PPARG_CRIGR
ID PPARG_CRIGR Reviewed; 475 AA.
AC P57797;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
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 Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=7557447; DOI=10.1016/0378-1119(95)00196-d;
RA Aperlo C., Pognonec P., Saladin R., Auwerx J., Boulukos K.E.;
RT "cDNA cloning and characterization of the transcriptional activities of the
RT hamster peroxisome proliferator-activated receptor haPPAR gamma.";
RL Gene 162:297-302(1995).
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. {ECO:0000250|UniProtKB:P37231, ECO:0000250|UniProtKB:P37238}.
CC -!- ACTIVITY REGULATION: PDPK1 activates its transcriptional activity
CC independently of its kinase activity. Interacts with HELZ2 and THRAP3;
CC the interaction enhances the transcriptional activity of PPARG (By
CC similarity). {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 -!- 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-54 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 induces
CC adipogenic activity (By similarity). {ECO:0000250|UniProtKB:P37231}.
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; Z30972; CAA83219.1; -; mRNA.
DR PIR; JC4264; JC4264.
DR RefSeq; NP_001231210.1; NM_001244281.1.
DR AlphaFoldDB; P57797; -.
DR SMR; P57797; -.
DR STRING; 10029.NP_001231210.1; -.
DR Ensembl; ENSCGRT00001016677; ENSCGRP00001012443; ENSCGRG00001013849.
DR GeneID; 100689245; -.
DR KEGG; cge:100689245; -.
DR CTD; 5468; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000158273; -.
DR OrthoDB; 1240230at2759; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
DR GO; GO:0004879; F:nuclear receptor activity; ISS:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0010742; P:macrophage derived foam cell differentiation; ISS:UniProtKB.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0048583; P:regulation of response to stimulus; IEA:UniProt.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0048384; P:retinoic acid receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Activator; Biological rhythms; Cytoplasm; DNA-binding; Glycoprotein;
KW Metal-binding; Nucleus; Phosphoprotein; Receptor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..475
FT /note="Peroxisome proliferator-activated receptor gamma"
FT /id="PRO_0000053491"
FT DOMAIN 208..473
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 106..180
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 109..129
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 146..168
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 175..250
FT /note="Interaction with FAM120B"
FT /evidence="ECO:0000250"
FT MOTIF 465..473
FT /note="9aaTAD"
FT /evidence="ECO:0000250|UniProtKB:P37231"
FT MOD_RES 82
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000250|UniProtKB:P37238"
FT CARBOHYD 54
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 475 AA; 54473 MW; BBDCA0704F837ADB CRC64;
MVDTEMPFWP TNFGISSVDL SMMDDHSHSF DIKPFTTVDF SSISAPHYED IPFTRADPMV
ADYKYDLKLQ EYQSAIKVEP ASPPYYSEKA 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
