ID   PPARG_RAT               Reviewed;         505 AA.
AC   O88275; Q9QWG0; Q9R197;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1999, sequence version 2.
DT   27-MAR-2024, entry version 212.
DE   RecName: Full=Peroxisome proliferator-activated receptor gamma;
DE            Short=PPAR-gamma;
DE   AltName: Full=Nuclear receptor subfamily 1 group C member 3;
GN   Name=Pparg; Synonyms=Nr1c3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=Sprague-Dawley; TISSUE=Brown adipose tissue;
RX   PubMed=10438514; DOI=10.1074/jbc.274.33.23368;
RA   Guardiola-Diaz H.M., Rehnmark S., Usuda N., Albrektsen T., Feltkamp D.,
RA   Gustafsson J.-A., Alexson S.E.H.;
RT   "Rat peroxisome proliferator-activated receptors and brown adipose tissue
RT   function during cold acclimatization.";
RL   J. Biol. Chem. 274:23368-23377(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=Sprague-Dawley; TISSUE=Adipose tissue;
RA   Tanaka T., Itoh H.;
RT   "Down-regulation of PPAR gammma.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA   Escher P.;
RL   Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Adipocyte;
RA   Miyakita A., Okuno S., Watanabe T.K., Oga K., Tsuji A., Hishigaki H.,
RA   Suto T., Nakagawa K., Nakahara Y., Higashi K.;
RT   "Molecular cloning of rat PPAR-gamma gene.";
RL   Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=Long Evans;
RX   PubMed=10797535;
RX   DOI=10.1002/(sici)1097-4547(20000501)60:3<328::aid-jnr7>3.0.co;2-5;
RA   Ershov A.V., Bazan N.G.;
RT   "Photoreceptor phagocytosis selectively activates PPARgamma expression in
RT   retinal pigment epithelial cells.";
RL   J. Neurosci. Res. 60:328-337(2000).
RN   [6]
RP   PHOSPHORYLATION.
RX   PubMed=8953045; DOI=10.1126/science.274.5295.2100;
RA   Hu E., Kim J.B., Sarraf P., Spiegelman B.M.;
RT   "Inhibition of adipogenesis through MAP kinase-mediated phosphorylation of
RT   PPARgamma.";
RL   Science 274:2100-2103(1996).
RN   [7]
RP   PHOSPHORYLATION AT SER-112, AND MUTAGENESIS OF SER-112.
RX   PubMed=9030579; DOI=10.1074/jbc.272.8.5128;
RA   Adams M., Reginato M.J., Shao D., Lazar M.A., Chatterjee V.K.;
RT   "Transcriptional activation by peroxisome proliferator-activated receptor
RT   gamma is inhibited by phosphorylation at a consensus mitogen-activated
RT   protein kinase site.";
RL   J. Biol. Chem. 272:5128-5132(1997).
RN   [8]
RP   PHOSPHORYLATION.
RX   PubMed=8943212; DOI=10.1074/jbc.271.50.31771;
RA   Zhang B., Berger J., Zhou G., Elbrecht A., Biswas S., White-Carrington S.,
RA   Szalkowski D., Moller D.E.;
RT   "Insulin- and mitogen-activated protein kinase-mediated phosphorylation and
RT   activation of peroxisome proliferator-activated receptor gamma.";
RL   J. Biol. Chem. 271:31771-31774(1996).
CC   -!- FUNCTION: Nuclear receptor that binds peroxisome proliferators such as
CC       hypolipidemic drugs and fatty acids. Once activated by a ligand, the
CC       nuclear receptor binds to DNA specific PPAR response elements (PPRE)
CC       and modulates the transcription of its target genes, such as acyl-CoA
CC       oxidase. It therefore controls the peroxisomal beta-oxidation pathway
CC       of fatty acids. Key regulator of adipocyte differentiation and glucose
CC       homeostasis. ARF6 acts as a key regulator of the tissue-specific
CC       adipocyte P2 (aP2) enhancer. Acts as a critical regulator of gut
CC       homeostasis by suppressing NF-kappa-B-mediated pro-inflammatory
CC       responses. Plays a role in the regulation of cardiovascular circadian
CC       rhythms by regulating the transcription of BMAL1 in the blood vessels.
CC       {ECO:0000250|UniProtKB:P37231, ECO:0000250|UniProtKB:P37238}.
CC   -!- ACTIVITY REGULATION: PDPK1 activates its transcriptional activity
CC       independently of its kinase activity. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with FOXO1 (acetylated form) (By similarity).
CC       Heterodimer with other nuclear receptors, such as RXRA. The heterodimer
CC       with the retinoic acid receptor RXRA is called adipocyte-specific
CC       transcription factor ARF6. Interacts with NCOA6 coactivator, leading to
CC       a strong increase in transcription of target genes. Interacts with
CC       coactivator PPARBP, leading to a mild increase in transcription of
CC       target genes. Interacts with NOCA7 in a ligand-inducible manner.
CC       Interacts with NCOA1 and NCOA2 LXXLL motifs. Interacts with ASXL1,
CC       ASXL2, DNTTIP2, FAM120B, MAP2K1/MEK1, NR0B2, PDPK1, PRDM16, PRMT2 and
CC       TGFB1I1. Interacts (when activated by agonist) with PPP5C. Interacts
CC       with HELZ2 and THRAP3; the interaction stimulates the transcriptional
CC       activity of PPARG. Interacts with PER2, the interaction is ligand
CC       dependent and blocks PPARG recruitment to target promoters. Interacts
CC       with NOCT. Interacts with ACTN4. Interacts (when in the liganded
CC       conformation) with GPS2 (By similarity). Interacts with CRY1 and CRY2
CC       in a ligand-dependent manner (By similarity). In the absence of
CC       hormonal ligand, interacts with TACC1 (By similarity).
CC       {ECO:0000250|UniProtKB:P37231, ECO:0000250|UniProtKB:P37238}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
CC       Cytoplasm {ECO:0000250}. Note=Redistributed from the nucleus to the
CC       cytosol through a MAP2K1/MEK1-dependent manner. NOCT enhances its
CC       nuclear translocation (By similarity). {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=2;
CC         IsoId=O88275-1; Sequence=Displayed;
CC       Name=1;
CC         IsoId=O88275-2; Sequence=VSP_003649;
CC   -!- TISSUE SPECIFICITY: Highest expression in adipose tissue.
CC   -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC       number of yeast and animal transcription factors.
CC       {ECO:0000250|UniProtKB:P37231}.
CC   -!- PTM: Phosphorylated by MAPK. The phosphorylation inhibits PPAR gamma
CC       activity. {ECO:0000269|PubMed:8943212, ECO:0000269|PubMed:8953045,
CC       ECO:0000269|PubMed:9030579}.
CC   -!- PTM: O-GlcNAcylation at Thr-84 reduces transcriptional activity in
CC       adipocytes. {ECO:0000250|UniProtKB:P37238}.
CC   -!- PTM: Phosphorylated at basal conditions and dephosphorylated when
CC       treated with the ligand. May be dephosphorylated by PPP5C. The
CC       phosphorylated form may be inactive and dephosphorylation at induces
CC       adipogenic activity (By similarity). {ECO:0000250|UniProtKB:P37231}.
CC   -!- PTM: Ubiquitinated by E3 ubiquitin-protein ligase complex containing
CC       FBXO9; leading to proteasomal degradation (By similarity).
CC       Ubiquitinated at Lys-252 by TRIM55 leading to proteasomal degradation
CC       (By similarity). {ECO:0000250|UniProtKB:P37231,
CC       ECO:0000250|UniProtKB:P37238}.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF156666; AAD40119.1; -; mRNA.
DR   EMBL; AF156665; AAD40118.1; -; mRNA.
DR   EMBL; AB019561; BAA36485.1; -; mRNA.
DR   EMBL; Y12882; CAA73382.2; -; mRNA.
DR   EMBL; AB011365; BAA32540.1; -; mRNA.
DR   EMBL; AF246457; AAF63385.1; -; mRNA.
DR   EMBL; AF246458; AAF63386.1; -; mRNA.
DR   RefSeq; NP_001138838.1; NM_001145366.1. [O88275-2]
DR   RefSeq; NP_001138839.1; NM_001145367.1. [O88275-2]
DR   RefSeq; NP_037256.1; NM_013124.3. [O88275-1]
DR   RefSeq; XP_006237071.1; XM_006237009.3. [O88275-2]
DR   AlphaFoldDB; O88275; -.
DR   BMRB; O88275; -.
DR   SMR; O88275; -.
DR   STRING; 10116.ENSRNOP00000012137; -.
DR   BindingDB; O88275; -.
DR   ChEMBL; CHEMBL4797; -.
DR   DrugCentral; O88275; -.
DR   GlyCosmos; O88275; 1 site, No reported glycans.
DR   GlyGen; O88275; 1 site.
DR   iPTMnet; O88275; -.
DR   PhosphoSitePlus; O88275; -.
DR   PaxDb; 10116-ENSRNOP00000012137; -.
DR   Ensembl; ENSRNOT00000012137.6; ENSRNOP00000012137.3; ENSRNOG00000008839.8. [O88275-1]
DR   Ensembl; ENSRNOT00000082969.2; ENSRNOP00000073235.1; ENSRNOG00000008839.8. [O88275-2]
DR   Ensembl; ENSRNOT00055015492; ENSRNOP00055012408; ENSRNOG00055009152. [O88275-1]
DR   Ensembl; ENSRNOT00060044788; ENSRNOP00060037139; ENSRNOG00060025849. [O88275-1]
DR   Ensembl; ENSRNOT00065050179; ENSRNOP00065041216; ENSRNOG00065029023. [O88275-1]
DR   GeneID; 25664; -.
DR   KEGG; rno:25664; -.
DR   UCSC; RGD:3371; rat. [O88275-1]
DR   AGR; RGD:3371; -.
DR   CTD; 5468; -.
DR   RGD; 3371; Pparg.
DR   eggNOG; KOG3575; Eukaryota.
DR   GeneTree; ENSGT00940000158273; -.
DR   InParanoid; O88275; -.
DR   OMA; AIDYKYD; -.
DR   OrthoDB; 3475284at2759; -.
DR   PhylomeDB; O88275; -.
DR   TreeFam; TF316304; -.
DR   Reactome; R-RNO-381340; Transcriptional regulation of white adipocyte differentiation.
DR   Reactome; R-RNO-383280; Nuclear Receptor transcription pathway.
DR   PRO; PR:O88275; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Bgee; ENSRNOG00000008839; Expressed in duodenum and 18 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR   GO; GO:0043235; C:receptor complex; ISO:RGD.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR   GO; GO:0106068; C:SUMO ligase complex; ISO:RGD.
DR   GO; GO:0051393; F:alpha-actinin binding; ISO:RGD.
DR   GO; GO:0050544; F:arachidonic acid binding; ISO:RGD.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:RGD.
DR   GO; GO:0050692; F:DNA binding domain binding; ISO:RGD.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:BHF-UCL.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0003690; F:double-stranded DNA binding; ISO:RGD.
DR   GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0050693; F:LBD domain binding; ISO:RGD.
DR   GO; GO:0030331; F:nuclear estrogen receptor binding; IPI:RGD.
DR   GO; GO:0004879; F:nuclear receptor activity; ISS:UniProtKB.
DR   GO; GO:0030374; F:nuclear receptor coactivator activity; ISO:RGD.
DR   GO; GO:0046965; F:nuclear retinoid X receptor binding; ISO:RGD.
DR   GO; GO:0003676; F:nucleic acid binding; ISO:RGD.
DR   GO; GO:0042277; F:peptide binding; ISO:RGD.
DR   GO; GO:1990841; F:promoter-specific chromatin binding; ISO:RGD.
DR   GO; GO:0019903; F:protein phosphatase binding; IDA:RGD.
DR   GO; GO:0043621; F:protein self-association; ISO:RGD.
DR   GO; GO:0070412; F:R-SMAD binding; ISO:RGD.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR   GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; ISO:RGD.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISO:RGD.
DR   GO; GO:0097677; F:STAT family protein binding; ISO:RGD.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:BHF-UCL.
DR   GO; GO:0001223; F:transcription coactivator binding; IPI:RGD.
DR   GO; GO:0001221; F:transcription coregulator binding; ISO:RGD.
DR   GO; GO:0008270; F:zinc ion binding; ISO:RGD.
DR   GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
DR   GO; GO:0030509; P:BMP signaling pathway; ISO:RGD.
DR   GO; GO:0050873; P:brown fat cell differentiation; ISO:RGD.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0045165; P:cell fate commitment; ISO:RGD.
DR   GO; GO:0048469; P:cell maturation; ISO:RGD.
DR   GO; GO:0008283; P:cell population proliferation; ISO:RGD.
DR   GO; GO:0071455; P:cellular response to hyperoxia; IEP:RGD.
DR   GO; GO:0071456; P:cellular response to hypoxia; IDA:BHF-UCL.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR   GO; GO:0071285; P:cellular response to lithium ion; ISO:RGD.
DR   GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; ISO:RGD.
DR   GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:RGD.
DR   GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; ISO:RGD.
DR   GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IEP:RGD.
DR   GO; GO:0071379; P:cellular response to prostaglandin stimulus; IEP:RGD.
DR   GO; GO:0071300; P:cellular response to retinoic acid; IEP:RGD.
DR   GO; GO:0071306; P:cellular response to vitamin E; IEP:RGD.
DR   GO; GO:0106106; P:cold-induced thermogenesis; ISO:RGD.
DR   GO; GO:0002024; P:diet induced thermogenesis; ISO:RGD.
DR   GO; GO:0030855; P:epithelial cell differentiation; ISO:RGD.
DR   GO; GO:0050673; P:epithelial cell proliferation; ISO:RGD.
DR   GO; GO:0045444; P:fat cell differentiation; ISO:RGD.
DR   GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR   GO; GO:0019395; P:fatty acid oxidation; IMP:RGD.
DR   GO; GO:0042593; P:glucose homeostasis; ISO:RGD.
DR   GO; GO:0007507; P:heart development; IEP:RGD.
DR   GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0042953; P:lipoprotein transport; ISO:RGD.
DR   GO; GO:0015909; P:long-chain fatty acid transport; ISO:RGD.
DR   GO; GO:0010742; P:macrophage derived foam cell differentiation; ISS:UniProtKB.
DR   GO; GO:0030224; P:monocyte differentiation; ISO:RGD.
DR   GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0002674; P:negative regulation of acute inflammatory response; IMP:RGD.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; ISO:RGD.
DR   GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; ISO:RGD.
DR   GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISO:RGD.
DR   GO; GO:1903243; P:negative regulation of cardiac muscle hypertrophy in response to stress; IDA:BHF-UCL.
DR   GO; GO:0030308; P:negative regulation of cell growth; IMP:RGD.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:RGD.
DR   GO; GO:1900077; P:negative regulation of cellular response to insulin stimulus; ISO:RGD.
DR   GO; GO:1903845; P:negative regulation of cellular response to transforming growth factor beta stimulus; ISO:RGD.
DR   GO; GO:0010887; P:negative regulation of cholesterol storage; ISO:RGD.
DR   GO; GO:0032966; P:negative regulation of collagen biosynthetic process; IMP:RGD.
DR   GO; GO:1904597; P:negative regulation of connective tissue replacement involved in inflammatory response wound healing; IDA:BHF-UCL.
DR   GO; GO:0001818; P:negative regulation of cytokine production; ISO:RGD.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISO:RGD.
DR   GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISO:RGD.
DR   GO; GO:1901202; P:negative regulation of extracellular matrix assembly; ISO:RGD.
DR   GO; GO:0010629; P:negative regulation of gene expression; IGI:BHF-UCL.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; IBA:GO_Central.
DR   GO; GO:0010888; P:negative regulation of lipid storage; IDA:BHF-UCL.
DR   GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; ISO:RGD.
DR   GO; GO:1903979; P:negative regulation of microglial cell activation; ISO:RGD.
DR   GO; GO:1902894; P:negative regulation of miRNA transcription; ISO:RGD.
DR   GO; GO:0090258; P:negative regulation of mitochondrial fission; ISO:RGD.
DR   GO; GO:0150079; P:negative regulation of neuroinflammatory response; ISO:RGD.
DR   GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISO:RGD.
DR   GO; GO:2000230; P:negative regulation of pancreatic stellate cell proliferation; IMP:RGD.
DR   GO; GO:0090278; P:negative regulation of peptide hormone secretion; ISO:RGD.
DR   GO; GO:1904893; P:negative regulation of receptor signaling pathway via STAT; ISO:RGD.
DR   GO; GO:0010891; P:negative regulation of sequestering of triglyceride; ISO:RGD.
DR   GO; GO:0060392; P:negative regulation of SMAD protein signal transduction; ISO:RGD.
DR   GO; GO:0014912; P:negative regulation of smooth muscle cell migration; ISO:RGD.
DR   GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IGI:BHF-UCL.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISO:RGD.
DR   GO; GO:0060336; P:negative regulation of type II interferon-mediated signaling pathway; ISO:RGD.
DR   GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; ISO:RGD.
DR   GO; GO:1905563; P:negative regulation of vascular endothelial cell proliferation; ISO:RGD.
DR   GO; GO:0035357; P:peroxisome proliferator activated receptor signaling pathway; ISO:RGD.
DR   GO; GO:0001890; P:placenta development; ISO:RGD.
DR   GO; GO:0070165; P:positive regulation of adiponectin secretion; IDA:BHF-UCL.
DR   GO; GO:1904179; P:positive regulation of adipose tissue development; ISO:RGD.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR   GO; GO:0010875; P:positive regulation of cholesterol efflux; ISO:RGD.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB.
DR   GO; GO:0045600; P:positive regulation of fat cell differentiation; IMP:ARUK-UCL.
DR   GO; GO:0045923; P:positive regulation of fatty acid metabolic process; IBA:GO_Central.
DR   GO; GO:0046321; P:positive regulation of fatty acid oxidation; IMP:RGD.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR   GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:RGD.
DR   GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IMP:RGD.
DR   GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; IMP:RGD.
DR   GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; ISO:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR   GO; GO:1905461; P:positive regulation of vascular associated smooth muscle cell apoptotic process; ISO:RGD.
DR   GO; GO:0008217; P:regulation of blood pressure; ISO:RGD.
DR   GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; ISO:RGD.
DR   GO; GO:0045598; P:regulation of fat cell differentiation; IDA:RGD.
DR   GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR   GO; GO:0019216; P:regulation of lipid metabolic process; IMP:RGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:RGD.
DR   GO; GO:0031000; P:response to caffeine; IEP:RGD.
DR   GO; GO:0002021; P:response to dietary excess; ISO:RGD.
DR   GO; GO:0043627; P:response to estrogen; IEP:RGD.
DR   GO; GO:0032094; P:response to food; ISO:RGD.
DR   GO; GO:0035902; P:response to immobilization stress; IEP:RGD.
DR   GO; GO:0009416; P:response to light stimulus; ISO:RGD.
DR   GO; GO:0033993; P:response to lipid; IEP:RGD.
DR   GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
DR   GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR   GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR   GO; GO:0042594; P:response to starvation; IEP:RGD.
DR   GO; GO:0033189; P:response to vitamin A; IEP:RGD.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR   GO; GO:0048384; P:retinoic acid receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; ISO:RGD.
DR   GO; GO:0050872; P:white fat cell differentiation; ISO:RGD.
DR   GO; GO:0002246; P:wound healing involved in inflammatory response; ISO:RGD.
DR   CDD; cd06965; NR_DBD_Ppar; 1.
DR   CDD; cd06932; NR_LBD_PPAR; 1.
DR   Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1.
DR   Gene3D; 1.10.565.10; Retinoid X Receptor; 1.
DR   InterPro; IPR003074; 1Cnucl_rcpt.
DR   InterPro; IPR035500; NHR-like_dom_sf.
DR   InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR   InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR   InterPro; IPR003077; PPAR-gamma.
DR   InterPro; IPR022590; PPARgamma_N.
DR   InterPro; IPR001628; Znf_hrmn_rcpt.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   PANTHER; PTHR24082; NUCLEAR HORMONE RECEPTOR; 1.
DR   PANTHER; PTHR24082:SF488; PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR GAMMA; 1.
DR   Pfam; PF00104; Hormone_recep; 1.
DR   Pfam; PF12577; PPARgamma_N; 1.
DR   Pfam; PF00105; zf-C4; 1.
DR   PRINTS; PR01288; PROXISOMEPAR.
DR   PRINTS; PR01291; PROXISOMPAGR.
DR   PRINTS; PR00398; STRDHORMONER.
DR   PRINTS; PR00047; STROIDFINGER.
DR   SMART; SM00430; HOLI; 1.
DR   SMART; SM00399; ZnF_C4; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   SUPFAM; SSF48508; Nuclear receptor ligand-binding domain; 1.
DR   PROSITE; PS51843; NR_LBD; 1.
DR   PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR   PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
DR   Genevisible; O88275; RN.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Biological rhythms; Cytoplasm;
KW   DNA-binding; Glycoprotein; Isopeptide bond; Metal-binding; Nucleus;
KW   Phosphoprotein; Receptor; Reference proteome; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..505
FT                   /note="Peroxisome proliferator-activated receptor gamma"
FT                   /id="PRO_0000053497"
FT   DOMAIN          238..503
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        136..210
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         139..159
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         176..198
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   REGION          205..280
FT                   /note="Interaction with FAM120B"
FT                   /evidence="ECO:0000250"
FT   MOTIF           495..503
FT                   /note="9aaTAD"
FT                   /evidence="ECO:0000250|UniProtKB:P37231"
FT   MOD_RES         112
FT                   /note="Phosphoserine; by MAPK"
FT                   /evidence="ECO:0000269|PubMed:9030579"
FT   CARBOHYD        84
FT                   /note="O-linked (GlcNAc) threonine"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        252
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P37231"
FT   VAR_SEQ         1..30
FT                   /note="Missing (in isoform 1)"
FT                   /evidence="ECO:0000303|PubMed:10438514,
FT                   ECO:0000303|PubMed:10797535, ECO:0000303|Ref.4"
FT                   /id="VSP_003649"
FT   MUTAGEN         112
FT                   /note="S->A: Increases adipogenic activity."
FT                   /evidence="ECO:0000269|PubMed:9030579"
FT   CONFLICT        111
FT                   /note="A -> R (in Ref. 3; CAA73382)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   505 AA;  57567 MW;  F16E5CAB122EBB32 CRC64;
     MGETLGDPPV DPEHGAFADA LPMSTSQEIT MVDTEMPFWP TNFGISSVDL SVMDDHSHSF
     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 LKSLRKPFGD FMEPKFEFAV KFNALELDDS DLAIFIAVII
     LSGDRPGLLN VKPIEDIQDN LLQALELQLK LNHPESSQLF AKVLQKMTDL RQIVTEHVQL
     LHVIKKTETD MSLHPLLQEI YKDLY
//