Swiss-Prot entry

ID   PPAT_XENLA     STANDARD;      PRT;   477 AA.
AC   P37234;
DT   01-OCT-1994 (Rel. 30, Created)
DT   01-OCT-1994 (Rel. 30, 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   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 
OC   Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; 
OC   Xenopodinae; Xenopus; Xenopus. 
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=92191267; PubMed=1312391 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1016/0092-8674(92)90031-7;
RA   Dreyer C., Krey G., Keller H., Givel F., Helftenbein G., Wahli W.;
RT   "Control of the peroxisomal beta-oxidation pathway by a novel family
RT   of nuclear hormone receptors.";
RL   Cell 68:879-887(1992).
RN   [2]
RP   CHARACTERIZATION.
RX   MEDLINE=94100165; PubMed=8274443 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1016/0960-0760(93)90058-5;
RA   Krey G., Keller H., Mahfoudi A., Medin J., Ozato K., Dreyer C.,
RA   Wahli W.;
RT   "Xenopus peroxisome proliferator activated receptors: genomic
RT   organization, response element recognition, heterodimer formation with
RT   retinoid X receptor and activation by fatty acids.";
RL   J. Steroid Biochem. Mol. Biol. 47:65-73(1993).
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: Heterodimer with the retinoid X receptor.
CC   -!- SUBCELLULAR LOCATION: Nuclear.
CC   -!- TISSUE SPECIFICITY: Expressed mainly in adipose tissue and kidney.
CC   -!- DEVELOPMENTAL STAGE: Adult.
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; M84163; AAA49937.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   PIR; C42214; C42214.
DR   HSSP; Q96J12; 1NYX. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR   TRANSFAC; T01354; -.
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; P37234.
DR   ProtoNet; P37234.
DR   ProtoMap; P37234.
DR   PRESAGE; P37234.
DR   DIP; P37234.
DR   ModBase; P37234.
DR   SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW   Activator; DNA-binding; Multigene family; Nuclear protein;
KW   Phosphorylation; Receptor; Transcription; Transcription regulation;
KW   Zinc-finger.
FT   DNA_BIND    110    184       Nuclear receptor-type.
FT   ZN_FING     113    133       C4-type.
FT   ZN_FING     150    172       C4-type.
FT   DOMAIN      293    477       Ligand-binding (Potential).
FT   MOD_RES      87     87       Phosphoserine (by MAPK) (By similarity).
SQ   SEQUENCE   477 AA;  54056 MW;  160F87A401CB7246 CRC64;
     MVDTEMPFWS NLNFGMNSMD MSALEDHCQP YDIKPFTTVD FSSINSHYDD ILDEKTFLCR
     NDQSPIDYKY DLKLQECQSS IKLEPPSPPY FSDKPQCSKA FEDTPNSFIA IECRVCGDKA
     SGFHYGVHAC EGCKGFFRRT IRLKLIYERC DLNCRIHKKS RNKCQFCRFQ KCLAVGMSHN
     AIRFGRMPQA EKEKLLAEIS SDIDQLNPES ADQRVLAKHL YDSYVKSFPL TKAKAPGHPD
     GQSHRQNSRG YTRHELADDG GGSDQGAVRE PRAEQGGGDS NLPALSVALR GGVREITEFA
     KNIPGFVSLD LNDQVTLLKY GVHEIIFTML ASLMNKDGVL VAEGQGFMTR EFLKSLRKPF
     SDFMEPKFEF AIRFNSLELD DSDLAIFVAV IILSGDRPGL LNVKPIEDIQ DSLLQALELQ
     LKLNHPDSAQ LFAKLLQKMT DLRQVVTEHV QLLQLIKKTE ADMCLHPLLQ EIYKDLY
//