Swiss-Prot entry
ID PPAS_MOUSE STANDARD; PRT; 440 AA.
AC P35396; P37239;
DT 01-JUN-1994 (Rel. 29, Created)
DT 01-JUN-1994 (Rel. 29, Last sequence update)
DT 01-MAY-2005 (Rel. 47, Last annotation update)
DE Peroxisome proliferator activated receptor delta (PPAR-delta) (PPAR-
DE beta) (Nuclear hormone receptor 1) (NUC1).
GN Name=Ppard; Synonyms=Nr1c2, Pparb;
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.
RC STRAIN=C57BL/6J; TISSUE=Adipocyte;
RX MEDLINE=95138211; PubMed=7836471 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1074/jbc.270.5.2367;
RA Amri E.-Z., Bonino F., Ailhaud G., Abumrad N.A., Grimaldi P.A.;
RT "Cloning of a protein that mediates transcriptional effects of fatty
RT acids in preadipocytes. Homology to peroxisome proliferator-activated
RT receptors.";
RL J. Biol. Chem. 270:2367-2371(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6; TISSUE=Brain;
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 1-145.
RC STRAIN=BALB/c; TISSUE=Brain;
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).
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.
CC -!- SUBCELLULAR LOCATION: Nuclear.
CC -!- TISSUE SPECIFICITY: Heart, adrenal and 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; L28116; AAA63394.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; U10375; AAA19972.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; BC070398; AAH70398.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; U01665; AAA03332.1; ALT_INIT. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR PIR; I55442; I55442.
DR HSSP; Q03181; 3GWX. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR SMR; P35396; 170-440.
DR TRANSFAC; T04781; -.
DR Ensembl; ENSMUSG00000002250; Mus_musculus
DR MGD; MGI:101884; Ppard.
DR GeneLynx; Ppard..
DR SOURCE; Ppard..
DR GO; GO:0003677; F:DNA binding; IDA.
DR GO; GO:0004879; F:ligand-dependent nuclear receptor activity; TAS.
DR GO; GO:0016564; F:transcriptional repressor activity; IDA.
DR GO; GO:0008283; P:cell proliferation; IMP.
DR GO; GO:0008544; P:epidermis development; TAS.
DR GO; GO:0006629; P:lipid metabolism; IMP.
DR GO; GO:0000122; P:negative regulation of transcription from P...; IDA.
DR GO; GO:0008366; P:nerve ensheathment; IMP.
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; PR01290; PROXISOMPABR.
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; P35396.
DR HOVERGEN [Family / Alignment / Tree]
DR BLOCKS; P35396.
DR ProtoNet; P35396.
DR ProtoMap; P35396.
DR PRESAGE; P35396.
DR DIP; P35396.
DR ModBase; P35396.
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 70 144 Nuclear receptor-type.
FT ZN_FING 73 93 C4-type.
FT ZN_FING 110 132 C4-type.
FT DOMAIN 253 440 Ligand-binding (Potential).
FT CONFLICT 149 150 EA -> DG (in Ref. 2).
SQ SEQUENCE 440 AA; 49715 MW; 58E0F595DD193FDA CRC64;
MEQPQEETPE AREEEKEEVA MGDGAPELNG GPEHTLPSSS CADLSQNSSP SSLLDQLQMG
CDGASGGSLN MECRVCGDKA SGFHYGVHAC EGCKGFFRRT IRMKLEYEKC DRICKIQKKN
RNKCQYCRFQ KCLALGMSHN AIRFGRMPEA EKRKLVAGLT ASEGCQHNPQ LADLKAFSKH
IYNAYLKNFN MTKKKARSIL TGKSSHNAPF VIHDIETLWQ AEKGLVWKQL VNGLPPYNEI
SVHVFYRCQS TTVETVRELT EFAKNIPNFS SLFLNDQVTL LKYGVHEAIF AMLASIVNKD
GLLVANGSGF VTHEFLRSLR KPFSDIIEPK FEFAVKFNAL ELDDSDLALF IAAIILCGDR
PGLMNVPQVE AIQDTILRAL EFHLQVNHPD SQYLFPKLLQ KMADLRQLVT EHAQMMQWLK
KTESETLLHP LLQEIYKDMY
//