Swiss-Prot entry
ID PPAT_BOVIN STANDARD; PRT; 505 AA.
AC O18971; Q8HY47;
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC Pecora; Bovidae; Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2).
RC TISSUE=Fat;
RX MEDLINE=98042483; PubMed=9367859 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1006/bbrc.1997.7564;
RA Sundvold H., Brzozowska A., Lien S.;
RT "Characterisation of bovine peroxisome proliferator-activated
RT receptors gamma 1 and gamma 2: genetic mapping and differential
RT expression of the two isoforms.";
RL Biochem. Biophys. Res. Commun. 239:857-861(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORM 2).
RA Jeoung Y.-H., Yoon D.-H., Chang E.-R., Kang M.-J.;
RT "Bovine PPAR gamma mRNA.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
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=O18971-1; Sequence=Displayed;
CC Name=1;
CC IsoId=O18971-2; Sequence=VSP_003644;
CC -!- TISSUE SPECIFICITY: Highest expression in adipose tissue. Lower in
CC spleen and lung. Also detected in ovary mammary gland and small
CC intestine.
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; Y12420; CAA73033.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; Y12419; CAA73032.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AY179866; AAN75018.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR PIR; JC5777; JC5777.
DR HSSP; Q96J12; 2PRG. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR SMR; O18971; 234-505.
DR TRANSFAC; T04780; -.
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 HOVERGEN [Family / Alignment / Tree]
DR BLOCKS; O18971.
DR ProtoNet; O18971.
DR ProtoMap; O18971.
DR PRESAGE; O18971.
DR DIP; O18971.
DR ModBase; O18971.
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) (By similarity).
FT VARSPLIC 1 30 Missing (in isoform 1).
FT /FTId=VSP_003644.
FT CONFLICT 81 81 I -> T (in Ref. 2).
FT CONFLICT 140 140 R -> W (in Ref. 2).
FT CONFLICT 157 157 E -> G (in Ref. 2).
FT CONFLICT 486 486 K -> I (in Ref. 2).
SQ SEQUENCE 505 AA; 57579 MW; 5F20B115087B3C83 CRC64;
MGETLGDALI DPESEPFAVT VSARTSQEIT MVDTEMPFWP TNFGISSVDL SMMDDHSHAF
DIKPFTTVDF SSISTPHYED IPFPRADPMV ADYKYDLKLQ EYQSAIKVEP VSPPYYSEKT
QLYSKPHEEP SNSLMAIECR VCGDKASGFH YGVHACEGCK GFFRRTIRLK LIYDRCDLNC
RIHKKSRNKC QYCRFQKCLA VGMSHNAIRF GRMPQAEKEK LLAEISSDID QLNPESADLR
ALAKHLYDSY IKSFPLTKAK ARAILTGKTT DKSPFVIYDM NSLMMGEDKI KFKHISPLQE
PSKEVAIRIF QGCQFRSVEA VQEITEYAKN IPGFVNLDLN DQVTLLKYGV HEIIYTMLAS
LMNKDGVLIS EGQGFMTREF LKSLRKPFGD FMEPKFEFAV KFNALELDDS DLAIFIAVII
LSGDRPGLLN VKPIEDIQDN LLQALELQLK LNHPESSQLF AKLLQKMTDL RQIVTEHVQL
LQVIKKTETD MSLHPLLQEI YKDLY
//