Swiss-Prot entry
ID PPAS_HUMAN STANDARD; PRT; 441 AA.
AC Q03181; Q7Z5K0; Q9BUD4;
DT 01-OCT-1993 (Rel. 27, Created)
DT 01-OCT-1993 (Rel. 27, 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) (NUCI).
GN Name=PPARD; Synonyms=NR1C2, PPARB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RX MEDLINE=93078797; PubMed=1333051 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1210/me.6.10.1634;
RA Schmidt A., Endo N., Rutledge S.J., Vogel R., Shinar D., Rodan G.A.;
RT "Identification of a new member of the steroid hormone receptor
RT superfamily that is activated by a peroxisome proliferator and fatty
RT acids.";
RL Mol. Endocrinol. 6:1634-1641(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RX MEDLINE=20311491; PubMed=10851270 [NCBI, ExPASy, EBI, Israel, Japan];
RA Skogsberg J., Kannisto K., Roshani L., Gagne E., Hamsten A.,
RA Larsson C., Ehrenborg E.;
RT "Characterization of the human peroxisome proliferator activated
RT receptor delta gene and its expression.";
RL Int. J. Mol. Med. 6:73-81(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RA Livingston R.J., Rieder M.J., Chung M.-W., Ritchie T.K., Olson A.N.,
RA Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D., Schackwitz W.S.,
RA Sherwood J.K., Sherwood A.M., Leithauser B.J., Nickerson D.A.;
RT "NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department
RT of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX MEDLINE=22935763; PubMed=14574404 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
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 [6]
RP NUCLEOTIDE SEQUENCE OF 1-161.
RA Aoto T., Ishizuka M., Kazusaka A., Fujita S.;
RT "PPAR-delta 5'-complete cDNA fragment.";
RL Submitted (JAN-2003) 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.
CC -!- SUBUNIT: Heterodimer with the retinoid X receptor.
CC -!- SUBCELLULAR LOCATION: Nuclear.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q03181-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q03181-2; Sequence=VSP_010133, VSP_010134;
CC -!- TISSUE SPECIFICITY: Ubiquitous with maximal levels in placenta and
CC skeletal muscle.
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; L07592; AAA36469.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AF246303; AAF62553.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AF246299; AAF62553.1; JOINED. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AF246300; AAF62553.1; JOINED. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AF246301; AAF62553.1; JOINED. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AF246302; AAF62553.1; JOINED. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AY442342; AAR05439.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AL022721; CAB38629.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AL022721; CAD92505.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; BC002715; AAH02715.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; BC007578; AAH07578.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AB099507; BAC78903.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR PDB; 1GWX; X-ray; A/B=171-441. [ExPASy / RCSB]
DR PDB; 2GWX; X-ray; A/B=175-441. [ExPASy / RCSB]
DR PDB; 3GWX; X-ray; A/B=171-441. [ExPASy / RCSB]
DR TRANSFAC; T02745; -.
DR Ensembl; ENSG00000112033; Homo_sapiens
DR Genew; HGNC:9235; PPARD.
DR CleanEx; HGNC:9235; PPARD.
DR MIM; 600409; -. [NCBI / EBI]
DR GeneCards; PPARD.
DR GeneLynx; PPARD.
DR GenAtlas; PPARD.
DR SOURCE; PPARD.
DR GO; GO:0005634; C:nucleus; TAS.
DR GO; GO:0003707; F:steroid hormone receptor activity; TAS.
DR GO; GO:0003700; F:transcription factor activity; TAS.
DR GO; GO:0006091; P:energy pathways; TAS.
DR GO; GO:0006629; P:lipid metabolism; TAS.
DR GO; GO:0006357; P:regulation of transcription from Pol II pro...; 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; 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; Q03181.
DR HOVERGEN [Family / Alignment / Tree]
DR BLOCKS; Q03181.
DR ProtoNet; Q03181.
DR ProtoMap; Q03181.
DR PRESAGE; Q03181.
DR DIP; Q03181.
DR ModBase; Q03181.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW 3D-structure; Activator; Alternative splicing; DNA-binding;
KW Multigene family; Nuclear protein; Receptor; Transcription;
KW Transcription regulation; Zinc-finger.
FT DNA_BIND 71 145 Nuclear receptor-type.
FT ZN_FING 74 94 C4-type.
FT ZN_FING 111 133 C4-type.
FT DOMAIN 254 441 Ligand-binding (By similarity).
FT VARSPLIC 360 361 DR -> GE (in isoform 2).
FT /FTId=VSP_010133.
FT VARSPLIC 362 441 Missing (in isoform 2).
FT /FTId=VSP_010134.
FT HELIX 176 189
FT HELIX 194 197
FT TURN 198 200
FT STRAND 211 213
FT HELIX 216 222
FT TURN 223 227
FT HELIX 241 266
FT TURN 268 272
FT HELIX 275 293
FT TURN 294 294
FT HELIX 295 297
FT STRAND 298 298
FT STRAND 302 305
FT TURN 306 309
FT STRAND 310 313
FT HELIX 314 318
FT TURN 319 319
FT TURN 322 323
FT HELIX 324 326
FT TURN 327 328
FT HELIX 329 339
FT TURN 340 341
FT HELIX 345 356
FT TURN 359 360
FT TURN 362 363
FT HELIX 367 388
FT HELIX 396 423
FT TURN 425 426
FT HELIX 431 437
FT TURN 438 439
SQ SEQUENCE 441 AA; 49903 MW; 94FBB2A4B46521E8 CRC64;
MEQPQEEAPE VREEEEKEEV AEAEGAPELN GGPQHALPSS SYTDLSRSSS PPSLLDQLQM
GCDGASCGSL NMECRVCGDK ASGFHYGVHA CEGCKGFFRR TIRMKLEYEK CERSCKIQKK
NRNKCQYCRF QKCLALGMSH NAIRFGRMPE AEKRKLVAGL TANEGSQYNP QVADLKAFSK
HIYNAYLKNF NMTKKKARSI LTGKASHTAP FVIHDIETLW QAEKGLVWKQ LVNGLPPYKE
ISVHVFYRCQ CTTVETVREL TEFAKSIPSF SSLFLNDQVT LLKYGVHEAI FAMLASIVNK
DGLLVANGSG FVTREFLRSL RKPFSDIIEP KFEFAVKFNA LELDDSDLAL FIAAIILCGD
RPGLMNVPRV EAIQDTILRA LEFHLQANHP DAQYLFPKLL QKMADLRQLV TEHAQMMQRI
KKTETETSLH PLLQEIYKDM Y
//