Swiss-Prot entry
ID PPAT_MOUSE STANDARD; PRT; 505 AA.
AC P37238;
DT 01-OCT-1994 (Rel. 30, 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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muridae; Murinae; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE (ISOFORM 2), AND SUBUNIT.
RC TISSUE=Adipose tissue;
RX MEDLINE=95011536; PubMed=7926726 [NCBI, ExPASy, EBI, Israel, Japan];
RA Tontonoz P., Hu E., Graves R.A., Budavari A.I., Spiegelman B.M.;
RT "mPPAR gamma 2: tissue-specific regulator of an adipocyte enhancer.";
RL Genes Dev. 8:1224-1234(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RC STRAIN=BALB/c; TISSUE=Heart;
RX MEDLINE=94059089; PubMed=8240342 [NCBI, ExPASy, EBI, Israel, Japan];
RA Chen F., Law S.W., O'Malley B.W.;
RT "Identification of two mPPAR related receptors and evidence for the
RT existence of five subfamily members.";
RL Biochem. Biophys. Res. Commun. 196:671-677(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RC STRAIN=C57BL/6 X CBA; TISSUE=Liver;
RX MEDLINE=94086482; PubMed=8262913 [NCBI, ExPASy, EBI, Israel, Japan];
RA Zhu Y., Alvares K., Huang Q., Rao M.S., Reddy J.K.;
RT "Cloning of a new member of the peroxisome proliferator-activated
RT receptor gene family from mouse liver.";
RL J. Biol. Chem. 268:26817-26820(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RC TISSUE=Liver;
RX MEDLINE=94316694; PubMed=8041794 [NCBI, ExPASy, EBI, Israel, Japan];
RA Kliewer S.A., Forman B.M., Blumberg B., Ong E.S., Borgmeyer U.,
RA Mangelsdorf D.J., Umesono K., Evans R.M.;
RT "Differential expression and activation of a family of murine
RT peroxisome proliferator-activated receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:7355-7359(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE.
RX MEDLINE=96249427; PubMed=8647948 [NCBI, ExPASy, EBI, Israel, Japan];
RA Vidal-Puig A., Jimenez-Linan M., Lowell B.B., Hamann A., Hu E.,
RA Spiegelman B., Flier J.S., Moller D.E.;
RT "Regulation of PPAR gamma gene expression by nutrition and obesity in
RT rodents.";
RL J. Clin. Invest. 97:2553-2561(1996).
RN [6]
RP PROTEIN SEQUENCE OF 66-85 AND 146-160, SUBUNIT, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Adipose tissue;
RX PubMed=7838715 [NCBI, ExPASy, EBI, Israel, Japan];
RA Tontonoz P., Graves R.A., Budavari A.I., Erdjument-Bromage H., Lui M.,
RA Hu E., Tempst P., Spiegelman B.M.;
RT "Adipocyte-specific transcription factor ARF6 is a heterodimeric
RT complex of two nuclear hormone receptors, PPAR gamma and RXR alpha.";
RL Nucleic Acids Res. 22:5628-5634(1994).
RN [7]
RP INTERACTION WITH NCOA6.
RX MEDLINE=20250907; PubMed=10788465 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1074/jbc.275.18.13510;
RA Zhu Y.-J., Kan L., Qi C., Kanwar Y.S., Yeldandi A.V., Rao M.S.,
RA Reddy J.K.;
RT "Isolation and characterization of peroxisome proliferator-activated
RT receptor (PPAR) interacting protein (PRIP) as a coactivator for
RT PPAR.";
RL J. Biol. Chem. 275:13510-13516(2000).
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. ARF6 acts as
CC a key regulator of the tissue-specific adipocyte P2 (aP2)
CC enhancer.
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.
CC -!- SUBCELLULAR LOCATION: Nuclear.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=P37238-1; Sequence=Displayed;
CC Name=1;
CC IsoId=P37238-2; Sequence=VSP_003647;
CC -!- TISSUE SPECIFICITY: Highest expression in adipose tissue. Also
CC found in liver, skeletal muscle, heart, adrenal gland, spleen,
CC kidney and intestine. Isoform 2 is more abundant than isoform 1 in
CC adipose tissue.
CC -!- DEVELOPMENTAL STAGE: It appears first at day 13.5 postconception,
CC and increases until birth.
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; U09138; AAA62277.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; U01664; AAA62110.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; U01841; AAC52134.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; U10374; AAA19971.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR PIR; A54101; A54101.
DR HSSP; Q96J12; 1NYX. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR SMR; P37238; 234-505.
DR TRANSFAC; T02529; -.
DR TRANSFAC; T05332; -.
DR Ensembl; ENSMUSG00000000440; Mus_musculus
DR MGD; MGI:97747; Pparg.
DR GeneLynx; Pparg..
DR SOURCE; Pparg..
DR GO; GO:0005829; C:cytosol; IDA.
DR GO; GO:0005634; C:nucleus; IDA.
DR GO; GO:0004879; F:ligand-dependent nuclear receptor activity; TAS.
DR GO; GO:0003700; F:transcription factor activity; IDA.
DR GO; GO:0016563; F:transcriptional activator activity; IDA.
DR GO; GO:0016564; F:transcriptional repressor activity; IDA.
DR GO; GO:0045444; P:adipocyte differentiation; IDA.
DR GO; GO:0006954; P:inflammatory response; TAS.
DR GO; GO:0000122; P:negative regulation of transcription from P...; IDA.
DR GO; GO:0045944; P:positive regulation of transcription from P...; IDA.
DR GO; GO:0045449; P:regulation of transcription; IDA.
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; P37238.
DR HOVERGEN [Family / Alignment / Tree]
DR BLOCKS; P37238.
DR ProtoNet; P37238.
DR ProtoMap; P37238.
DR PRESAGE; P37238.
DR DIP; P37238.
DR ModBase; P37238.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW Activator; Alternative splicing; Direct protein sequencing;
KW DNA-binding; Multigene family; Nuclear protein; Phosphorylation;
KW Receptor; Transcription; 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) (By similarity).
FT VARSPLIC 1 30 Missing (in isoform 1).
FT /FTId=VSP_003647.
FT CONFLICT 213 214 MP -> DR (in Ref. 2).
FT CONFLICT 281 283 NSL -> SSF (in Ref. 2).
FT CONFLICT 383 383 N -> S (in Ref. 2 and 4).
FT CONFLICT 497 497 L -> F (in Ref. 2).
SQ SEQUENCE 505 AA; 57598 MW; AB8F3F6086E2A10A CRC64;
MGETLGDSPV DPEHGAFADA LPMSTSQEIT MVDTEMPFWP TNFGISSVDL SVMEDHSHSF
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 LKNLRKPFGD FMEPKFEFAV KFNALELDDS DLAIFIAVII
LSGDRPGLLN VKPIEDIQDN LLQALELQLK LNHPESSQLF AKVLQKMTDL RQIVTEHVQL
LHVIKKTETD MSLHPLLQEI YKDLY
//