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Database: UniProt
Entry: O18924
LinkDB: O18924
Original site: O18924 
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   01-OCT-2014, entry version 118.
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: Nuclear receptor that binds peroxisome proliferators
CC       such as hypolipidemic drugs and fatty acids. Once activated by a
CC       ligand, the nuclear receptor binds to DNA specific PPAR response
CC       elements (PPRE) and modulates the transcription of its target
CC       genes, such as acyl-CoA oxidase. It therefore controls the
CC       peroxisomal beta-oxidation pathway of fatty acids. Key regulator
CC       of adipocyte differentiation and glucose homeostasis. ARF6 acts as
CC       a key regulator of the tissue-specific adipocyte P2 (aP2)
CC       enhancer. Acts as a critical regulator of gut homeostasis by
CC       suppressing NF-kappa-B-mediated proinflammatory responses (By
CC       similarity). {ECO:0000250}.
CC   -!- ENZYME REGULATION: PDPK1 activates its transcriptional activity
CC       independently of its kinase activity. {ECO:0000250}.
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       (when activated by agonist) with PPP5C. Interacts with HELZ2 and
CC       THRAP3; the interaction stimulates the transcriptional activity of
CC       PPARG. Interacts with PER2, the interaction is ligand dependent
CC       and blocks PPARG recruitment to target promoters. Interacts with
CC       CCRN4L/NOC. Interacts with FOXO1 (acetylated form) (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
CC       ProRule:PRU00407}. Cytoplasm {ECO:0000250}. Note=Redistributed
CC       from the nucleus to the cytosol through a MAP2K1/MEK1-dependent
CC       manner. CCRN4L/NOC enhances its nuclear translocation (By
CC       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=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. {ECO:0000250}.
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}.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC       subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 nuclear receptor DNA-binding domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00407}.
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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. [O18924-1]
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   NextBio; 19981584; -.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0008144; F:drug binding; IEA:Ensembl.
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:Ensembl.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0003707; F:steroid hormone receptor activity; IEA:InterPro.
DR   GO; GO:0044212; F:transcription regulatory region DNA binding; ISS:UniProtKB.
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:Ensembl.
DR   GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0045165; P:cell fate commitment; IEA:Ensembl.
DR   GO; GO:0048469; P:cell maturation; IEA:Ensembl.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
DR   GO; GO:0071285; P:cellular response to lithium ion; IEA:Ensembl.
DR   GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
DR   GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR   GO; GO:0042953; P:lipoprotein transport; IEA:Ensembl.
DR   GO; GO:0015909; P:long-chain fatty acid transport; IEA:Ensembl.
DR   GO; GO:0045713; P:low-density lipoprotein particle receptor biosynthetic process; IEA:Ensembl.
DR   GO; GO:0030224; P:monocyte differentiation; IEA:Ensembl.
DR   GO; GO:0010887; P:negative regulation of cholesterol storage; IEA:Ensembl.
DR   GO; GO:0060336; P:negative regulation of interferon-gamma-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0010871; P:negative regulation of receptor biosynthetic process; IEA:Ensembl.
DR   GO; GO:0010891; P:negative regulation of sequestering of triglyceride; IEA:Ensembl.
DR   GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR   GO; GO:0035357; P:peroxisome proliferator activated receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0001890; P:placenta development; IEA:Ensembl.
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:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
DR   GO; GO:0060850; P:regulation of transcription involved in cell fate commitment; ISS:UniProtKB.
DR   GO; GO:0055098; P:response to low-density lipoprotein particle; IEA:Ensembl.
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; SSF48508; 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. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00407}.
FT   ZN_FING     139    159       NR C4-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00407}.
FT   ZN_FING     176    198       NR C4-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00407}.
FT   REGION      205    280       Interaction with FAM120B. {ECO:0000250}.
FT   REGION      317    505       Ligand-binding. {ECO:0000250}.
FT   MOD_RES     112    112       Phosphoserine; by MAPK. {ECO:0000250}.
FT   CARBOHYD     84     84       O-linked (GlcNAc). {ECO:0000250}.
FT   VAR_SEQ       1     30       Missing (in isoform 1).
FT                                {ECO:0000303|PubMed:9806316}.
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
//
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