC redundant functions with RORA as positive or negative modulator of
CC expression of genes encoding phase I and Phase II proteins involved in
CC the metabolism of lipids, steroids and xenobiotics, such as SULT1E1.
CC Also plays a role in the regulation of hepatocyte glucose metabolism
CC through the regulation of G6PC1 and PCK1 (PubMed:19965867). Regulates
CC the rhythmic expression of PROX1 and promotes its nuclear localization
CC (PubMed:19381306, PubMed:19965867, PubMed:22789990, PubMed:26160376,
CC PubMed:20203100). Plays an indispensable role in the induction of IFN-
CC gamma dependent anti-mycobacterial systemic immunity (PubMed:26160376).
CC {ECO:0000250|UniProtKB:P51450, ECO:0000269|PubMed:19381306,
CC ECO:0000269|PubMed:19965867, ECO:0000269|PubMed:20203100,
CC ECO:0000269|PubMed:22789990, ECO:0000269|PubMed:26160376}.
CC -!- FUNCTION: [Isoform 2]: Essential for thymopoiesis and the development
CC of several secondary lymphoid tissues, including lymph nodes and
CC Peyer's patches. Required for the generation of LTi (lymphoid tissue
CC inducer) cells. Regulates thymocyte survival through DNA-binding on
CC ROREs of target gene promoter regions and recruitment of coactivaros
CC via the AF-2. Also plays a key role, downstream of IL6 and TGFB and
CC synergistically with RORA, for lineage specification of uncommitted
CC CD4(+) T-helper (T(H)) cells into T(H)17 cells, antagonizing the T(H)1
CC program. Probably regulates IL17 and IL17F expression on T(H) by
CC binding to the essential enhancer conserved non-coding sequence 2
CC (CNS2) in the IL17-IL17F locus. May also play a role in the pre-TCR
CC activation cascade leading to the maturation of alpha/beta T-cells and
CC may participate in the regulation of DNA accessibility in the TCR-
CC J(alpha) locus. {ECO:0000269|PubMed:21499262}.
CC -!- SUBUNIT: Interacts (via AF-2 motif) with the coactivator NCOA2 (via
CC LXXLL motif) (PubMed:20211758). Interacts with the corepressor NCOR1
CC (By similarity). Interacts with CRY1 (PubMed:22170608). Interacts (via
CC AF-2 motif) with the coactivators NCOA1 and PPARGC1A (via LXXLL motif)
CC (By similarity). Interacts (via AF-2 motif) with PROX1 (By similarity).
CC Interacts with FOXP3 (PubMed:18368049). Interacts with NR0B2 (By
CC similarity). {ECO:0000250|UniProtKB:P51450,
CC ECO:0000269|PubMed:18368049, ECO:0000269|PubMed:20211758,
CC ECO:0000269|PubMed:22170608}.
CC -!- INTERACTION:
CC P51449; Q15788: NCOA1; NbExp=2; IntAct=EBI-3908771, EBI-455189;
CC P51449; P62195: PSMC5; NbExp=3; IntAct=EBI-3908771, EBI-357745;
CC P51449; Q9WTL8: Arntl; Xeno; NbExp=2; IntAct=EBI-3908771, EBI-644534;
CC P51449; O08785: Clock; Xeno; NbExp=2; IntAct=EBI-3908771, EBI-79859;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26160376}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=1;
CC IsoId=P51449-1; Sequence=Displayed;
CC Name=2; Synonyms=RORgT;
CC IsoId=P51449-2; Sequence=VSP_010632, VSP_010633;
CC -!- TISSUE SPECIFICITY: Isoform 1 is widely expressed in many tissues,
CC including liver and adipose, and highly expressed in skeletal muscle.
CC Isoform 2 is primarily expressed in immature thymocytes.
CC -!- INDUCTION: Up-regulated in the state of obesity.
CC {ECO:0000269|PubMed:21853531}.
CC -!- DOMAIN: The AF-2 (activation function-2) motif is required for
CC recruiting coregulators containing LXXLL motifs such as NCOA1 and
CC NCOA2. {ECO:0000250|UniProtKB:P51450}.
CC -!- DISEASE: Immunodeficiency 42 (IMD42) [MIM:616622]: An autosomal
CC recessive primary immunodeficiency characterized by increased
CC susceptibility to concomitant candidiasis and mycobacteriosis.
CC Candidiasis is characterized by persistent and/or recurrent infections
CC of the skin, nails and mucous membranes caused by organisms of the
CC genus Candida. Mycobacteriosis is characterized by infections caused by
CC moderately virulent mycobacterial species, such as Bacillus Calmette-
CC Guerin (BCG) vaccine, environmental non-tuberculous mycobacteria, and
CC by the more virulent Mycobacterium tuberculosis. IMD42 patients
CC vaccinated with BCG are particularly at risk for developing
CC disseminated mycobacterial infections. {ECO:0000269|PubMed:26160376}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA64751.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U16997; AAA64751.1; ALT_FRAME; mRNA.
DR EMBL; AL834219; CAD38900.1; -; mRNA.
DR EMBL; AL589765; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031554; AAH31554.1; -; mRNA.
DR CCDS; CCDS1004.1; -. [P51449-1]
DR CCDS; CCDS30856.1; -. [P51449-2]
DR PIR; JC2494; JC2494.
DR RefSeq; NP_001001523.1; NM_001001523.1. [P51449-2]
DR RefSeq; NP_005051.2; NM_005060.3. [P51449-1]
DR PDB; 3B0W; X-ray; 2.20 A; A/B=265-507.
DR PDB; 3KYT; X-ray; 2.35 A; A=265-507.
DR PDB; 3L0J; X-ray; 2.40 A; A=265-507.
DR PDB; 3L0L; X-ray; 1.74 A; A/B=260-507.
DR PDB; 4NB6; X-ray; 2.85 A; A/B=262-507.
DR PDB; 4NIE; X-ray; 2.01 A; A/B=263-509.
DR PDB; 4QM0; X-ray; 2.20 A; A/C=262-507.
DR PDB; 4S14; X-ray; 3.54 A; A=262-518.
DR PDB; 4WLB; X-ray; 1.70 A; A/B=262-507.
DR PDB; 4WPF; X-ray; 2.20 A; A/D=262-509.
DR PDB; 4WQP; X-ray; 1.99 A; A/B=262-507, P=480-492.
DR PDB; 4XT9; X-ray; 2.25 A; A=265-507.
DR PDB; 4YMQ; X-ray; 2.00 A; A=260-507.
DR PDB; 4YPQ; X-ray; 2.32 A; A=265-507.
DR PDB; 4ZJR; X-ray; 2.70 A; A/B/C/D=265-487.
DR PDB; 4ZJW; X-ray; 2.50 A; A/B=265-487.
DR PDB; 4ZOM; X-ray; 2.27 A; A/B/C/D=265-487.
DR PDB; 5APH; X-ray; 1.54 A; A=265-507.
DR PDB; 5APJ; X-ray; 2.08 A; A=265-507.
DR PDB; 5APK; X-ray; 2.10 A; A/B=265-507, D=480-492.
DR PDB; 5AYG; X-ray; 2.60 A; A/B=261-518.
DR PDB; 5C4O; X-ray; 2.24 A; A=267-507.
DR PDB; 5C4S; X-ray; 2.23 A; A=267-507.
DR PDB; 5C4T; X-ray; 1.77 A; A=267-507.
DR PDB; 5C4U; X-ray; 2.08 A; A=267-507.
DR PDB; 5EJV; X-ray; 2.58 A; A/B=259-518.
DR PDB; 5ETH; X-ray; 2.80 A; A/B=267-487.
DR PDB; 5G42; X-ray; 1.72 A; A=265-507.
DR PDB; 5G43; X-ray; 2.58 A; A=265-507.
DR PDB; 5G44; X-ray; 1.84 A; A=265-507.
DR PDB; 5G45; X-ray; 2.07 A; A=265-507.
DR PDB; 5G46; X-ray; 1.76 A; A=265-507.
DR PDB; 5IXK; X-ray; 2.35 A; A/B=268-487.
DR PDB; 5IZ0; X-ray; 2.63 A; A/B/D/G=259-518.
DR PDB; 5K38; X-ray; 2.05 A; A/B=265-507.
DR PDB; 5K3L; X-ray; 2.75 A; A/B/C/D=265-507.
DR PDB; 5K3M; X-ray; 2.89 A; A/B=265-507.
DR PDB; 5K3N; X-ray; 2.67 A; A/B/C/D=265-507.
DR PDB; 5K6E; X-ray; 2.80 A; A/B=265-507.
DR PDB; 5K74; X-ray; 2.75 A; A/B=265-507.
DR PDB; 5LWP; X-ray; 2.40 A; A=265-506.
DR PDB; 5M96; X-ray; 1.77 A; A/B=263-491.
DR PDB; 5NI5; X-ray; 2.30 A; A=265-507.
DR PDB; 5NI7; X-ray; 2.45 A; A=265-507.
DR PDB; 5NI8; X-ray; 1.94 A; A=265-507.
DR PDB; 5NIB; X-ray; 1.82 A; A=265-507.
DR PDB; 5NTI; X-ray; 2.40 A; A/B/C/D=263-518.
DR PDB; 5NTK; X-ray; 1.90 A; A/B=263-491.
DR PDB; 5NTN; X-ray; 1.90 A; A/B/C/D=263-518.
DR PDB; 5NTP; X-ray; 1.70 A; A=263-499.
DR PDB; 5NTQ; X-ray; 2.26 A; A/B=263-499.
DR PDB; 5NTW; X-ray; 1.64 A; A/B/C/D=263-518.
DR PDB; 5NU1; X-ray; 1.85 A; A/B=263-518.
DR PDB; 5UFO; X-ray; 2.80 A; A=265-507.
DR PDB; 5UFR; X-ray; 2.07 A; A/B=265-507.
DR PDB; 5UHI; X-ray; 3.20 A; A/B=265-507.
DR PDB; 5VB3; X-ray; 1.95 A; A=260-507.
DR PDB; 5VB5; X-ray; 2.23 A; A=260-507.
DR PDB; 5VB6; X-ray; 2.04 A; A=260-507.
DR PDB; 5VB7; X-ray; 2.33 A; A=260-507.
DR PDB; 5VQK; X-ray; 3.10 A; A=260-507.
DR PDB; 5VQL; X-ray; 2.70 A; A=260-507.
DR PDB; 5W4R; X-ray; 3.00 A; A/B=265-481.
DR PDB; 5W4V; X-ray; 2.65 A; A/B/C/D/E/F=266-475.
DR PDB; 5X8Q; X-ray; 2.20 A; A/C/E/G=261-518.
DR PDB; 5YP5; X-ray; 2.65 A; A=265-507.
DR PDB; 5YP6; X-ray; 2.20 A; A=265-507.
DR PDB; 5ZA1; X-ray; 2.52 A; A/B=265-494.
DR PDB; 6A22; X-ray; 2.55 A; A/C/E/G=261-518.
DR PDB; 6B30; X-ray; 2.69 A; A/B=265-479.
DR PDB; 6B31; X-ray; 3.18 A; A/B=265-492.
DR PDB; 6B33; X-ray; 2.48 A; A/B=265-482.
DR PDB; 6BN6; X-ray; 2.40 A; A/B=265-508.
DR PDB; 6BR2; X-ray; 3.18 A; A/B=265-479.
DR PDB; 6BR3; X-ray; 3.00 A; A/B=265-480.
DR PDB; 6CN5; X-ray; 2.30 A; A/B=259-518.
DR PDB; 6CN6; X-ray; 2.45 A; A=259-517.
DR PDB; 6CVH; X-ray; 3.50 A; A=265-489.
DR PDB; 6E3E; X-ray; 2.47 A; A/B=265-481.
DR PDB; 6E3G; X-ray; 2.10 A; A/B=263-507.
DR PDB; 6ESN; X-ray; 1.84 A; A=265-507.
DR PDB; 6FGQ; X-ray; 2.37 A; A/B=265-507.
DR PDB; 6FZU; X-ray; 1.80 A; A/B=263-518.
DR PDB; 6G05; X-ray; 1.90 A; A/B=263-518.
DR PDB; 6G07; X-ray; 1.66 A; A/B/C/D=263-518.
DR PDB; 6IVX; X-ray; 2.35 A; A/C/E/G=261-518.
DR PDB; 6J1L; X-ray; 2.30 A; A/B/C=262-507.
DR PDB; 6J3N; X-ray; 1.99 A; A=265-509.
DR PDB; 6LO9; X-ray; 1.86 A; A=260-507.
DR PDB; 6LOA; X-ray; 2.50 A; A=260-507.
DR PDB; 6LOB; X-ray; 2.40 A; A=260-507.
DR PDB; 6LOC; X-ray; 2.20 A; A=260-507.
DR PDB; 6NAD; X-ray; 2.90 A; A/B=265-507.
DR PDB; 6NWS; X-ray; 2.44 A; A=265-507.
DR PDB; 6NWT; X-ray; 2.35 A; A/C=265-507.
DR PDB; 6NWU; X-ray; 3.20 A; A=265-507.
DR PDB; 6O3Z; X-ray; 2.40 A; A=259-508.
DR PDB; 6O98; X-ray; 2.29 A; A/B=265-508.
DR PDB; 6P9F; X-ray; 2.80 A; A/B=265-508.
DR PDB; 6Q2W; X-ray; 1.99 A; A/B=267-487.
DR PDB; 6Q6M; X-ray; 2.35 A; A=263-499.
DR PDB; 6Q6O; X-ray; 2.30 A; A=263-499.
DR PDB; 6Q7A; X-ray; 2.20 A; A=263-499.
DR PDB; 6Q7H; X-ray; 2.30 A; A=263-499.
DR PDB; 6R7A; X-ray; 2.13 A; A=265-507.
DR PDB; 6R7J; X-ray; 1.84 A; A=265-507.
DR PDB; 6R7K; X-ray; 1.54 A; A=265-507.
DR PDB; 6SAL; X-ray; 1.61 A; A=265-507.
DR PDB; 6SLZ; X-ray; 2.20 A; A/B=261-507.
DR PDB; 6T4G; X-ray; 1.93 A; A=265-507.
DR PDB; 6T4I; X-ray; 1.84 A; A=265-507.
DR PDB; 6T4J; X-ray; 1.79 A; A=265-507.
DR PDB; 6T4K; X-ray; 1.89 A; A=265-507.
DR PDB; 6T4T; X-ray; 1.62 A; A=267-507.
DR PDB; 6T4U; X-ray; 2.00 A; A=268-507.
DR PDB; 6T4W; X-ray; 1.71 A; A=268-507.
DR PDB; 6T4X; X-ray; 1.48 A; A=265-507.
DR PDB; 6T4Y; X-ray; 1.95 A; A=265-507.
DR PDB; 6T50; X-ray; 1.87 A; A=265-507.
DR PDB; 6TLM; X-ray; 2.32 A; A=265-507.
DR PDB; 6TLQ; X-ray; 1.76 A; A=265-507.
DR PDB; 6TLT; X-ray; 2.11 A; A=265-507.
DR PDB; 6U25; X-ray; 2.61 A; A=265-508.
DR PDB; 6UCG; X-ray; 2.87 A; A=267-507.
DR PDB; 6VQF; X-ray; 2.00 A; A=265-508.
DR PDB; 6VSW; X-ray; 3.20 A; A/B=261-492.
DR PDB; 6W9H; X-ray; 2.00 A; A=265-508.
DR PDB; 6W9I; X-ray; 1.61 A; A=265-508.
DR PDB; 6XAE; X-ray; 2.26 A; A=265-508.
DR PDB; 6XFV; X-ray; 2.15 A; A/B=265-508.
DR PDB; 7E3M; X-ray; 2.80 A; A=265-507.
DR PDB; 7JH2; X-ray; 2.37 A; A/B=265-508.
DR PDB; 7JTM; X-ray; 2.43 A; A=265-508.
DR PDB; 7JTW; X-ray; 1.90 A; A=259-508.
DR PDB; 7JYM; X-ray; 3.05 A; A=265-508.
DR PDB; 7KCO; X-ray; 1.86 A; A/B=262-507.
DR PDB; 7KQJ; X-ray; 2.65 A; A=265-508.
DR PDB; 7KXD; X-ray; 1.62 A; A=265-508.
DR PDB; 7KXE; X-ray; 2.42 A; A=265-508.
DR PDB; 7KXF; X-ray; 2.14 A; A=265-508.
DR PDB; 7LUK; X-ray; 2.09 A; A=265-508.
DR PDB; 7NEC; X-ray; 1.95 A; A=265-507.
DR PDB; 7NP5; X-ray; 1.55 A; A=265-507.
DR PDB; 7NP6; X-ray; 1.84 A; A=265-507.
DR PDB; 7NPC; X-ray; 1.47 A; A=268-507.
DR PDB; 7OFI; X-ray; 1.95 A; A=265-507.
DR PDB; 7OFK; X-ray; 1.61 A; A=265-507.
DR PDBsum; 3B0W; -.
DR PDBsum; 3KYT; -.
DR PDBsum; 3L0J; -.
DR PDBsum; 3L0L; -.
DR PDBsum; 4NB6; -.
DR PDBsum; 4NIE; -.
DR PDBsum; 4QM0; -.
DR PDBsum; 4S14; -.
DR PDBsum; 4WLB; -.
DR PDBsum; 4WPF; -.
DR PDBsum; 4WQP; -.
DR PDBsum; 4XT9; -.
DR PDBsum; 4YMQ; -.
DR PDBsum; 4YPQ; -.
DR PDBsum; 4ZJR; -.
DR PDBsum; 4ZJW; -.
DR PDBsum; 4ZOM; -.
DR PDBsum; 5APH; -.
DR PDBsum; 5APJ; -.
DR PDBsum; 5APK; -.
DR PDBsum; 5AYG; -.
DR PDBsum; 5C4O; -.
DR PDBsum; 5C4S; -.
DR PDBsum; 5C4T; -.
DR PDBsum; 5C4U; -.
DR PDBsum; 5EJV; -.
DR PDBsum; 5ETH; -.
DR PDBsum; 5G42; -.
DR PDBsum; 5G43; -.
DR PDBsum; 5G44; -.
DR PDBsum; 5G45; -.
DR PDBsum; 5G46; -.
DR PDBsum; 5IXK; -.
DR PDBsum; 5IZ0; -.
DR PDBsum; 5K38; -.
DR PDBsum; 5K3L; -.
DR PDBsum; 5K3M; -.
DR PDBsum; 5K3N; -.
DR PDBsum; 5K6E; -.
DR PDBsum; 5K74; -.
DR PDBsum; 5LWP; -.
DR PDBsum; 5M96; -.
DR PDBsum; 5NI5; -.
DR PDBsum; 5NI7; -.
DR PDBsum; 5NI8; -.
DR PDBsum; 5NIB; -.
DR PDBsum; 5NTI; -.
DR PDBsum; 5NTK; -.
DR PDBsum; 5NTN; -.
DR PDBsum; 5NTP; -.
DR PDBsum; 5NTQ; -.
DR PDBsum; 5NTW; -.
DR PDBsum; 5NU1; -.
DR PDBsum; 5UFO; -.
DR PDBsum; 5UFR; -.
DR PDBsum; 5UHI; -.
DR PDBsum; 5VB3; -.
DR PDBsum; 5VB5; -.
DR PDBsum; 5VB6; -.
DR PDBsum; 5VB7; -.
DR PDBsum; 5VQK; -.
DR PDBsum; 5VQL; -.
DR PDBsum; 5W4R; -.
DR PDBsum; 5W4V; -.
DR PDBsum; 5X8Q; -.
DR PDBsum; 5YP5; -.
DR PDBsum; 5YP6; -.
DR PDBsum; 5ZA1; -.
DR PDBsum; 6A22; -.
DR PDBsum; 6B30; -.
DR PDBsum; 6B31; -.
DR PDBsum; 6B33; -.
DR PDBsum; 6BN6; -.
DR PDBsum; 6BR2; -.
DR PDBsum; 6BR3; -.
DR PDBsum; 6CN5; -.
DR PDBsum; 6CN6; -.
DR PDBsum; 6CVH; -.
DR PDBsum; 6E3E; -.
DR PDBsum; 6E3G; -.
DR PDBsum; 6ESN; -.
DR PDBsum; 6FGQ; -.
DR PDBsum; 6FZU; -.
DR PDBsum; 6G05; -.
DR PDBsum; 6G07; -.
DR PDBsum; 6IVX; -.
DR PDBsum; 6J1L; -.
DR PDBsum; 6J3N; -.
DR PDBsum; 6LO9; -.
DR PDBsum; 6LOA; -.
DR PDBsum; 6LOB; -.
DR PDBsum; 6LOC; -.
DR PDBsum; 6NAD; -.
DR PDBsum; 6NWS; -.
DR PDBsum; 6NWT; -.
DR PDBsum; 6NWU; -.
DR PDBsum; 6O3Z; -.
DR PDBsum; 6O98; -.
DR PDBsum; 6P9F; -.
DR PDBsum; 6Q2W; -.
DR PDBsum; 6Q6M; -.
DR PDBsum; 6Q6O; -.
DR PDBsum; 6Q7A; -.
DR PDBsum; 6Q7H; -.
DR PDBsum; 6R7A; -.
DR PDBsum; 6R7J; -.
DR PDBsum; 6R7K; -.
DR PDBsum; 6SAL; -.
DR PDBsum; 6SLZ; -.
DR PDBsum; 6T4G; -.
DR PDBsum; 6T4I; -.
DR PDBsum; 6T4J; -.
DR PDBsum; 6T4K; -.
DR PDBsum; 6T4T; -.
DR PDBsum; 6T4U; -.
DR PDBsum; 6T4W; -.
DR PDBsum; 6T4X; -.
DR PDBsum; 6T4Y; -.
DR PDBsum; 6T50; -.
DR PDBsum; 6TLM; -.
DR PDBsum; 6TLQ; -.
DR PDBsum; 6TLT; -.
DR PDBsum; 6U25; -.
DR PDBsum; 6UCG; -.
DR PDBsum; 6VQF; -.
DR PDBsum; 6VSW; -.
DR PDBsum; 6W9H; -.
DR PDBsum; 6W9I; -.
DR PDBsum; 6XAE; -.
DR PDBsum; 6XFV; -.
DR PDBsum; 7E3M; -.
DR PDBsum; 7JH2; -.
DR PDBsum; 7JTM; -.
DR PDBsum; 7JTW; -.
DR PDBsum; 7JYM; -.
DR PDBsum; 7KCO; -.
DR PDBsum; 7KQJ; -.
DR PDBsum; 7KXD; -.
DR PDBsum; 7KXE; -.
DR PDBsum; 7KXF; -.
DR PDBsum; 7LUK; -.
DR PDBsum; 7NEC; -.
DR PDBsum; 7NP5; -.
DR PDBsum; 7NP6; -.
DR PDBsum; 7NPC; -.
DR PDBsum; 7OFI; -.
DR PDBsum; 7OFK; -.
DR AlphaFoldDB; P51449; -.
DR SASBDB; P51449; -.
DR SMR; P51449; -.
DR BioGRID; 112024; 40.
DR DIP; DIP-60622N; -.
DR IntAct; P51449; 32.
DR MINT; P51449; -.
DR STRING; 9606.ENSP00000327025; -.
DR BindingDB; P51449; -.
DR ChEMBL; CHEMBL1741186; -.
DR DrugCentral; P51449; -.
DR GuidetoPHARMACOLOGY; 600; -.
DR iPTMnet; P51449; -.
DR PhosphoSitePlus; P51449; -.
DR BioMuta; RORC; -.
DR DMDM; 49066040; -.
DR jPOST; P51449; -.
DR MassIVE; P51449; -.
DR PaxDb; P51449; -.
DR PeptideAtlas; P51449; -.
DR PRIDE; P51449; -.
DR ProteomicsDB; 56305; -. [P51449-1]
DR ProteomicsDB; 56306; -. [P51449-2]
DR Antibodypedia; 20336; 818 antibodies from 43 providers.
DR DNASU; 6097; -.
DR Ensembl; ENST00000318247.7; ENSP00000327025.6; ENSG00000143365.19. [P51449-1]
DR Ensembl; ENST00000356728.11; ENSP00000349164.6; ENSG00000143365.19. [P51449-2]
DR GeneID; 6097; -.
DR KEGG; hsa:6097; -.
DR MANE-Select; ENST00000318247.7; ENSP00000327025.6; NM_005060.4; NP_005051.2.
DR UCSC; uc001ezg.4; human. [P51449-1]
DR CTD; 6097; -.
DR DisGeNET; 6097; -.
DR GeneCards; RORC; -.
DR HGNC; HGNC:10260; RORC.
DR HPA; ENSG00000143365; Tissue enhanced (liver, skeletal muscle).
DR MalaCards; RORC; -.
DR MIM; 602943; gene.
DR MIM; 616622; phenotype.
DR neXtProt; NX_P51449; -.
DR OpenTargets; ENSG00000143365; -.
DR Orphanet; 477857; Autosomal recessive mendelian susceptibility to mycobacterial diseases due to complete RORgamma receptor deficiency.
DR PharmGKB; PA34632; -.
DR VEuPathDB; HostDB:ENSG00000143365; -.
DR eggNOG; KOG4216; Eukaryota.
DR GeneTree; ENSGT00940000161521; -.
DR HOGENOM; CLU_007368_2_0_1; -.
DR InParanoid; P51449; -.
DR OMA; ILHRDNH; -.
DR OrthoDB; 583704at2759; -.
DR PhylomeDB; P51449; -.
DR TreeFam; TF319910; -.
DR PathwayCommons; P51449; -.
DR Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-HSA-8949275; RUNX3 Regulates Immune Response and Cell Migration. [P51449-2]
DR SignaLink; P51449; -.
DR SIGNOR; P51449; -.
DR BioGRID-ORCS; 6097; 12 hits in 1094 CRISPR screens.
DR ChiTaRS; RORC; human.
DR EvolutionaryTrace; P51449; -.
DR GeneWiki; RAR-related_orphan_receptor_gamma; -.
DR GenomeRNAi; 6097; -.
DR Pharos; P51449; Tchem.
DR PRO; PR:P51449; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P51449; protein.
DR Bgee; ENSG00000143365; Expressed in gastrocnemius and 149 other tissues.
DR ExpressionAtlas; P51449; baseline and differential.
DR Genevisible; P51449; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0098531; F:ligand-activated transcription factor activity; IDA:UniProtKB.
DR GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central.
DR GO; GO:0008142; F:oxysterol binding; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0060612; P:adipose tissue development; ISS:UniProtKB.
DR GO; GO:0036315; P:cellular response to sterol; IDA:UniProtKB.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0048535; P:lymph node development; ISS:UniProtKB.
DR GO; GO:0070244; P:negative regulation of thymocyte apoptotic process; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0048541; P:Peyer's patch development; ISS:UniProtKB.
DR GO; GO:0042753; P:positive regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0045598; P:regulation of fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0010906; P:regulation of glucose metabolic process; ISS:UniProtKB.
DR GO; GO:0019218; P:regulation of steroid metabolic process; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0072539; P:T-helper 17 cell differentiation; ISS:UniProtKB.
DR GO; GO:0042093; P:T-helper cell differentiation; ISS:UniProtKB.
DR GO; GO:0006805; P:xenobiotic metabolic process; ISS:UniProtKB.
DR CDD; cd06968; NR_DBD_ROR; 1.
DR DisProt; DP01647; -.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR IDEAL; IID00305; -.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR044101; NR_DBD_ROR.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR003079; ROR_rcpt.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR01293; RORNUCRECPTR.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative promoter usage; Biological rhythms;
KW Developmental protein; Disease variant; DNA-binding; Metal-binding;
KW Nucleus; Receptor; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..518
FT /note="Nuclear receptor ROR-gamma"
FT /id="PRO_0000053517"
FT DOMAIN 269..508
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 31..96
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 31..51
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 67..91
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..30
FT /note="Modulating"
FT /evidence="ECO:0000255"
FT REGION 105..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 501..506
FT /note="AF-2"
FT COMPBIAS 119..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..21
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_010632"
FT VAR_SEQ 22..24
FT /note="HTS -> MRT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_010633"
FT VARIANT 38
FT /note="S -> L (in IMD42; does not affect nuclear
FT localization; loss of transcription regulatory region
FT sequence-specific DNA binding; loss of transcriptional
FT activity; dbSNP:rs774357869)"
FT /evidence="ECO:0000269|PubMed:26160376"
FT /id="VAR_073725"
FT MUTAGEN 327
FT /note="A->F: Completely abolishes transcriptional
FT activity."
FT /evidence="ECO:0000269|PubMed:20203100"
FT MUTAGEN 378
FT /note="F->Q: Completely abolishes transcriptional
FT activity."
FT /evidence="ECO:0000269|PubMed:20203100"
FT MUTAGEN 397
FT /note="I->N: Nearly abolishes transcriptional activity."
FT /evidence="ECO:0000269|PubMed:20203100"
FT HELIX 269..284
FT /evidence="ECO:0007829|PDB:7NPC"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:7NP5"
FT HELIX 289..294
FT /evidence="ECO:0007829|PDB:7NPC"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:7NPC"
FT HELIX 302..310
FT /evidence="ECO:0007829|PDB:7NPC"
FT HELIX 313..336
FT /evidence="ECO:0007829|PDB:7NPC"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:7NPC"
FT HELIX 346..364
FT /evidence="ECO:0007829|PDB:7NPC"
FT HELIX 365..368
FT /evidence="ECO:0007829|PDB:7NPC"
FT TURN 371..374
FT /evidence="ECO:0007829|PDB:7NPC"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:7NPC"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:7NPC"
FT HELIX 385..391
FT /evidence="ECO:0007829|PDB:7NPC"
FT HELIX 394..408
FT /evidence="ECO:0007829|PDB:7NPC"
FT TURN 409..411
FT /evidence="ECO:0007829|PDB:7NPC"
FT HELIX 414..425
FT /evidence="ECO:0007829|PDB:7NPC"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:5K3N"
FT HELIX 436..456
FT /evidence="ECO:0007829|PDB:7NPC"
FT HELIX 460..465
FT /evidence="ECO:0007829|PDB:7NPC"
FT HELIX 471..489
FT /evidence="ECO:0007829|PDB:7NPC"
FT HELIX 491..497
FT /evidence="ECO:0007829|PDB:5APH"
FT HELIX 499..505
FT /evidence="ECO:0007829|PDB:7NPC"
SQ 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
