Swiss-Prot entry
ID PPAT_RAT STANDARD; PRT; 505 AA.
AC O88275; Q9QWG0; Q9R197;
DT 16-OCT-2001 (Rel. 40, Created)
DT 16-OCT-2001 (Rel. 40, Last sequence update)
DT 01-MAY-2005 (Rel. 47, Last annotation update)
DE Peroxisome proliferator activated receptor gamma (PPAR-gamma).
GN Name=Pparg; Synonyms=Nr1c3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muridae; Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2).
RC STRAIN=Sprague-Dawley; TISSUE=Brown adipose tissue;
RX MEDLINE=99367468; PubMed=10438514 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1074/jbc.274.33.23368;
RA Guardiola-Diaz H.M., Rehnmark S., Usuda N., Albrektsen T.,
RA Feltkamp D., Gustafsson J.-A., Alexson S.E.H.;
RT "Rat peroxisome proliferator-activated receptors and brown adipose
RT tissue function during cold acclimatization.";
RL J. Biol. Chem. 274:23368-23377(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORM 2).
RC STRAIN=Sprague-Dawley; TISSUE=Adipose tissue;
RA Tanaka T., Itoh H.;
RT "Down-regulation of PPAR gammma.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE (ISOFORM 2).
RA Escher P.;
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RC TISSUE=Adipocyte;
RA Miyakita A., Okuno S., Watanabe T.K., Oga K., Tsuji A., Hishigaki H.,
RA Suto T., Nakagawa K., Nakahara Y., Higashi K.;
RT "Molecular cloning of rat PPAR-gamma gene.";
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RC STRAIN=Long Evans;
RX MEDLINE=20259576; PubMed=10797535 [NCBI, ExPASy, EBI, Israel, Japan];
RX DOI=10.1002/(SICI)1097-4547(20000501)60:3<328::AID-JNR7>3.0.CO;2-5;
RA Ershov A.V., Bazan N.G.;
RT "Photoreceptor phagocytosis selectively activates PPARgamma expression
RT in retinal pigment epithelial cells.";
RL J. Neurosci. Res. 60:328-337(2000).
RN [6]
RP PHOSPHORYLATION.
RX MEDLINE=97113205; PubMed=8953045 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1126/science.274.5295.2100;
RA Hu E., Kim J.B., Sarraf P., Spiegelman B.M.;
RT "Inhibition of adipogenesis through MAP kinase-mediated
RT phosphorylation of PPARgamma.";
RL Science 274:2100-2103(1996).
RN [7]
RP PHOSPHORYLATION SITE SER-112, AND MUTAGENESIS OF SER-112.
RX MEDLINE=97184167; PubMed=9030579 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1074/jbc.272.8.5128;
RA Adams M., Reginato M.J., Shao D., Lazar M.A., Chatterjee V.K.;
RT "Transcriptional activation by peroxisome proliferator-activated
RT receptor gamma is inhibited by phosphorylation at a consensus mitogen-
RT activated protein kinase site.";
RL J. Biol. Chem. 272:5128-5132(1997).
RN [8]
RP PHOSPHORYLATION.
RX MEDLINE=97112959; PubMed=8943212 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1074/jbc.271.50.31771;
RA Zhang B., Berger J., Zhou G., Elbrecht A., Biswas S.,
RA White-Carrington S., Szalkowski D., Moller D.E.;
RT "Insulin- and mitogen-activated protein kinase-mediated
RT phosphorylation and activation of peroxisome proliferator-activated
RT receptor gamma.";
RL J. Biol. Chem. 271:31771-31774(1996).
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.
CC -!- SUBUNIT: Forms a heterodimer with the retinoic acid receptor RXR-
CC alpha called adipocyte-specific transcription factor ARF6.
CC Interacts with NCOA6 coactivator, leading to a strong increase in
CC transcription of target genes (By similarity).
CC -!- SUBCELLULAR LOCATION: Nuclear.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist;
CC Name=2;
CC IsoId=O88275-1; Sequence=Displayed;
CC Name=1;
CC IsoId=O88275-2; Sequence=VSP_003649;
CC -!- TISSUE SPECIFICITY: Highest expression in adipose tissue.
CC -!- PTM: Phosphorylated by MAPK. The phosphorylation inhibits PPAR
CC gamma activity.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily.
CC -!- SIMILARITY: Contains 1 nuclear receptor DNA-binding domain.
CC --------------------------------------------------------------------------
CC This Swiss-Prot entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use as long as its content is in no way modified and this statement is not
CC removed.
CC --------------------------------------------------------------------------
DR EMBL; AF156666; AAD40119.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AF156665; AAD40118.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AB019561; BAA36485.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; Y12882; CAA73382.2; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AB011365; BAA32540.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AF246457; AAF63385.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AF246458; AAF63386.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR HSSP; Q96J12; 1NYX. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR SMR; O88275; 234-505.
DR TRANSFAC; T05329; -.
DR TRANSFAC; T05330; -.
DR TRANSFAC; T05331; -.
DR Ensembl; ENSRNOG00000008839; Rattus_norvegicus
DR RGD; 3371; Pparg.
DR GO; GO:0006631; P:fatty acid metabolism; TAS.
DR GO; GO:0045598; P:regulation of adipocyte differentiation; IDA.
DR GO; GO:0006357; P:regulation of transcription from Pol II pro...; IEP.
DR InterPro; IPR000536; Hrmon_recept_lig.
DR InterPro; IPR001723; Stdhrmn_receptor.
DR InterPro; IPR008946; Str_ncl_receptor.
DR InterPro; IPR001628; Znf_C4steroid.
DR InterPro; Graphical view of domain structure.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR Pfam; Graphical view of domain structure.
DR PRINTS; PR01288; PROXISOMEPAR.
DR PRINTS; PR01291; PROXISOMPAGR.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR ProDom; PD000035; Znf_C4steroid; 1.
DR ProDom [Domain structure / List of seq. sharing at least 1 domain ]
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
DR CMR; O88275.
DR HOVERGEN [Family / Alignment / Tree]
DR BLOCKS; O88275.
DR ProtoNet; O88275.
DR ProtoMap; O88275.
DR PRESAGE; O88275.
DR DIP; O88275.
DR ModBase; O88275.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW Activator; Alternative splicing; DNA-binding; Multigene family;
KW Nuclear protein; Phosphorylation; Receptor; Transcription;
KW Transcription regulation; Zinc-finger.
FT DNA_BIND 136 210 Nuclear receptor-type.
FT ZN_FING 139 159 C4-type.
FT ZN_FING 176 198 C4-type.
FT DOMAIN 318 505 Ligand-binding (Potential).
FT MOD_RES 112 112 Phosphoserine (by MAPK).
FT VARSPLIC 1 30 Missing (in isoform 1).
FT /FTId=VSP_003649.
FT MUTAGEN 112 112 S->A: Increases adipogenic activity.
FT CONFLICT 111 111 A -> R (in Ref. 3).
SQ SEQUENCE 505 AA; 57567 MW; F16E5CAB122EBB32 CRC64;
MGETLGDPPV DPEHGAFADA LPMSTSQEIT MVDTEMPFWP TNFGISSVDL SVMDDHSHSF
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 LKSLRKPFGD FMEPKFEFAV KFNALELDDS DLAIFIAVII
LSGDRPGLLN VKPIEDIQDN LLQALELQLK LNHPESSQLF AKVLQKMTDL RQIVTEHVQL
LHVIKKTETD MSLHPLLQEI YKDLY
//