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Peroxisome proliferator-activated receptor gamma (PPAR-gamma) (Nuclear receptor subfamily 1 group C member 3)

 PPARG_MOUSE             Reviewed;         505 AA.
P37238;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
27-APR-2001, sequence version 3.
22-NOV-2017, entry version 188.
RecName: Full=Peroxisome proliferator-activated receptor gamma;
Short=PPAR-gamma;
AltName: Full=Nuclear receptor subfamily 1 group C member 3;
Name=Pparg; Synonyms=Nr1c3;
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 [MRNA] (ISOFORM 2), AND SUBUNIT.
TISSUE=Adipose tissue;
PubMed=7926726; DOI=10.1101/gad.8.10.1224;
Tontonoz P., Hu E., Graves R.A., Budavari A.I., Spiegelman B.M.;
"mPPAR gamma 2: tissue-specific regulator of an adipocyte enhancer.";
Genes Dev. 8:1224-1234(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=BALB/cJ; TISSUE=Heart;
PubMed=8240342; DOI=10.1006/bbrc.1993.2302;
Chen F., Law S.W., O'Malley B.W.;
"Identification of two mPPAR related receptors and evidence for the
existence of five subfamily members.";
Biochem. Biophys. Res. Commun. 196:671-677(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=C57BL/6 X CBA; TISSUE=Liver;
PubMed=8262913;
Zhu Y., Alvares K., Huang Q., Rao M.S., Reddy J.K.;
"Cloning of a new member of the peroxisome proliferator-activated
receptor gene family from mouse liver.";
J. Biol. Chem. 268:26817-26820(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=8041794; DOI=10.1073/pnas.91.15.7355;
Kliewer S.A., Forman B.M., Blumberg B., Ong E.S., Borgmeyer U.,
Mangelsdorf D.J., Umesono K., Evans R.M.;
"Differential expression and activation of a family of murine
peroxisome proliferator-activated receptors.";
Proc. Natl. Acad. Sci. U.S.A. 91:7355-7359(1994).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8647948; DOI=10.1172/JCI118703;
Vidal-Puig A., Jimenez-Linan M., Lowell B.B., Hamann A., Hu E.,
Spiegelman B., Flier J.S., Moller D.E.;
"Regulation of PPAR gamma gene expression by nutrition and obesity in
rodents.";
J. Clin. Invest. 97:2553-2561(1996).
[6]
PROTEIN SEQUENCE OF 66-85 AND 146-160, SUBUNIT, AND TISSUE
SPECIFICITY.
TISSUE=Adipose tissue;
PubMed=7838715; DOI=10.1093/nar/22.25.5628;
Tontonoz P., Graves R.A., Budavari A.I., Erdjument-Bromage H., Lui M.,
Hu E., Tempst P., Spiegelman B.M.;
"Adipocyte-specific transcription factor ARF6 is a heterodimeric
complex of two nuclear hormone receptors, PPAR gamma and RXR alpha.";
Nucleic Acids Res. 22:5628-5634(1994).
[7]
INTERACTION WITH PPARBP.
PubMed=9325263; DOI=10.1074/jbc.272.41.25500;
Zhu Y., Qi C., Jain S., Rao M.S., Reddy J.K.;
"Isolation and characterization of PBP, a protein that interacts with
peroxisome proliferator-activated receptor.";
J. Biol. Chem. 272:25500-25506(1997).
[8]
INTERACTION WITH NCOA6.
PubMed=10788465; DOI=10.1074/jbc.275.18.13510;
Zhu Y.-J., Kan L., Qi C., Kanwar Y.S., Yeldandi A.V., Rao M.S.,
Reddy J.K.;
"Isolation and characterization of peroxisome proliferator-activated
receptor (PPAR) interacting protein (PRIP) as a coactivator for
PPAR.";
J. Biol. Chem. 275:13510-13516(2000).
[9]
INTERACTION WITH TGFB1I1.
PubMed=15687259; DOI=10.1101/gad.1240705;
Drori S., Girnun G.D., Tou L., Szwaya J.D., Mueller E., Xia K.,
Shivdasani R.A., Spiegelman B.M.;
"Hic-5 regulates an epithelial program mediated by PPARgamma.";
Genes Dev. 19:362-375(2005).
[10]
INTERACTION WITH FAM120B.
PubMed=17595322; DOI=10.1210/me.2006-0520;
Li D., Kang Q., Wang D.-M.;
"Constitutive coactivator of peroxisome proliferator-activated
receptor (PPARgamma), a novel coactivator of PPARgamma that promotes
adipogenesis.";
Mol. Endocrinol. 21:2320-2333(2007).
[11]
FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
PubMed=19041764; DOI=10.1016/j.cmet.2008.10.009;
Wang N., Yang G., Jia Z., Zhang H., Aoyagi T., Soodvilai S.,
Symons J.D., Schnermann J.B., Gonzalez F.J., Litwin S.E., Yang T.;
"Vascular PPARgamma controls circadian variation in blood pressure and
heart rate through Bmal1.";
Cell Metab. 8:482-491(2008).
[12]
FUNCTION, AND INTERACTION WITH PRDM16.
PubMed=18719582; DOI=10.1038/nature07182;
Seale P., Bjork B., Yang W., Kajimura S., Chin S., Kuang S., Scime A.,
Devarakonda S., Conroe H.M., Erdjument-Bromage H., Tempst P.,
Rudnicki M.A., Beier D.R., Spiegelman B.M.;
"PRDM16 controls a brown fat/skeletal muscle switch.";
Nature 454:961-967(2008).
[13]
INTERACTION WITH FOXO1.
PubMed=19037106; DOI=10.1091/mbc.E08-06-0647;
Wang F., Tong Q.;
"SIRT2 suppresses adipocyte differentiation by deacetylating FOXO1 and
enhancing FOXO1's repressive interaction with PPARgamma.";
Mol. Biol. Cell 20:801-808(2009).
[14]
FUNCTION IN ADIPOGENESIS, INTERACTION WITH PER2, PHOSPHORYLATION AT
SER-112, MUTAGENESIS OF SER-112, AND TISSUE SPECIFICITY.
PubMed=21035761; DOI=10.1016/j.cmet.2010.10.005;
Grimaldi B., Bellet M.M., Katada S., Astarita G., Hirayama J.,
Amin R.H., Granneman J.G., Piomelli D., Leff T., Sassone-Corsi P.;
"PER2 controls lipid metabolism by direct regulation of PPARgamma.";
Cell Metab. 12:509-520(2010).
[15]
SUBCELLULAR LOCATION, AND INTERACTION WITH NOCT.
PubMed=20498072; DOI=10.1073/pnas.1000788107;
Kawai M., Green C.B., Lecka-Czernik B., Douris N., Gilbert M.R.,
Kojima S., Ackert-Bicknell C., Garg N., Horowitz M.C., Adamo M.L.,
Clemmons D.R., Rosen C.J.;
"A circadian-regulated gene, Nocturnin, promotes adipogenesis by
stimulating PPAR-gamma nuclear translocation.";
Proc. Natl. Acad. Sci. U.S.A. 107:10508-10513(2010).
[16]
FUNCTION IN ADIPOGENESIS, INTERACTION WITH PPP5C, PHOSPHORYLATION AT
SER-112, DEPHOSPHORYLATION AT SER-112, AND MUTAGENESIS OF SER-112.
PubMed=21994940; DOI=10.1074/jbc.M111.311662;
Hinds T.D. Jr., Stechschulte L.A., Cash H.A., Whisler D., Banerjee A.,
Yong W., Khuder S.S., Kaw M.K., Shou W., Najjar S.M., Sanchez E.R.;
"Protein phosphatase 5 mediates lipid metabolism through reciprocal
control of glucocorticoid receptor and peroxisome proliferator-
activated receptor-? (PPAR?).";
J. Biol. Chem. 286:42911-42922(2011).
[17]
GLYCOSYLATION AT THR-84.
PubMed=22226965; DOI=10.1016/j.bbrc.2011.12.086;
Ji S., Park S.Y., Roth J., Kim H.S., Cho J.W.;
"O-GlcNAc modification of PPARgamma reduces its transcriptional
activity.";
Biochem. Biophys. Res. Commun. 417:1158-1163(2012).
[18]
FUNCTION, INTERACTION WITH HELZ2 AND THRAP3, AND SUBCELLULAR LOCATION.
PubMed=23525231; DOI=10.1210/me.2012-1332;
Katano-Toki A., Satoh T., Tomaru T., Yoshino S., Ishizuka T.,
Ishii S., Ozawa A., Shibusawa N., Tsuchiya T., Saito T., Shimizu H.,
Hashimoto K., Okada S., Yamada M., Mori M.;
"THRAP3 interacts with HELZ2 and plays a novel role in adipocyte
differentiation.";
Mol. Endocrinol. 27:769-780(2013).
-!- FUNCTION: Nuclear receptor that binds peroxisome proliferators
such as hypolipidemic drugs and fatty acids. Once activated by a
ligand, the nuclear receptor binds to DNA specific PPAR response
elements (PPRE) and modulates the transcription of its target
genes, such as acyl-CoA oxidase. It therefore controls the
peroxisomal beta-oxidation pathway of fatty acids. Key regulator
of adipocyte differentiation and glucose homeostasis. ARF6 acts as
a key regulator of the tissue-specific adipocyte P2 (aP2)
enhancer. Acts as a critical regulator of gut homeostasis by
suppressing NF-kappa-B-mediated proinflammatory responses. Plays a
role in the regulation of cardiovascular circadian rhythms by
regulating the transcription of ARNTL/BMAL1 in the blood vessels
(PubMed:19041764). {ECO:0000269|PubMed:18719582,
ECO:0000269|PubMed:19041764, ECO:0000269|PubMed:21035761,
ECO:0000269|PubMed:21994940, ECO:0000269|PubMed:23525231}.
-!- ENZYME REGULATION: PDPK1 activates its transcriptional activity
independently of its kinase activity. {ECO:0007001}.
-!- SUBUNIT: Heterodimer with other nuclear receptors, such as RXRA.
The heterodimer with the retinoic acid receptor RXRA is called
adipocyte-specific transcription factor ARF6. Interacts with NCOA6
coactivator, leading to a strong increase in transcription of
target genes. Interacts with coactivator PPARBP, leading to a mild
increase in transcription of target genes. Interacts with NOCA7 in
a ligand-inducible manner. Interacts with NCOA1 and NCOA2 LXXLL
motifs. Interacts with ASXL1, ASXL2, DNTTIP2, FAM120B,
MAP2K1/MEK1, NR0B2, PDPK1, PRDM16, PRMT2 and TGFB1I1. Interacts
(when activated by agonist) with PPP5C. Interacts with HELZ2 and
THRAP3; the interaction stimulates the transcriptional activity of
PPARG. Interacts with PER2, the interaction is ligand dependent
and blocks PPARG recruitment to target promoters. Interacts with
NOCT. Interacts with FOXO1 (acetylated form). Interacts with ACTN4
(By similarity). {ECO:0000269|PubMed:10788465,
ECO:0000269|PubMed:15687259, ECO:0000269|PubMed:17595322,
ECO:0000269|PubMed:18719582, ECO:0000269|PubMed:19037106,
ECO:0000269|PubMed:20498072, ECO:0000269|PubMed:21035761,
ECO:0000269|PubMed:21994940, ECO:0000269|PubMed:23525231,
ECO:0000269|PubMed:7838715, ECO:0000269|PubMed:7926726,
ECO:0000269|PubMed:9325263, ECO:0007001|UniProtKB:P37231}.
-!- INTERACTION:
Q96EB6:SIRT1 (xeno); NbExp=3; IntAct=EBI-5260705, EBI-1802965;
Q923E4:Sirt1; NbExp=2; IntAct=EBI-5260705, EBI-1802585;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20498072,
ECO:0000269|PubMed:23525231, ECO:0000270|PROSITE-
ProRule:PRU00407}. Cytoplasm {ECO:0007001}. Note=Redistributed
from the nucleus to the cytosol through a MAP2K1/MEK1-dependent
manner (By similarity). NOCT enhances its nuclear translocation.
{ECO:0007001}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=2;
IsoId=P37238-1; Sequence=Displayed;
Name=1;
IsoId=P37238-2; Sequence=VSP_003647;
-!- TISSUE SPECIFICITY: Highest expression in white and brown adipose
tissue. Also found in liver, skeletal muscle, heart, adrenal
gland, spleen, kidney and intestine. Isoform 2 is more abundant
than isoform 1 in adipose tissue. {ECO:0000269|PubMed:21035761,
ECO:0000269|PubMed:7838715}.
-!- DEVELOPMENTAL STAGE: It appears first at 13.5 dpc and increases
until birth.
-!- INDUCTION: Expressed in a circadian manner in the aorta.
{ECO:0000269|PubMed:19041764}.
-!- PTM: O-GlcNAcylation at Thr-84 reduces transcriptional activity in
adipocytes.
-!- PTM: Phosphorylated in basal conditions and dephosphorylated when
treated with the ligand. May be dephosphorylated by PPP5C. The
phosphorylated Ser-112 form is recognized by PER2 and repressed,
dephosphorylation at Ser-112 induces adipogenic activity. Ser-112
phosphorylation levels are reduced by 65% in brown adipose tissue
compared to white adipose tissue. {ECO:0000269|PubMed:21035761,
ECO:0000269|PubMed:21994940}.
-!- DISRUPTION PHENOTYPE: Mice develop abnormalities in circadian
variations in blood pressure and heart rate, in parallel with a
reduction of diurnal variations in the sympathetic nerve activity,
and impaired rhythmicity of ARNTL/BMAL1 in the blood vessels.
{ECO:0000269|PubMed:19041764}.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
subfamily. {ECO:0000320}.
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EMBL; U09138; AAA62277.1; -; mRNA.
EMBL; U01664; AAA62110.1; -; mRNA.
EMBL; U01841; AAC52134.1; -; mRNA.
EMBL; U10374; AAA19971.1; -; mRNA.
CCDS; CCDS20439.1; -. [P37238-1]
CCDS; CCDS51876.1; -. [P37238-2]
PIR; A54101; A54101.
RefSeq; NP_001120802.1; NM_001127330.2.
RefSeq; NP_001295281.1; NM_001308352.1.
RefSeq; NP_001295283.1; NM_001308354.1.
RefSeq; NP_035276.2; NM_011146.3.
RefSeq; XP_006505806.1; XM_006505743.3.
RefSeq; XP_011239554.1; XM_011241252.1.
RefSeq; XP_017176944.1; XM_017321455.1.
UniGene; Mm.3020; -.
ProteinModelPortal; P37238; -.
SMR; P37238; -.
BioGrid; 202320; 76.
CORUM; P37238; -.
DIP; DIP-60435N; -.
ELM; P37238; -.
IntAct; P37238; 6.
STRING; 10090.ENSMUSP00000000450; -.
BindingDB; P37238; -.
ChEMBL; CHEMBL2459; -.
SwissLipids; SLP:000001625; -.
iPTMnet; P37238; -.
PhosphoSitePlus; P37238; -.
PaxDb; P37238; -.
PRIDE; P37238; -.
GeneID; 19016; -.
KEGG; mmu:19016; -.
CTD; 5468; -.
MGI; MGI:97747; Pparg.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
HOGENOM; HOG000261626; -.
HOVERGEN; HBG106004; -.
InParanoid; P37238; -.
KO; K08530; -.
PhylomeDB; P37238; -.
Reactome; R-MMU-442533; Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.
PRO; PR:P37238; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_PPARG; -.
GO; GO:0005737; C:cytoplasm; HTP:UniProtKB.
GO; GO:0005829; C:cytosol; HTP:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IGI:MGI.
GO; GO:0005654; C:nucleoplasm; IBA:Reactome.
GO; GO:0005634; C:nucleus; HTP:UniProtKB.
GO; GO:0043234; C:protein complex; IGI:MGI.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; IGI:MGI.
GO; GO:0033613; F:activating transcription factor binding; IGI:MGI.
GO; GO:0051393; F:alpha-actinin binding; IGI:MGI.
GO; GO:0050544; F:arachidonic acid binding; HTP:BHF-UCL.
GO; GO:0003682; F:chromatin binding; HTP:UniProtKB.
GO; GO:0001046; F:core promoter sequence-specific DNA binding; HTP:UniProtKB.
GO; GO:0050692; F:DBD domain binding; IGI:MGI.
GO; GO:0003677; F:DNA binding; HTP:UniProtKB.
GO; GO:0003690; F:double-stranded DNA binding; IGI:MGI.
GO; GO:0008144; F:drug binding; IGI:MGI.
GO; GO:0019899; F:enzyme binding; IGI:MGI.
GO; GO:0042802; F:identical protein binding; IGI:MGI.
GO; GO:0050693; F:LBD domain binding; IGI:MGI.
GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; HTP:UniProtKB.
GO; GO:0004879; F:nuclear receptor activity; IGI:MGI.
GO; GO:0042277; F:peptide binding; IGI:MGI.
GO; GO:0008022; F:protein C-terminus binding; IGI:MGI.
GO; GO:0046982; F:protein heterodimerization activity; IGI:MGI.
GO; GO:0043621; F:protein self-association; IGI:MGI.
GO; GO:0046965; F:retinoid X receptor binding; IGI:MGI.
GO; GO:0001012; F:RNA polymerase II regulatory region DNA binding; HTP:MGI.
GO; GO:0003707; F:steroid hormone receptor activity; RCA:InterPro.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; HTP:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IGI:MGI.
GO; GO:0044212; F:transcription regulatory region DNA binding; HTP:UniProtKB.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; HTP:MGI.
GO; GO:0050699; F:WW domain binding; HDA:MGI.
GO; GO:0008270; F:zinc ion binding; IGI:MGI.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IGI:MGI.
GO; GO:0050873; P:brown fat cell differentiation; HTP:MGI.
GO; GO:0045165; P:cell fate commitment; HDA:MGI.
GO; GO:0048469; P:cell maturation; IGI:MGI.
GO; GO:0032869; P:cellular response to insulin stimulus; HDA:MGI.
GO; GO:0071285; P:cellular response to lithium ion; HTP:MGI.
GO; GO:0071407; P:cellular response to organic cyclic compound; HTP:MGI.
GO; GO:0002024; P:diet induced thermogenesis; HDA:MGI.
GO; GO:0030855; P:epithelial cell differentiation; IPI:MGI.
GO; GO:0045444; P:fat cell differentiation; HTP:MGI.
GO; GO:0042593; P:glucose homeostasis; IGI:MGI.
GO; GO:0006954; P:inflammatory response; IBA:MGI.
GO; GO:0042953; P:lipoprotein transport; IGI:MGI.
GO; GO:0015909; P:long-chain fatty acid transport; HDA:MGI.
GO; GO:0045713; P:low-density lipoprotein particle receptor biosynthetic process; IGI:MGI.
GO; GO:0010742; P:macrophage derived foam cell differentiation; HMP:UniProtKB.
GO; GO:0030224; P:monocyte differentiation; IGI:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; HDA:MGI.
GO; GO:1900077; P:negative regulation of cellular response to insulin stimulus; HDA:BHF-UCL.
GO; GO:0010887; P:negative regulation of cholesterol storage; IGI:MGI.
GO; GO:0001818; P:negative regulation of cytokine production; HDA:BHF-UCL.
GO; GO:0060336; P:negative regulation of interferon-gamma-mediated signaling pathway; IGI:MGI.
GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; IGI:MGI.
GO; GO:0090278; P:negative regulation of peptide hormone secretion; HDA:BHF-UCL.
GO; GO:0010871; P:negative regulation of receptor biosynthetic process; IGI:MGI.
GO; GO:0010891; P:negative regulation of sequestering of triglyceride; IGI:MGI.
GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IGI:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; HTP:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; HTP:BHF-UCL.
GO; GO:0035357; P:peroxisome proliferator activated receptor signaling pathway; IDA:MGI.
GO; GO:0001890; P:placenta development; HDA:MGI.
GO; GO:0043388; P:positive regulation of DNA binding; IGI:MGI.
GO; GO:0045600; P:positive regulation of fat cell differentiation; HTP:UniProtKB.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IGI:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; HTP:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; HTP:UniProtKB.
GO; GO:0008217; P:regulation of blood pressure; IGI:MGI.
GO; GO:0042752; P:regulation of circadian rhythm; HDA:UniProtKB.
GO; GO:0045598; P:regulation of fat cell differentiation; HTP:MGI.
GO; GO:0010468; P:regulation of gene expression; HDA:MGI.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; HDA:MGI.
GO; GO:0060850; P:regulation of transcription involved in cell fate commitment; HDA:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; HDA:UniProtKB.
GO; GO:0002021; P:response to dietary excess; HTP:MGI.
GO; GO:0032094; P:response to food; HTP:UniProtKB.
GO; GO:0009416; P:response to light stimulus; HTP:UniProtKB.
GO; GO:0033993; P:response to lipid; HTP:BHF-UCL.
GO; GO:0055098; P:response to low-density lipoprotein particle stimulus; IGI:MGI.
GO; GO:0032526; P:response to retinoic acid; HTP:UniProtKB.
GO; GO:0048511; P:rhythmic process; RCA:UniProtKB-KW.
GO; GO:0007165; P:signal transduction; IGI:MGI.
GO; GO:0050872; P:white fat cell differentiation; HTP:MGI.
Gene3D; 1.10.565.10; -; 2.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR003074; 1Cnucl_rcpt.
InterPro; IPR003077; 1Cnucl_rcpt_G.
InterPro; IPR035500; NHR_like_dom_sf.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
InterPro; IPR022590; PPARgamma_N.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF12577; PPARgamma_N; 1.
Pfam; PF00105; zf-C4; 1.
PRINTS; PR01288; PROXISOMEPAR.
PRINTS; PR01291; PROXISOMPAGR.
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 splicing; Biological rhythms;
Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding;
Glycoprotein; Metal-binding; Nucleus; Phosphoprotein; Receptor;
Reference proteome; Transcription; Transcription regulation; Zinc;
Zinc-finger.
CHAIN 1 505 Peroxisome proliferator-activated
receptor gamma.
/FTId=PRO_0000053494.
DNA_BIND 136 210 Nuclear receptor. {ECO:0000270|PROSITE-
ProRule:PRU00407}.
ZN_FING 139 159 NR C4-type. {ECO:0000270|PROSITE-
ProRule:PRU00407}.
ZN_FING 176 198 NR C4-type. {ECO:0000270|PROSITE-
ProRule:PRU00407}.
REGION 205 280 Interaction with FAM120B.
{ECO:0000269|PubMed:17595322}.
REGION 317 505 Ligand-binding. {ECO:0007001}.
MOD_RES 112 112 Phosphoserine; by MAPK.
{ECO:0000269|PubMed:21035761,
ECO:0000269|PubMed:21994940}.
CARBOHYD 84 84 O-linked (GlcNAc) threonine.
{ECO:0000269|PubMed:22226965}.
VAR_SEQ 1 30 Missing (in isoform 1).
{ECO:0000319|PubMed:8041794,
ECO:0000319|PubMed:8240342,
ECO:0000319|PubMed:8262913}.
/FTId=VSP_003647.
MUTAGEN 112 112 S->A: Increases basal and ligand-induced
adipogenic activity. Abolishes repression
by PER2 on transactivation activity.
{ECO:0000269|PubMed:21035761,
ECO:0000269|PubMed:21994940}.
MUTAGEN 112 112 S->D: No effect on repression by PER2 on
transactivation activity.
{ECO:0000269|PubMed:21035761,
ECO:0000269|PubMed:21994940}.
CONFLICT 213 214 MP -> DR (in Ref. 2; AAA62110).
{ECO:0000320}.
CONFLICT 281 283 NSL -> SSF (in Ref. 2; AAA62110).
{ECO:0000320}.
CONFLICT 383 383 N -> S (in Ref. 2; AAA62110 and 4;
AAA19971). {ECO:0000320}.
CONFLICT 497 497 L -> F (in Ref. 2; AAA62110).
{ECO:0000320}.
SEQUENCE 505 AA; 57598 MW; AB8F3F6086E2A10A CRC64;
MGETLGDSPV DPEHGAFADA LPMSTSQEIT MVDTEMPFWP TNFGISSVDL SVMEDHSHSF
DIKPFTTVDF SSISAPHYED IPFTRADPMV ADYKYDLKLQ EYQSAIKVEP ASPPYYSEKT
QLYNRPHEEP SNSLMAIECR VCGDKASGFH YGVHACEGCK GFFRRTIRLK LIYDRCDLNC
RIHKKSRNKC QYCRFQKCLA VGMSHNAIRF GRMPQAEKEK LLAEISSDID QLNPESADLR
ALAKHLYDSY IKSFPLTKAK ARAILTGKTT DKSPFVIYDM NSLMMGEDKI KFKHITPLQE
QSKEVAIRIF QGCQFRSVEA VQEITEYAKN IPGFINLDLN DQVTLLKYGV HEIIYTMLAS
LMNKDGVLIS EGQGFMTREF LKNLRKPFGD FMEPKFEFAV KFNALELDDS DLAIFIAVII
LSGDRPGLLN VKPIEDIQDN LLQALELQLK LNHPESSQLF AKVLQKMTDL RQIVTEHVQL
LHVIKKTETD MSLHPLLQEI YKDLY


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