Swiss-Prot entry
ID PPAR_MOUSE STANDARD; PRT; 468 AA.
AC P23204;
DT 01-NOV-1991 (Rel. 20, Created)
DT 01-OCT-1996 (Rel. 34, 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 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.
RX MEDLINE=91015382; PubMed=2129546 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1038/347645a0;
RA Issemann I., Green S.;
RT "Activation of a member of the steroid hormone receptor superfamily by
RT peroxisome proliferators.";
RL Nature 347:645-650(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=129/Sv;
RX MEDLINE=94168583; PubMed=8123021 [NCBI, ExPASy, EBI, Israel, Japan];
RA Gearing K.L., Crickmore A., Gustafsson J.-A.;
RT "Structure of the mouse peroxisome proliferator activated receptor
RT alpha gene.";
RL Biochem. Biophys. Res. Commun. 199:255-263(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
RX MEDLINE=22388257; PubMed=12477932 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1073/pnas.242603899;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length human
RT and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE OF 413-468.
RC STRAIN=Swiss Webster; TISSUE=Liver;
RX MEDLINE=96061953; PubMed=7588749 [NCBI, ExPASy, EBI, Israel, Japan];
RA Jones P.S., Savory R., Barratt P., Bell A.R., Gray T.J.B.,
RA Jenkins N.A., Gilbert D.J., Copeland N.G., Bell D.R.;
RT "Chromosomal localisation, inducibility, tissue-specific expression
RT and strain differences in three murine peroxisome-proliferator-
RT activated-receptor genes.";
RL Eur. J. Biochem. 233:219-226(1995).
RN [5]
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.
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.
CC -!- SUBCELLULAR LOCATION: Nuclear.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver, kidney and heart.
CC Very weakly expressed in brain and testis.
CC -!- DEVELOPMENTAL STAGE: It appears first at day 13.5 postconception,
CC and increases until birth.
CC -!- DISEASE: Peroxisome proliferators are a diverse group of chemicals
CC that include hypolipidaemic drugs, herbicides and industrial
CC plasticisers. Administration of these chemicals to rodents results
CC in the dramatic proliferation of hepatic peroxisomes as well as
CC liver hyperplasia.
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; X57638; CAA40856.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; X75289; CAA53042.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; X75290; CAA53042.1; JOINED. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; X75291; CAA53042.1; JOINED. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; X75292; CAA53042.1; JOINED. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; X75293; CAA53042.1; JOINED. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; X75294; CAA53042.1; JOINED. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; BC016892; AAH16892.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; X89577; CAA61754.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR PIR; JC2085; JC2085.
DR HSSP; Q07869; 1I7G. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR SMR; P23204; 200-468.
DR TRANSFAC; T00694; -.
DR Ensembl; ENSMUSG00000022383; Mus_musculus
DR MGD; MGI:104740; Ppara.
DR GeneLynx; Ppara..
DR SOURCE; Ppara..
DR GO; GO:0005634; C:nucleus; TAS.
DR GO; GO:0003677; F:DNA binding; IDA.
DR GO; GO:0004872; F:receptor activity; IDA.
DR GO; GO:0003707; F:steroid hormone receptor activity; TAS.
DR GO; GO:0016563; F:transcriptional activator activity; IDA.
DR GO; GO:0008544; P:epidermis development; IMP.
DR GO; GO:0006006; P:glucose metabolism; TAS.
DR GO; GO:0045944; P:positive regulation of transcription from P...; IDA.
DR GO; GO:0019217; P:regulation of fatty acid metabolism; IMP.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; TAS.
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; P23204.
DR HOVERGEN [Family / Alignment / Tree]
DR BLOCKS; P23204.
DR ProtoNet; P23204.
DR ProtoMap; P23204.
DR PRESAGE; P23204.
DR DIP; P23204.
DR ModBase; P23204.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW Activator; DNA-binding; Multigene family; Nuclear protein; Receptor;
KW Transcription; Transcription regulation; 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).
FT CONFLICT 75 75 A -> R (in Ref. 1).
SQ SEQUENCE 468 AA; 52347 MW; 2930A5191C610B6B CRC64;
MVDTESPICP LSPLEADDLE SPLSEEFLQE MGNIQEISQS IGEESSGSFG FADYQYLGSC
PGSEGSVITD TLSPASSPSS VSCPVIPAST DESPGSALNI ECRICGDKAS GYHYGVHACE
GCKGFFRRTI RLKLVYDKCD RSCKIQKKNR NKCQYCRFHK CLSVGMSHNA IRFGRMPRSE
KAKLKAEILT CEHDLKDSET ADLKSLGKRI HEAYLKNFNM NKVKARVILA GKTSNNPPFV
IHDMETLCMA EKTLVAKMVA NGVEDKEAEV RFFHCCQCMS VETVTELTEF AKAIPGFANL
DLNDQVTLLK YGVYEAIFTM LSSLMNKDGM LIAYGNGFIT REFLKNLRKP FCDIMEPKFD
FAMKFNALEL DDSDISLFVA AIICCGDRPG LLNIGYIEKL QEGIVHVLKL HLQSNHPDDT
FLFPKLLQKM VDLRQLVTEH AQLVQVIKKT ESDAALHPLL QEIYRDMY
//