PPARG_MOUSE
ID PPARG_MOUSE Reviewed; 505 AA.
AC P37238;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 3.
DT 03-AUG-2022, entry version 221.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND SUBUNIT.
RC TISSUE=Adipose tissue;
RX PubMed=7926726; DOI=10.1101/gad.8.10.1224;
RA Tontonoz P., Hu E., Graves R.A., Budavari A.I., Spiegelman B.M.;
RT "mPPAR gamma 2: tissue-specific regulator of an adipocyte enhancer.";
RL Genes Dev. 8:1224-1234(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ; TISSUE=Heart;
RX PubMed=8240342; DOI=10.1006/bbrc.1993.2302;
RA Chen F., Law S.W., O'Malley B.W.;
RT "Identification of two mPPAR related receptors and evidence for the
RT existence of five subfamily members.";
RL Biochem. Biophys. Res. Commun. 196:671-677(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6 X CBA; TISSUE=Liver;
RX PubMed=8262913; DOI=10.1016/s0021-9258(19)74184-2;
RA Zhu Y., Alvares K., Huang Q., Rao M.S., Reddy J.K.;
RT "Cloning of a new member of the peroxisome proliferator-activated receptor
RT gene family from mouse liver.";
RL J. Biol. Chem. 268:26817-26820(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=8041794; DOI=10.1073/pnas.91.15.7355;
RA Kliewer S.A., Forman B.M., Blumberg B., Ong E.S., Borgmeyer U.,
RA Mangelsdorf D.J., Umesono K., Evans R.M.;
RT "Differential expression and activation of a family of murine peroxisome
RT proliferator-activated receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:7355-7359(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8647948; DOI=10.1172/jci118703;
RA Vidal-Puig A., Jimenez-Linan M., Lowell B.B., Hamann A., Hu E.,
RA Spiegelman B., Flier J.S., Moller D.E.;
RT "Regulation of PPAR gamma gene expression by nutrition and obesity in
RT rodents.";
RL J. Clin. Invest. 97:2553-2561(1996).
RN [6]
RP PROTEIN SEQUENCE OF 66-85 AND 146-160, SUBUNIT, AND TISSUE SPECIFICITY.
RC TISSUE=Adipose tissue;
RX PubMed=7838715; DOI=10.1093/nar/22.25.5628;
RA Tontonoz P., Graves R.A., Budavari A.I., Erdjument-Bromage H., Lui M.,
RA Hu E., Tempst P., Spiegelman B.M.;
RT "Adipocyte-specific transcription factor ARF6 is a heterodimeric complex of
RT two nuclear hormone receptors, PPAR gamma and RXR alpha.";
RL Nucleic Acids Res. 22:5628-5634(1994).
RN [7]
RP INTERACTION WITH PPARBP.
RX PubMed=9325263; DOI=10.1074/jbc.272.41.25500;
RA Zhu Y., Qi C., Jain S., Rao M.S., Reddy J.K.;
RT "Isolation and characterization of PBP, a protein that interacts with
RT peroxisome proliferator-activated receptor.";
RL J. Biol. Chem. 272:25500-25506(1997).
RN [8]
RP INTERACTION WITH NCOA6.
RX PubMed=10788465; DOI=10.1074/jbc.275.18.13510;
RA Zhu Y.-J., Kan L., Qi C., Kanwar Y.S., Yeldandi A.V., Rao M.S., Reddy J.K.;
RT "Isolation and characterization of peroxisome proliferator-activated
RT receptor (PPAR) interacting protein (PRIP) as a coactivator for PPAR.";
RL J. Biol. Chem. 275:13510-13516(2000).
RN [9]
RP INTERACTION WITH TGFB1I1.
RX PubMed=15687259; DOI=10.1101/gad.1240705;
RA Drori S., Girnun G.D., Tou L., Szwaya J.D., Mueller E., Xia K.,
RA Shivdasani R.A., Spiegelman B.M.;
RT "Hic-5 regulates an epithelial program mediated by PPARgamma.";
RL Genes Dev. 19:362-375(2005).
RN [10]
RP INTERACTION WITH FAM120B.
RX PubMed=17595322; DOI=10.1210/me.2006-0520;
RA Li D., Kang Q., Wang D.-M.;
RT "Constitutive coactivator of peroxisome proliferator-activated receptor
RT (PPARgamma), a novel coactivator of PPARgamma that promotes adipogenesis.";
RL Mol. Endocrinol. 21:2320-2333(2007).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=19041764; DOI=10.1016/j.cmet.2008.10.009;
RA Wang N., Yang G., Jia Z., Zhang H., Aoyagi T., Soodvilai S., Symons J.D.,
RA Schnermann J.B., Gonzalez F.J., Litwin S.E., Yang T.;
RT "Vascular PPARgamma controls circadian variation in blood pressure and
RT heart rate through Bmal1.";
RL Cell Metab. 8:482-491(2008).
RN [12]
RP FUNCTION, AND INTERACTION WITH PRDM16.
RX PubMed=18719582; DOI=10.1038/nature07182;
RA Seale P., Bjork B., Yang W., Kajimura S., Chin S., Kuang S., Scime A.,
RA Devarakonda S., Conroe H.M., Erdjument-Bromage H., Tempst P.,
RA Rudnicki M.A., Beier D.R., Spiegelman B.M.;
RT "PRDM16 controls a brown fat/skeletal muscle switch.";
RL Nature 454:961-967(2008).
RN [13]
RP INTERACTION WITH FOXO1.
RX PubMed=19037106; DOI=10.1091/mbc.e08-06-0647;
RA Wang F., Tong Q.;
RT "SIRT2 suppresses adipocyte differentiation by deacetylating FOXO1 and
RT enhancing FOXO1's repressive interaction with PPARgamma.";
RL Mol. Biol. Cell 20:801-808(2009).
RN [14]
RP INTERACTION WITH TACC1.
RX PubMed=20078863; DOI=10.1186/1471-2199-11-3;
RA Guyot R., Vincent S., Bertin J., Samarut J., Ravel-Chapuis P.;
RT "The transforming acidic coiled coil (TACC1) protein modulates the
RT transcriptional activity of the nuclear receptors TR and RAR.";
RL BMC Mol. Biol. 11:3-3(2010).
RN [15]
RP FUNCTION IN ADIPOGENESIS, INTERACTION WITH PER2, PHOSPHORYLATION AT
RP SER-112, MUTAGENESIS OF SER-112, AND TISSUE SPECIFICITY.
RX PubMed=21035761; DOI=10.1016/j.cmet.2010.10.005;
RA Grimaldi B., Bellet M.M., Katada S., Astarita G., Hirayama J., Amin R.H.,
RA Granneman J.G., Piomelli D., Leff T., Sassone-Corsi P.;
RT "PER2 controls lipid metabolism by direct regulation of PPARgamma.";
RL Cell Metab. 12:509-520(2010).
RN [16]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH NOCT.
RX PubMed=20498072; DOI=10.1073/pnas.1000788107;
RA Kawai M., Green C.B., Lecka-Czernik B., Douris N., Gilbert M.R., Kojima S.,
RA Ackert-Bicknell C., Garg N., Horowitz M.C., Adamo M.L., Clemmons D.R.,
RA Rosen C.J.;
RT "A circadian-regulated gene, Nocturnin, promotes adipogenesis by
RT stimulating PPAR-gamma nuclear translocation.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:10508-10513(2010).
RN [17]
RP FUNCTION IN ADIPOGENESIS, INTERACTION WITH PPP5C, PHOSPHORYLATION AT
RP SER-112, DEPHOSPHORYLATION AT SER-112, AND MUTAGENESIS OF SER-112.
RX PubMed=21994940; DOI=10.1074/jbc.m111.311662;
RA Hinds T.D. Jr., Stechschulte L.A., Cash H.A., Whisler D., Banerjee A.,
RA Yong W., Khuder S.S., Kaw M.K., Shou W., Najjar S.M., Sanchez E.R.;
RT "Protein phosphatase 5 mediates lipid metabolism through reciprocal control
RT of glucocorticoid receptor and peroxisome proliferator-activated receptor-?
RT (PPAR?).";
RL J. Biol. Chem. 286:42911-42922(2011).
RN [18]
RP GLYCOSYLATION AT THR-84.
RX PubMed=22226965; DOI=10.1016/j.bbrc.2011.12.086;
RA Ji S., Park S.Y., Roth J., Kim H.S., Cho J.W.;
RT "O-GlcNAc modification of PPARgamma reduces its transcriptional activity.";
RL Biochem. Biophys. Res. Commun. 417:1158-1163(2012).
RN [19]
RP FUNCTION, INTERACTION WITH HELZ2 AND THRAP3, AND SUBCELLULAR LOCATION.
RX PubMed=23525231; DOI=10.1210/me.2012-1332;
RA Katano-Toki A., Satoh T., Tomaru T., Yoshino S., Ishizuka T., Ishii S.,
RA Ozawa A., Shibusawa N., Tsuchiya T., Saito T., Shimizu H., Hashimoto K.,
RA Okada S., Yamada M., Mori M.;
RT "THRAP3 interacts with HELZ2 and plays a novel role in adipocyte
RT differentiation.";
RL Mol. Endocrinol. 27:769-780(2013).
RN [20]
RP INTERACTION WITH GPS2.
RX PubMed=25519902; DOI=10.1074/jbc.m114.598797;
RA Guo C., Li Y., Gow C.H., Wong M., Zha J., Yan C., Liu H., Wang Y.,
RA Burris T.P., Zhang J.;
RT "The optimal corepressor function of nuclear receptor corepressor (NCoR)
RT for peroxisome proliferator-activated receptor gamma requires G protein
RT pathway suppressor 2.";
RL J. Biol. Chem. 290:3666-3679(2015).
RN [21]
RP INTERACTION WITH CRY1 AND CRY2.
RX PubMed=28683290; DOI=10.1016/j.cmet.2017.06.002;
RA Jordan S.D., Kriebs A., Vaughan M., Duglan D., Fan W., Henriksson E.,
RA Huber A.L., Papp S.J., Nguyen M., Afetian M., Downes M., Yu R.T.,
RA Kralli A., Evans R.M., Lamia K.A.;
RT "CRY1/2 selectively repress PPARdelta and limit exercise capacity.";
RL Cell Metab. 26:243-255(2017).
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 ARNTL/BMAL1 in the blood
CC vessels (PubMed:19041764). {ECO:0000269|PubMed:18719582,
CC ECO:0000269|PubMed:19041764, ECO:0000269|PubMed:21035761,
CC ECO:0000269|PubMed:21994940, ECO:0000269|PubMed:23525231}.
CC -!- ACTIVITY REGULATION: PDPK1 activates its transcriptional activity
CC independently of its kinase activity. {ECO:0000250|UniProtKB:P37231}.
CC -!- SUBUNIT: Heterodimer with other nuclear receptors, such as RXRA. The
CC heterodimer with the retinoic acid receptor RXRA is called adipocyte-
CC specific transcription factor ARF6. Interacts with NCOA6 coactivator,
CC leading to a strong increase in transcription of target genes.
CC Interacts with coactivator PPARBP, leading to a mild increase in
CC transcription of target genes. Interacts with NOCA7 in a ligand-
CC inducible manner. Interacts with NCOA1 and NCOA2 LXXLL motifs.
CC Interacts with ASXL1, ASXL2, DNTTIP2, FAM120B, MAP2K1/MEK1, NR0B2,
CC PDPK1, PRDM16, PRMT2 and TGFB1I1. Interacts (when activated by agonist)
CC with PPP5C. Interacts with HELZ2 and THRAP3; the interaction stimulates
CC the transcriptional activity of PPARG. Interacts with PER2, the
CC interaction is ligand dependent and blocks PPARG recruitment to target
CC promoters. Interacts with NOCT. Interacts with FOXO1 (acetylated form).
CC Interacts with ACTN4 (By similarity). Interacts (when in the liganded
CC conformation) with GPS2 (PubMed:25519902). Interacts with CRY1 and CRY2
CC in a ligand-dependent manner (PubMed:28683290). In the absence of
CC hormonal ligand, interacts with TACC1 (PubMed:20078863).
CC {ECO:0000250|UniProtKB:P37231, ECO:0000269|PubMed:10788465,
CC ECO:0000269|PubMed:15687259, ECO:0000269|PubMed:17595322,
CC ECO:0000269|PubMed:18719582, ECO:0000269|PubMed:19037106,
CC ECO:0000269|PubMed:20078863, ECO:0000269|PubMed:20498072,
CC ECO:0000269|PubMed:21035761, ECO:0000269|PubMed:21994940,
CC ECO:0000269|PubMed:23525231, ECO:0000269|PubMed:25519902,
CC ECO:0000269|PubMed:28683290, ECO:0000269|PubMed:7838715,
CC ECO:0000269|PubMed:7926726, ECO:0000269|PubMed:9325263}.
CC -!- INTERACTION:
CC P37238; P97431: Irf6; NbExp=2; IntAct=EBI-5260705, EBI-21183505;
CC P37238; Q923E4: Sirt1; NbExp=2; IntAct=EBI-5260705, EBI-1802585;
CC P37238; Q96EB6: SIRT1; Xeno; NbExp=3; IntAct=EBI-5260705, EBI-1802965;
CC P37238-1; Q96EB6: SIRT1; Xeno; NbExp=2; IntAct=EBI-6267861, EBI-1802965;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407,
CC ECO:0000269|PubMed:20498072, ECO:0000269|PubMed:23525231}. Cytoplasm
CC {ECO:0000250}. Note=Redistributed from the nucleus to the cytosol
CC through a MAP2K1/MEK1-dependent manner (By similarity). NOCT enhances
CC its nuclear translocation. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=P37238-1; Sequence=Displayed;
CC Name=1;
CC IsoId=P37238-2; Sequence=VSP_003647;
CC -!- TISSUE SPECIFICITY: Highest expression in white and brown adipose
CC tissue. Also found in liver, skeletal muscle, heart, adrenal gland,
CC spleen, kidney and intestine. Isoform 2 is more abundant than isoform 1
CC in adipose tissue. {ECO:0000269|PubMed:21035761,
CC ECO:0000269|PubMed:7838715}.
CC -!- DEVELOPMENTAL STAGE: It appears first at 13.5 dpc and increases until
CC birth.
CC -!- INDUCTION: Expressed in a circadian manner in the aorta.
CC {ECO:0000269|PubMed:19041764}.
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: O-GlcNAcylation at Thr-84 reduces transcriptional activity in
CC adipocytes. {ECO:0000269|PubMed:22226965}.
CC -!- PTM: Phosphorylated in basal conditions and dephosphorylated when
CC treated with the ligand. May be dephosphorylated by PPP5C. The
CC phosphorylated Ser-112 form is recognized by PER2 and repressed,
CC dephosphorylation at Ser-112 induces adipogenic activity. Ser-112
CC phosphorylation levels are reduced by 65% in brown adipose tissue
CC compared to white adipose tissue. {ECO:0000269|PubMed:21035761,
CC ECO:0000269|PubMed:21994940}.
CC -!- DISRUPTION PHENOTYPE: Mice develop abnormalities in circadian
CC variations in blood pressure and heart rate, in parallel with a
CC reduction of diurnal variations in the sympathetic nerve activity, and
CC impaired rhythmicity of ARNTL/BMAL1 in the blood vessels.
CC {ECO:0000269|PubMed:19041764}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily. {ECO:0000305}.
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DR EMBL; U09138; AAA62277.1; -; mRNA.
DR EMBL; U01664; AAA62110.1; -; mRNA.
DR EMBL; U01841; AAC52134.1; -; mRNA.
DR EMBL; U10374; AAA19971.1; -; mRNA.
DR CCDS; CCDS20439.1; -. [P37238-1]
DR CCDS; CCDS51876.1; -. [P37238-2]
DR PIR; A54101; A54101.
DR RefSeq; NP_001120802.1; NM_001127330.2.
DR RefSeq; NP_001295281.1; NM_001308352.1.
DR RefSeq; NP_001295283.1; NM_001308354.1.
DR RefSeq; NP_035276.2; NM_011146.3.
DR RefSeq; XP_006505806.1; XM_006505743.3.
DR RefSeq; XP_011239554.1; XM_011241252.1.
DR RefSeq; XP_017176944.1; XM_017321455.1.
DR AlphaFoldDB; P37238; -.
DR SMR; P37238; -.
DR BioGRID; 202320; 82.
DR ComplexPortal; CPX-703; PPARgamma-NCOA2 activated nuclear receptor complex.
DR ComplexPortal; CPX-864; PPARgamma-NCOA1 activated nuclear receptor complex.
DR CORUM; P37238; -.
DR DIP; DIP-60435N; -.
DR ELM; P37238; -.
DR IntAct; P37238; 8.
DR STRING; 10090.ENSMUSP00000000450; -.
DR BindingDB; P37238; -.
DR ChEMBL; CHEMBL2459; -.
DR DrugCentral; P37238; -.
DR SwissLipids; SLP:000001625; -.
DR GlyGen; P37238; 1 site.
DR iPTMnet; P37238; -.
DR PhosphoSitePlus; P37238; -.
DR PaxDb; P37238; -.
DR PRIDE; P37238; -.
DR ProteomicsDB; 289874; -. [P37238-1]
DR ProteomicsDB; 289875; -. [P37238-2]
DR DNASU; 19016; -.
DR GeneID; 19016; -.
DR KEGG; mmu:19016; -.
DR CTD; 5468; -.
DR MGI; MGI:97747; Pparg.
DR eggNOG; KOG3575; Eukaryota.
DR InParanoid; P37238; -.
DR OrthoDB; 1240230at2759; -.
DR PhylomeDB; P37238; -.
DR Reactome; R-MMU-381340; Transcriptional regulation of white adipocyte differentiation.
DR Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
DR BioGRID-ORCS; 19016; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Pparg; mouse.
DR PRO; PR:P37238; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P37238; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0051393; F:alpha-actinin binding; ISO:MGI.
DR GO; GO:0050544; F:arachidonic acid binding; IDA:BHF-UCL.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0050692; F:DNA binding domain binding; ISO:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
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:MGI.
DR GO; GO:0070888; F:E-box binding; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0050693; F:LBD domain binding; ISO:MGI.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISO:MGI.
DR GO; GO:0004879; F:nuclear receptor activity; IDA:GO_Central.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IDA:UniProtKB.
DR GO; GO:0046965; F:nuclear retinoid X receptor binding; ISO:MGI.
DR GO; GO:0042277; F:peptide binding; ISO:MGI.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0043621; F:protein self-association; ISO:MGI.
DR GO; GO:0070412; F:R-SMAD binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0097677; F:STAT family protein binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0001221; F:transcription coregulator binding; ISO:MGI.
DR GO; GO:0050699; F:WW domain binding; IMP:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0030509; P:BMP signaling pathway; ISO:MGI.
DR GO; GO:0050873; P:brown fat cell differentiation; IDA:MGI.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0045165; P:cell fate commitment; IMP:MGI.
DR GO; GO:0048469; P:cell maturation; ISO:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0071456; P:cellular response to hypoxia; ISO:MGI.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IMP:MGI.
DR GO; GO:0071285; P:cellular response to lithium ion; IDA:MGI.
DR GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; ISO:MGI.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IMP:BHF-UCL.
DR GO; GO:0106106; P:cold-induced thermogenesis; IMP:MGI.
DR GO; GO:0002024; P:diet induced thermogenesis; IMP:MGI.
DR GO; GO:0030855; P:epithelial cell differentiation; IGI:MGI.
DR GO; GO:0050673; P:epithelial cell proliferation; IMP:MGI.
DR GO; GO:0045444; P:fat cell differentiation; IDA:MGI.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0019395; P:fatty acid oxidation; ISO:MGI.
DR GO; GO:0042593; P:glucose homeostasis; ISO:MGI.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; TAS:MGI.
DR GO; GO:0042953; P:lipoprotein transport; ISO:MGI.
DR GO; GO:0015909; P:long-chain fatty acid transport; IMP:MGI.
DR GO; GO:0010742; P:macrophage derived foam cell differentiation; ISS:UniProtKB.
DR GO; GO:0030224; P:monocyte differentiation; ISO:MGI.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0002674; P:negative regulation of acute inflammatory response; ISO:MGI.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:MGI.
DR GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; ISO:MGI.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISO:MGI.
DR GO; GO:1903243; P:negative regulation of cardiac muscle hypertrophy in response to stress; ISO:MGI.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:1900077; P:negative regulation of cellular response to insulin stimulus; IMP:BHF-UCL.
DR GO; GO:1903845; P:negative regulation of cellular response to transforming growth factor beta stimulus; ISO:MGI.
DR GO; GO:0010887; P:negative regulation of cholesterol storage; ISO:MGI.
DR GO; GO:0032966; P:negative regulation of collagen biosynthetic process; ISO:MGI.
DR GO; GO:1904597; P:negative regulation of connective tissue replacement involved in inflammatory response wound healing; ISO:MGI.
DR GO; GO:0001818; P:negative regulation of cytokine production; IMP:BHF-UCL.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:BHF-UCL.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IBA:GO_Central.
DR GO; GO:0060336; P:negative regulation of interferon-gamma-mediated signaling pathway; ISO:MGI.
DR GO; GO:0010888; P:negative regulation of lipid storage; IMP:BHF-UCL.
DR GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; ISO:MGI.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; ISO:MGI.
DR GO; GO:1903979; P:negative regulation of microglial cell activation; IGI:ARUK-UCL.
DR GO; GO:1902894; P:negative regulation of miRNA transcription; ISO:MGI.
DR GO; GO:0060965; P:negative regulation of miRNA-mediated gene silencing; ISO:MGI.
DR GO; GO:0090258; P:negative regulation of mitochondrial fission; ISO:MGI.
DR GO; GO:0150079; P:negative regulation of neuroinflammatory response; IGI:ARUK-UCL.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISO:MGI.
DR GO; GO:2000230; P:negative regulation of pancreatic stellate cell proliferation; ISO:MGI.
DR GO; GO:0060394; P:negative regulation of pathway-restricted SMAD protein phosphorylation; ISO:MGI.
DR GO; GO:0090278; P:negative regulation of peptide hormone secretion; IMP:BHF-UCL.
DR GO; GO:1904893; P:negative regulation of receptor signaling pathway via STAT; ISO:MGI.
DR GO; GO:0010891; P:negative regulation of sequestering of triglyceride; ISO:MGI.
DR GO; GO:2000272; P:negative regulation of signaling receptor activity; ISO:MGI.
DR GO; GO:0060392; P:negative regulation of SMAD protein signal transduction; ISO:MGI.
DR GO; GO:0014912; P:negative regulation of smooth muscle cell migration; IDA:BHF-UCL.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IDA:BHF-UCL.
DR GO; GO:0051974; P:negative regulation of telomerase activity; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:1905563; P:negative regulation of vascular endothelial cell proliferation; ISO:MGI.
DR GO; GO:0035357; P:peroxisome proliferator activated receptor signaling pathway; IPI:MGI.
DR GO; GO:0001890; P:placenta development; IMP:MGI.
DR GO; GO:0070165; P:positive regulation of adiponectin secretion; ISO:MGI.
DR GO; GO:1904179; P:positive regulation of adipose tissue development; IMP:ARUK-UCL.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; ISO:MGI.
DR GO; GO:0043388; P:positive regulation of DNA binding; ISO:MGI.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; IDA:UniProtKB.
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; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IGI:BHF-UCL.
DR GO; GO:1905599; P:positive regulation of low-density lipoprotein receptor activity; ISO:MGI.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:MGI.
DR GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; ISO:MGI.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IGI:BHF-UCL.
DR GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; ISO:MGI.
DR GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; IGI:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0061411; P:positive regulation of transcription from RNA polymerase II promoter in response to cold; IMP:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:1905461; P:positive regulation of vascular associated smooth muscle cell apoptotic process; ISO:MGI.
DR GO; GO:0008217; P:regulation of blood pressure; ISO:MGI.
DR GO; GO:1900076; P:regulation of cellular response to insulin stimulus; IC:ComplexPortal.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:0045598; P:regulation of fat cell differentiation; ISO:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0019216; P:regulation of lipid metabolic process; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0002021; P:response to dietary excess; IDA:MGI.
DR GO; GO:0032094; P:response to food; IDA:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IDA:UniProtKB.
DR GO; GO:0033993; P:response to lipid; IDA:BHF-UCL.
DR GO; GO:0048384; P:retinoic acid receptor signaling pathway; IDA:GO_Central.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; ISO:MGI.
DR GO; GO:0050872; P:white fat cell differentiation; IDA:MGI.
DR GO; GO:0002246; P:wound healing involved in inflammatory response; IDA:BHF-UCL.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 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 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; 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 Activator; Alternative splicing; Biological rhythms; Cytoplasm;
KW Direct protein sequencing; DNA-binding; Glycoprotein; Metal-binding;
KW Nucleus; Phosphoprotein; Receptor; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..505
FT /note="Peroxisome proliferator-activated receptor gamma"
FT /id="PRO_0000053494"
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:0000269|PubMed:17595322"
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:21035761,
FT ECO:0000269|PubMed:21994940"
FT CARBOHYD 84
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000269|PubMed:22226965"
FT VAR_SEQ 1..30
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:8041794,
FT ECO:0000303|PubMed:8240342, ECO:0000303|PubMed:8262913"
FT /id="VSP_003647"
FT MUTAGEN 112
FT /note="S->A: Increases basal and ligand-induced adipogenic
FT activity. Abolishes repression by PER2 on transactivation
FT activity."
FT /evidence="ECO:0000269|PubMed:21035761,
FT ECO:0000269|PubMed:21994940"
FT MUTAGEN 112
FT /note="S->D: No effect on repression by PER2 on
FT transactivation activity."
FT /evidence="ECO:0000269|PubMed:21035761,
FT ECO:0000269|PubMed:21994940"
FT CONFLICT 213..214
FT /note="MP -> DR (in Ref. 2; AAA62110)"
FT /evidence="ECO:0000305"
FT CONFLICT 281..283
FT /note="NSL -> SSF (in Ref. 2; AAA62110)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="N -> S (in Ref. 2; AAA62110 and 4; AAA19971)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="L -> F (in Ref. 2; AAA62110)"
FT /evidence="ECO:0000305"
SQ 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
