ID PPARG_MACMU Reviewed; 505 AA.
AC O18924; Q9TQW6;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-APR-2013, entry version 109.
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 Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Adipose tissue;
RX PubMed=9806316; DOI=10.1038/sj.ijo.0800718;
RA Hotta K., Gustafson T.A., Yoshioka S., Ortmeyer H.K., Bodkin N.L.,
RA Hansen B.C.;
RT "Relationships of PPARgamma and PPARgamma2 mRNA levels to obesity,
RT diabetes and hyperinsulinaemia in rhesus monkeys.";
RL Int. J. Obes. Relat. Metab. Disord. 22:1000-1010(1998).
CC -!- FUNCTION: Receptor that binds peroxisome proliferators such as
CC hypolipidemic drugs and fatty acids. Once activated by a ligand,
CC the receptor binds to a promoter element in the gene for acyl-CoA
CC oxidase and activates its transcription. It therefore controls the
CC peroxisomal beta-oxidation pathway of fatty acids. Key regulator
CC of adipocyte differentiation and glucose homeostasis. Acts as a
CC critical regulator of gut homeostasis by suppressing NF-kappa-B-
CC mediated proinflammatory responses (By similarity).
CC -!- ENZYME REGULATION: PDPK1 activates its transcriptional activity
CC independently of its kinase activity (By similarity).
CC -!- SUBUNIT: Heterodimer with other nuclear receptors, such as RXRA.
CC The heterodimer with the retinoic acid receptor RXRA is called
CC adipocyte-specific transcription factor ARF6. Interacts with NCOA6
CC coactivator, leading to a strong increase in transcription of
CC target genes. Interacts with coactivator PPARBP, leading to a mild
CC increase in transcription of target genes. Interacts with NOCA7 in
CC a ligand-inducible manner. Interacts with NCOA1 and NCOA2 LXXLL
CC motifs. Interacts with ASXL1, ASXL2, DNTTIP2, FAM120B,
CC MAP2K1/MEK1, NR0B2, PDPK1, PRDM16, PRMT2 and TGFB1I1. Interacts
CC (via DNA-binding domain) with HELZ2; the interaction stimulates
CC the transcriptional activity of PPARG (By similarity).
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By
CC similarity). Note=Redistributed from the nucleus to the cytosol
CC through a MAP2K1/MEK1-dependent manner (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist;
CC Name=2;
CC IsoId=O18924-1; Sequence=Displayed;
CC Name=1;
CC IsoId=O18924-2; Sequence=VSP_003646;
CC -!- TISSUE SPECIFICITY: Highest expression in adipose tissue. Lower in
CC liver, heart, kidney, stomach, duodenum and colon.
CC -!- PTM: O-GlcNAcylation at Thr-84 reduces transcriptional activity in
CC adipocytes (By similarity).
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily.
CC -!- SIMILARITY: Contains 1 nuclear receptor DNA-binding domain.
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DR EMBL; AF033103; AAB87480.1; -; mRNA.
DR EMBL; AF033343; AAB87482.1; -; mRNA.
DR EMBL; AF033342; AAB87481.1; -; mRNA.
DR RefSeq; NP_001028032.1; NM_001032860.1.
DR UniGene; Mmu.3422; -.
DR ProteinModelPortal; O18924; -.
DR SMR; O18924; 131-216, 234-505.
DR MINT; MINT-138526; -.
DR STRING; 9544.ENSMMUP00000009427; -.
DR GeneID; 574190; -.
DR KEGG; mcc:574190; -.
DR CTD; 5468; -.
DR eggNOG; NOG266867; -.
DR HOGENOM; HOG000261626; -.
DR HOVERGEN; HBG106004; -.
DR InParanoid; O18924; -.
DR KO; K08530; -.
DR OrthoDB; EOG41ZF9W; -.
DR NextBio; 19981584; -.
DR GO; GO:0005829; C:cytosol; IEA:Compara.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; IEA:Compara.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0008144; F:drug binding; IEA:Compara.
DR GO; GO:0004879; F:ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity; IEA:InterPro.
DR GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0001012; F:RNA polymerase II regulatory region DNA binding; IEA:Compara.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0003707; F:steroid hormone receptor activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Compara.
DR GO; GO:0050873; P:brown fat cell differentiation; IEA:Compara.
DR GO; GO:0045165; P:cell fate commitment; IEA:Compara.
DR GO; GO:0048469; P:cell maturation; IEA:Compara.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Compara.
DR GO; GO:0071285; P:cellular response to lithium ion; IEA:Compara.
DR GO; GO:0030855; P:epithelial cell differentiation; IEA:Compara.
DR GO; GO:0042593; P:glucose homeostasis; IEA:Compara.
DR GO; GO:0006917; P:induction of apoptosis; IEA:Compara.
DR GO; GO:0042953; P:lipoprotein transport; IEA:Compara.
DR GO; GO:0015909; P:long-chain fatty acid transport; IEA:Compara.
DR GO; GO:0045713; P:low-density lipoprotein particle receptor biosynthetic process; IEA:Compara.
DR GO; GO:0030224; P:monocyte differentiation; IEA:Compara.
DR GO; GO:0010887; P:negative regulation of cholesterol storage; IEA:Compara.
DR GO; GO:0060336; P:negative regulation of interferon-gamma-mediated signaling pathway; IEA:Compara.
DR GO; GO:0010871; P:negative regulation of receptor biosynthetic process; IEA:Compara.
DR GO; GO:0010891; P:negative regulation of sequestering of triglyceride; IEA:Compara.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IEA:Compara.
DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Compara.
DR GO; GO:0035357; P:peroxisome proliferator activated receptor signaling pathway; IEA:Compara.
DR GO; GO:0001890; P:placenta development; IEA:Compara.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:HGNC.
DR GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IEA:Compara.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
DR GO; GO:0008217; P:regulation of blood pressure; IEA:Compara.
DR GO; GO:0055098; P:response to low-density lipoprotein particle stimulus; IEA:Compara.
DR GO; GO:0032526; P:response to retinoic acid; ISS:UniProtKB.
DR GO; GO:0050872; P:white fat cell differentiation; ISS:HGNC.
DR Gene3D; 1.10.565.10; -; 2.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR003074; 1Cnucl_rcpt.
DR InterPro; IPR003077; 1Cnucl_rcpt_G.
DR InterPro; IPR008946; Nucl_hormone_rcpt_ligand-bd.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd_core.
DR InterPro; IPR022590; PPARgamma_N.
DR InterPro; IPR001723; Str_hrmn_rcpt.
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; Str_ncl_receptor; 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; Alternative splicing; Complete proteome; Cytoplasm;
KW DNA-binding; Glycoprotein; Metal-binding; Nucleus; Phosphoprotein;
KW Receptor; Reference proteome; Transcription; Transcription regulation;
KW Zinc; Zinc-finger.
FT CHAIN 1 505 Peroxisome proliferator-activated
FT receptor gamma.
FT /FTId=PRO_0000053493.
FT DNA_BIND 136 210 Nuclear receptor.
FT ZN_FING 139 159 NR C4-type.
FT ZN_FING 176 198 NR C4-type.
FT REGION 205 280 Interaction with FAM120B (By similarity).
FT REGION 317 505 Ligand-binding (By similarity).
FT MOD_RES 112 112 Phosphoserine; by MAPK (By similarity).
FT CARBOHYD 84 84 O-linked (GlcNAc...) (By similarity).
FT VAR_SEQ 1 30 Missing (in isoform 1).
FT /FTId=VSP_003646.
SQ SEQUENCE 505 AA; 57590 MW; 41836A624AAF6942 CRC64;
MGETLGDSPI DPESDSFTDT LSANISQEIT MVDTEMPFWP TNFGISSVDL SVMDDHSHSF
DIKPFTTVDF SSISAPHYED IPFTRTDPMV ADYKYDLKLQ EYQSAIKVEP ASPPYYSEKT
QLYNKPHEEP SNSLMAIECR VCGDKASGFH YGVHACEGCK GFFRRTIRLK LIYDRCDLNC
RIHKKSRNKC QYCRFQKCLA VGMSHNAIRF GRMPQAEKEK LLAEISSDID QLNPESADLR
ALAKHLYDSY IKSFPLTKAK ARAILTGKTT DKSPFVIYDM NSLMMGEDKI KFKHITPLQE
QSKEVAIRIF QGCQFRSVEA VQEITEYAKS IPGFVNLDLN DQVTLLKYGV HEIIYTMLAS
LMNKDGVLIS EGQGFMTREF LKSLRKPFGD FMEPKFEFAV KFNALELDDS DLAIFIAVII
LSGDRPGLLN VKPIEDIQDN LLQALELQLK LNHPESSQLF AKLLQKMTDL RQIVTEHVQL
LQVIKKTETD MSLHPLLQEI YKDLY
//
