Swiss-Prot entry

ID   PPAR_RAT       STANDARD;      PRT;   468 AA.
AC   P37230;
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 alpha (PPAR-alpha).
GN   Name=Ppara; Synonyms=Nr1c1, Ppar;
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.
RX   MEDLINE=92262498; PubMed=1316614 [NCBI, ExPASy, EBI, Israel, Japan];
RA   Goettlicher M., Widmark E., Li Q., Gustafsson J.-A.;
RT   "Fatty acids activate a chimera of the clofibric acid-activated
RT   receptor and the glucocorticoid receptor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:4653-4657(1992).
RN   [2]
RP   PHOSPHORYLATION.
RX   MEDLINE=96426218; PubMed=8828512 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1210/en.137.10.4499;
RA   Shalev A., Siegrist-Kaiser C.A., Yen P.M., Wahli W., Burger A.G.,
RA   Chin W.W., Meier C.A.;
RT   "The peroxisome proliferator-activated receptor alpha is a
RT   phosphoprotein: regulation by insulin.";
RL   Endocrinology 137:4499-4502(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.
CC   -!- SUBUNIT: Heterodimer with the retinoid X receptor. Interacts with
CC       NCOA3 and NCOA6 coactivators, leading to a strong increase of
CC       transcription of target genes (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nuclear.
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in liver and kidney.
CC   -!- PTM: Phosphorylated.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 nuclear receptor DNA-binding domain.
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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.
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DR   EMBL; M88592; AAA41918.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   PIR; A45288; A45288.
DR   HSSP; Q07869; 1I7G. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR   SMR; P37230; 200-468.
DR   TRANSFAC; T00991; -.
DR   Ensembl; ENSRNOG00000021463; Rattus_norvegicus
DR   RGD; 3369; Ppara.
DR   GO; GO:0003706; F:ligand-regulated transcription factor activity; IDA.
DR   GO; GO:0019904; F:protein domain specific binding; IDA.
DR   GO; GO:0003707; F:steroid hormone receptor activity; TAS.
DR   GO; GO:0019217; P:regulation of fatty acid metabolism; TAS.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; 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; PR01289; PROXISOMPAAR.
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; P37230.
DR   HOVERGEN [Family / Alignment / Tree]
DR   BLOCKS; P37230.
DR   ProtoNet; P37230.
DR   ProtoMap; P37230.
DR   PRESAGE; P37230.
DR   DIP; P37230.
DR   ModBase; P37230.
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     99    173       Nuclear receptor-type.
FT   ZN_FING     102    122       C4-type.
FT   ZN_FING     139    161       C4-type.
FT   DOMAIN      281    468       Ligand-binding (Potential).
SQ   SEQUENCE   468 AA;  52377 MW;  2A89E7D715C8DBA9 CRC64;
     MVDTESPICP LSPLEADDLE SPLSEEFLQE MGNIQEISQS LGEESSGSFS FADYQYLGSC
     PGSEGSVITD TLSPASSPSS VSCPAVPTST DESPGNALNI ECRICGDKAS GYHYGVHACE
     GCKGFFRRTI RLKLAYDKCD RSCKIQKKNR NKCQYCRFHK CLSVGMSHNA IRFGRMPRSE
     KAKLKAEILT CEHDLKDSET ADLKSLAKRI HEAYLKNFNM NKVKARVILA GKTSNNPPFV
     IHDMETLCMA EKTLVAKMVA NGVENKEAEV RFFHCCQCMS VETVTELTEF AKAIPGFANL
     DLNDQVTLLK YGVYEAIFTM LSSLMNKDGM LIAYGNGFIT REFLKNLRKP FCDIMEPKFD
     FAMKFNALEL DDSDISLFVA AIICCGDRPG LLNIGYIEKL QEGIVHVLKL HLQSNHPDDT
     FLFPKLLQKM VDLRQLVTEH AQLVQVIKKT ESDAALHPLL QEIYRDMY
//