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Peroxisome proliferator-activated receptor gamma (PPAR-gamma) (Nuclear receptor subfamily 1 group C member 3)

 PPARG_MACMU             Reviewed;         505 AA.
O18924; Q9TQW6;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
23-MAY-2018, entry version 149.
RecName: Full=Peroxisome proliferator-activated receptor gamma;
Short=PPAR-gamma;
AltName: Full=Nuclear receptor subfamily 1 group C member 3;
Name=PPARG; Synonyms=NR1C3;
Macaca mulatta (Rhesus macaque).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
NCBI_TaxID=9544;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Adipose tissue;
PubMed=9806316; DOI=10.1038/sj.ijo.0800718;
Hotta K., Gustafson T.A., Yoshioka S., Ortmeyer H.K., Bodkin N.L.,
Hansen B.C.;
"Relationships of PPARgamma and PPARgamma2 mRNA levels to obesity,
diabetes and hyperinsulinaemia in rhesus monkeys.";
Int. J. Obes. Relat. Metab. Disord. 22:1000-1010(1998).
-!- FUNCTION: Nuclear receptor that binds peroxisome proliferators
such as hypolipidemic drugs and fatty acids. Once activated by a
ligand, the nuclear receptor binds to DNA specific PPAR response
elements (PPRE) and modulates the transcription of its target
genes, such as acyl-CoA oxidase. It therefore controls the
peroxisomal beta-oxidation pathway of fatty acids. Key regulator
of adipocyte differentiation and glucose homeostasis. ARF6 acts as
a key regulator of the tissue-specific adipocyte P2 (aP2)
enhancer. Acts as a critical regulator of gut homeostasis by
suppressing NF-kappa-B-mediated proinflammatory responses. Plays a
role in the regulation of cardiovascular circadian rhythms by
regulating the transcription of ARNTL/BMAL1 in the blood vessels.
{ECO:0000250|UniProtKB:P37231, ECO:0000250|UniProtKB:P37238}.
-!- ENZYME REGULATION: PDPK1 activates its transcriptional activity
independently of its kinase activity. {ECO:0000250}.
-!- SUBUNIT: Interacts with FOXO1 (acetylated form) (By similarity).
Heterodimer with other nuclear receptors, such as RXRA. The
heterodimer with the retinoic acid receptor RXRA is called
adipocyte-specific transcription factor ARF6. Interacts with NCOA6
coactivator, leading to a strong increase in transcription of
target genes. Interacts with coactivator PPARBP, leading to a mild
increase in transcription of target genes. Interacts with NOCA7 in
a ligand-inducible manner. Interacts with NCOA1 and NCOA2 LXXLL
motifs. Interacts with ASXL1, ASXL2, DNTTIP2, FAM120B,
MAP2K1/MEK1, NR0B2, PDPK1, PRDM16, PRMT2 and TGFB1I1. Interacts
(when activated by agonist) with PPP5C. Interacts with HELZ2 and
THRAP3; the interaction stimulates the transcriptional activity of
PPARG. Interacts with PER2, the interaction is ligand dependent
and blocks PPARG recruitment to target promoters. Interacts with
NOCT. Interacts with ACTN4. Interacts (when in the liganded
conformation) with GPS2 (By similarity).
{ECO:0000250|UniProtKB:P37231, ECO:0000250|UniProtKB:P37238}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00407}. Cytoplasm {ECO:0000250}. Note=Redistributed
from the nucleus to the cytosol through a MAP2K1/MEK1-dependent
manner. NOCT enhances its nuclear translocation (By similarity).
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=Additional isoforms seem to exist.;
Name=2;
IsoId=O18924-1; Sequence=Displayed;
Name=1;
IsoId=O18924-2; Sequence=VSP_003646;
-!- TISSUE SPECIFICITY: Highest expression in adipose tissue. Lower in
liver, heart, kidney, stomach, duodenum and colon.
-!- PTM: O-GlcNAcylation at Thr-84 reduces transcriptional activity in
adipocytes. {ECO:0000250|UniProtKB:P37238}.
-!- PTM: Phosphorylated at basal conditions and dephosphorylated when
treated with the ligand. May be dephosphorylated by PPP5C. The
phosphorylated form may be inactive and dephosphorylation induces
adipogenic activity (By similarity).
{ECO:0000250|UniProtKB:P37231}.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF033103; AAB87480.1; -; mRNA.
EMBL; AF033343; AAB87482.1; -; mRNA.
EMBL; AF033342; AAB87481.1; -; mRNA.
RefSeq; NP_001028032.1; NM_001032860.1. [O18924-1]
RefSeq; XP_014985685.1; XM_015130199.1. [O18924-2]
RefSeq; XP_014985686.1; XM_015130200.1. [O18924-2]
RefSeq; XP_014985687.1; XM_015130201.1. [O18924-2]
RefSeq; XP_014985688.1; XM_015130202.1. [O18924-2]
UniGene; Mmu.3422; -.
ProteinModelPortal; O18924; -.
SMR; O18924; -.
MINT; O18924; -.
STRING; 9544.ENSMMUP00000009427; -.
PRIDE; O18924; -.
GeneID; 574190; -.
KEGG; mcc:574190; -.
CTD; 5468; -.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
HOGENOM; HOG000261626; -.
HOVERGEN; HBG106004; -.
InParanoid; O18924; -.
KO; K08530; -.
Proteomes; UP000006718; Unplaced.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0001046; F:core promoter sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:0003700; F:DNA binding transcription factor activity; ISS:UniProtKB.
GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; ISS:UniProtKB.
GO; GO:0004879; F:nuclear receptor activity; IEA:InterPro.
GO; GO:0003707; F:steroid hormone receptor activity; IEA:InterPro.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0010742; P:macrophage derived foam cell differentiation; ISS:UniProtKB.
GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:HGNC.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
GO; GO:0060850; P:regulation of transcription involved in cell fate commitment; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0032526; P:response to retinoic acid; ISS:UniProtKB.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0050872; P:white fat cell differentiation; ISS:HGNC.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR003074; 1Cnucl_rcpt.
InterPro; IPR035500; NHR_like_dom_sf.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
InterPro; IPR003077; PPAR-gamma.
InterPro; IPR022590; PPARgamma_N.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF12577; PPARgamma_N; 1.
Pfam; PF00105; zf-C4; 1.
PRINTS; PR01288; PROXISOMEPAR.
PRINTS; PR01291; PROXISOMPAGR.
PRINTS; PR00398; STRDHORMONER.
PRINTS; PR00047; STROIDFINGER.
SMART; SM00430; HOLI; 1.
SMART; SM00399; ZnF_C4; 1.
SUPFAM; SSF48508; SSF48508; 1.
PROSITE; PS51843; NR_LBD; 1.
PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
2: Evidence at transcript level;
Activator; Alternative splicing; Biological rhythms;
Complete proteome; Cytoplasm; DNA-binding; Glycoprotein;
Metal-binding; Nucleus; Phosphoprotein; Receptor; Reference proteome;
Transcription; Transcription regulation; Zinc; Zinc-finger.
CHAIN 1 505 Peroxisome proliferator-activated
receptor gamma.
/FTId=PRO_0000053493.
DOMAIN 238 503 NR LBD. {ECO:0000255|PROSITE-
ProRule:PRU01189}.
DNA_BIND 136 210 Nuclear receptor. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 139 159 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 176 198 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
REGION 205 280 Interaction with FAM120B. {ECO:0000250}.
MOD_RES 112 112 Phosphoserine; by MAPK.
{ECO:0000250|UniProtKB:P37238}.
CARBOHYD 84 84 O-linked (GlcNAc) threonine.
{ECO:0000250}.
VAR_SEQ 1 30 Missing (in isoform 1).
{ECO:0000303|PubMed:9806316}.
/FTId=VSP_003646.
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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