ID PPARD_HUMAN Reviewed; 441 AA. AC Q03181; A8K6J6; B6ZGS1; Q5D1P0; Q7Z5K0; Q9BUD4; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 05-OCT-2010, entry version 135. DE RecName: Full=Peroxisome proliferator-activated receptor delta; DE Short=PPAR-delta; DE AltName: Full=NUCI; DE AltName: Full=Nuclear hormone receptor 1; DE Short=NUC1; DE AltName: Full=Nuclear receptor subfamily 1 group C member 2; DE AltName: Full=Peroxisome proliferator-activated receptor beta; DE Short=PPAR-beta; GN Name=PPARD; Synonyms=NR1C2, PPARB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND FATTY ACID RP BINDING. RX MEDLINE=93078797; PubMed=1333051; 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 [GENOMIC DNA] (ISOFORM 1). RC TISSUE=Placenta; RX MEDLINE=20311491; PubMed=10851270; 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 [MRNA] (ISOFORM 1). RX PubMed=18619963; DOI=10.1016/j.febslet.2008.07.003; RA Kobayashi T., Kodani Y., Nozawa A., Endo Y., Sawasaki T.; RT "DNA-binding profiling of human hormone nuclear receptors via RT fluorescence correlation spectroscopy in a cell-free system."; RL FEBS Lett. 582:2737-2744(2008). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Spleen; RA Cho M.-C., Yoon D.-Y.; RT "Human PPARdelta cDNA."; RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Placenta; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NIEHS SNPs program; RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22935763; PubMed=14574404; 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.M., 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Placenta; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] 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. RN [11] RP FUNCTION IN NPC1L1 EXPRESSION. RX PubMed=15604518; DOI=10.1194/jlr.M400400-JLR200; RA van der Veen J.N., Kruit J.K., Havinga R., Baller J.F.W., Chimini G., RA Lestavel S., Staels B., Groot P.H.E., Groen A.K., Kuipers F.; RT "Reduced cholesterol absorption upon PPARdelta activation coincides RT with decreased intestinal expression of NPC1L1."; RL J. Lipid Res. 46:526-534(2005). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 171-441 IN COMPLEXES WITH RP EICOSAPENTAENOIC ACID AND THE SYNTHETIC AGONIST GW2433, AND RP UNSATURATED FATTY ACID BINDING. RX PubMed=10198642; DOI=10.1016/S1097-2765(00)80467-0; RA Xu H.E., Lambert M.H., Montana V.G., Parks D.J., Blanchard S.G., RA Brown P.J., Sternbach D.D., Lehmann J.M., Wisely G.B., Willson T.M., RA Kliewer S.A., Milburn M.V.; RT "Molecular recognition of fatty acids by peroxisome proliferator- RT activated receptors."; RL Mol. Cell 3:397-403(1999). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 170-441 IN COMPLEX WITH THE RP SYNTHETIC AGONIST GW2331. RX PubMed=10809235; DOI=10.1210/me.14.5.733; RA Takada I., Yu R.T., Xu H.E., Lambert M.H., Montana V.G., Kliewer S.A., RA Evans R.M., Umesono K.; RT "Alteration of a single amino acid in peroxisome proliferator- RT activated receptor-alpha (PPAR alpha) generates a PPAR delta RT phenotype."; RL Mol. Endocrinol. 14:733-740(2000). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 165-441 IN COMPLEX WITH RP SYNTHETIC AGONIST. RX PubMed=16931011; DOI=10.1016/j.bmcl.2006.08.052; RA Epple R., Azimioara M., Russo R., Xie Y., Wang X., Cow C., Wityak J., RA Karanewsky D., Bursulaya B., Kreusch A., Tuntland T., Gerken A., RA Iskandar M., Saez E., Martin Seidel H., Tian S.-S.; RT "3,4,5-trisubstituted isoxazoles as novel PPARdelta agonists. Part RT 2."; RL Bioorg. Med. Chem. Lett. 16:5488-5492(2006). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 169-440 IN COMPLEX WITH FATTY RP ACIDS. RX PubMed=16405912; DOI=10.1016/j.jmb.2005.12.047; RA Fyffe S.A., Alphey M.S., Buetow L., Smith T.K., Ferguson M.A., RA Soerensen M.D., Bjoerkling F., Hunter W.N.; RT "Recombinant human PPAR-beta/delta ligand-binding domain is locked in RT an activated conformation by endogenous fatty acids."; RL J. Mol. Biol. 356:1005-1013(2006). RN [16] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 175-441. RX PubMed=16387648; DOI=10.1016/j.molcel.2005.12.001; RA Fyffe S.A., Alphey M.S., Buetow L., Smith T.K., Ferguson M.A., RA Soerensen M.D., Bjoerkling F., Hunter W.N.; RT "Reevaluation of the PPAR-beta/delta ligand binding domain model RT reveals why it exhibits the activated form."; RL Mol. Cell 21:1-2(2006). RN [17] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 165-441 IN COMPLEX WITH RP SYNTHETIC AGONIST. RX PubMed=17560785; DOI=10.1016/j.bmcl.2007.05.079; RA Pettersson I., Ebdrup S., Havranek M., Pihera P., Korinek M., RA Mogensen J.P., Jeppesen C.B., Johansson E., Sauerberg P.; RT "Design of a partial PPARdelta agonist."; RL Bioorg. Med. Chem. Lett. 17:4625-4629(2007). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 171-441. RX PubMed=18722772; DOI=10.1016/j.bmcl.2008.08.011; RA Shearer B.G., Patel H.S., Billin A.N., Way J.M., Winegar D.A., RA Lambert M.H., Xu R.X., Leesnitzer L.M., Merrihew R.V., Huet S., RA Willson T.M.; RT "Discovery of a novel class of PPARdelta partial agonists."; RL Bioorg. Med. Chem. Lett. 18:5018-5022(2008). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 170-441 IN COMPLEXES WITH RP THE SYNTHETIC AGONISTS TIPP-401 AND TIPP-204. RX PubMed=19622862; DOI=10.1107/S0907444909015935; RA Oyama T., Toyota K., Waku T., Hirakawa Y., Nagasawa N., Kasuga J.I., RA Hashimoto Y., Miyachi H., Morikawa K.; RT "Adaptability and selectivity of human peroxisome proliferator- RT activated receptor (PPAR) pan agonists revealed from crystal RT structures."; RL Acta Crystallogr. D 65:786-795(2009). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 171-439 IN COMPLEX WITH RP SYNTHETIC AGONIST. RX PubMed=19464171; DOI=10.1016/j.bmcl.2009.04.151; RA Connors R.V., Wang Z., Harrison M., Zhang A., Wanska M., Hiscock S., RA Fox B., Dore M., Labelle M., Sudom A., Johnstone S., Liu J., RA Walker N.P., Chai A., Siegler K., Li Y., Coward P.; RT "Identification of a PPARdelta agonist with partial agonistic activity RT on PPARgamma."; RL Bioorg. Med. Chem. Lett. 19:3550-3554(2009). RN [21] RP X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) OF 165-441 IN COMPLEX WITH RP INDEGLITAZAR. RX PubMed=19116277; DOI=10.1073/pnas.0811325106; RA Artis D.R., Lin J.J., Zhang C., Wang W., Mehra U., Perreault M., RA Erbe D., Krupka H.I., England B.P., Arnold J., Plotnikov A.N., RA Marimuthu A., Nguyen H., Will S., Signaevsky M., Kral J., Cantwell J., RA Settachatgull C., Yan D.S., Fong D., Oh A., Shi S., Womack P., RA Powell B., Habets G., West B.L., Zhang K.Y.J., Milburn M.V., RA Vlasuk G.P., Hirth K.P., Nolop K., Bollag G., Ibrahim P.N., RA Tobin J.F.; RT "Scaffold-based discovery of indeglitazar, a PPAR pan-active anti- RT diabetic agent."; RL Proc. Natl. Acad. Sci. U.S.A. 106:262-267(2009). RN [22] RP STRUCTURE BY NMR OF 66-151. RG RIKEN structural genomics initiative (RSGI); RT "Solution sturcture of the C4-type zinc finger domain from human RT peroxisome proliferator-activated receptor delta."; RL Submitted (APR-2008) to the PDB data bank. CC -!- FUNCTION: Ligand-activated transcription factor. Receptor that CC binds peroxisome proliferators such as hypolipidemic drugs and CC fatty acids. Has a preference for poly-unsaturated fatty acids, CC such as gamma-linoleic acid and eicosapentanoic acid. Once CC activated by a ligand, the receptor binds to promoter elements of CC target genes. Regulates the peroxisomal beta-oxidation pathway of CC fatty acids. Functions as transcription activator for the acyl-CoA CC oxidase gene. Decreases expression of NPC1L1 once activated by a CC ligand. CC -!- SUBUNIT: Heterodimer with the retinoid X receptor. CC -!- SUBCELLULAR LOCATION: Nucleus. 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 -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/ppard/"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Peroxisome proliferator- CC activated receptor entry; CC URL="http://en.wikipedia.org/wiki/Peroxisome_proliferator-activated_receptor"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L07592; AAA36469.1; -; mRNA. DR EMBL; AF246303; AAF62553.1; -; Genomic_DNA. DR EMBL; AF246299; AAF62553.1; JOINED; Genomic_DNA. DR EMBL; AF246300; AAF62553.1; JOINED; Genomic_DNA. DR EMBL; AF246301; AAF62553.1; JOINED; Genomic_DNA. DR EMBL; AF246302; AAF62553.1; JOINED; Genomic_DNA. DR EMBL; AB307691; BAH02282.1; -; mRNA. DR EMBL; AY919140; AAX14041.1; -; mRNA. DR EMBL; AK291661; BAF84350.1; -; mRNA. DR EMBL; AK122614; BAG53624.1; -; mRNA. DR EMBL; AY442342; AAR05439.1; -; Genomic_DNA. DR EMBL; AL022721; CAB38629.1; -; Genomic_DNA. DR EMBL; AL022721; CAD92505.1; -; Genomic_DNA. DR EMBL; CH471081; EAX03825.1; -; Genomic_DNA. DR EMBL; BC002715; AAH02715.1; -; mRNA. DR EMBL; BC007578; AAH07578.1; -; mRNA. DR EMBL; AB099507; BAC78903.1; -; mRNA. DR IPI; IPI00009330; -. DR IPI; IPI00219761; -. DR PIR; A45360; A45360. DR RefSeq; NP_001165289.1; -. DR RefSeq; NP_001165290.1; -. DR RefSeq; NP_001165291.1; -. DR RefSeq; NP_006229.1; -. DR RefSeq; NP_803184.1; -. DR UniGene; Hs.696032; -. DR PDB; 1GWX; X-ray; 2.50 A; A/B=171-441. DR PDB; 1Y0S; X-ray; 2.65 A; A/B=170-441. DR PDB; 2AWH; X-ray; 2.00 A; A/B=174-441. DR PDB; 2B50; X-ray; 2.00 A; A/B=169-440. DR PDB; 2BAW; X-ray; 2.30 A; A/B=175-441. DR PDB; 2ENV; NMR; -; A=72-146. DR PDB; 2GWX; X-ray; 2.30 A; A/B=175-441. DR PDB; 2J14; X-ray; 2.80 A; A/B=165-441. DR PDB; 2Q5G; X-ray; 2.70 A; A/B=165-441. DR PDB; 2ZNP; X-ray; 3.00 A; A/B=170-441. DR PDB; 2ZNQ; X-ray; 2.65 A; A/B=170-441. DR PDB; 3D5F; X-ray; 2.20 A; A/B=175-441. DR PDB; 3DY6; X-ray; 2.90 A; A/B=171-441. DR PDB; 3ET2; X-ray; 2.24 A; A/B=165-441. DR PDB; 3GWX; X-ray; 2.40 A; A/B=171-441. DR PDB; 3GZ9; X-ray; 2.00 A; A=171-439. DR PDBsum; 1GWX; -. DR PDBsum; 1Y0S; -. DR PDBsum; 2AWH; -. DR PDBsum; 2B50; -. DR PDBsum; 2BAW; -. DR PDBsum; 2ENV; -. DR PDBsum; 2GWX; -. DR PDBsum; 2J14; -. DR PDBsum; 2Q5G; -. DR PDBsum; 2ZNP; -. DR PDBsum; 2ZNQ; -. DR PDBsum; 3D5F; -. DR PDBsum; 3DY6; -. DR PDBsum; 3ET2; -. DR PDBsum; 3GWX; -. DR PDBsum; 3GZ9; -. DR ProteinModelPortal; Q03181; -. DR SMR; Q03181; 65-151. DR MINT; MINT-1200178; -. DR STRING; Q03181; -. DR PhosphoSite; Q03181; -. DR PRIDE; Q03181; -. DR Ensembl; ENST00000311565; ENSP00000310928; ENSG00000112033. DR Ensembl; ENST00000360694; ENSP00000353916; ENSG00000112033. DR GeneID; 5467; -. DR UCSC; uc003okl.2; human. DR UCSC; uc003okm.1; human. DR CTD; 5467; -. DR GeneCards; GC06P035357; -. DR H-InvDB; HIX0005804; -. DR HGNC; HGNC:9235; PPARD. DR HPA; CAB017635; -. DR MIM; 600409; gene. DR PharmGKB; PA33557; -. DR eggNOG; prNOG09323; -. DR HOGENOM; HBG446936; -. DR HOVERGEN; HBG106004; -. DR InParanoid; Q03181; -. DR OMA; SSLFLND; -. DR OrthoDB; EOG9V45TJ; -. DR PhylomeDB; Q03181; -. DR Pathway_Interaction_DB; ps1pathway; Presenilin action in Notch and Wnt signaling. DR Pathway_Interaction_DB; rxr_vdr_pathway; RXR and RAR hetrodimerization with other nuclear receptor. DR Reactome; REACT_71; Gene Expression. DR BindingDB; Q03181; -. DR DrugBank; DB00159; Icosapent. DR DrugBank; DB00605; Sulindac. DR DrugBank; DB00374; Treprostinil. DR NextBio; 21160; -. DR ArrayExpress; Q03181; -. DR Bgee; Q03181; -. DR CleanEx; HS_PPARD; -. DR Genevestigator; Q03181; -. DR GermOnline; ENSG00000112033; Homo sapiens. DR GO; GO:0005634; C:nucleus; NAS:UniProtKB. DR GO; GO:0008144; F:drug binding; IDA:UniProtKB. DR GO; GO:0070539; F:linoleic acid binding; IDA:UniProtKB. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0003707; F:steroid hormone receptor activity; TAS:ProtInc. DR GO; GO:0016563; F:transcription activator activity; IDA:UniProtKB. DR GO; GO:0003700; F:transcription factor activity; IDA:UniProtKB. DR GO; GO:0016564; F:transcription repressor activity; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006915; P:apoptosis; IMP:UniProtKB. DR GO; GO:0008366; P:axon ensheathment; ISS:UniProtKB. DR GO; GO:0008203; P:cholesterol metabolic process; TAS:UniProtKB. DR GO; GO:0046697; P:decidualization; TAS:UniProtKB. DR GO; GO:0007566; P:embryo implantation; TAS:UniProtKB. DR GO; GO:0006635; P:fatty acid beta-oxidation; TAS:UniProtKB. DR GO; GO:0015908; P:fatty acid transport; ISS:UniProtKB. DR GO; GO:0006091; P:generation of precursor metabolites and energy; TAS:ProtInc. DR GO; GO:0006006; P:glucose metabolic process; NAS:UniProtKB. DR GO; GO:0015758; P:glucose transport; NAS:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription from R...; ISS:UniProtKB. DR GO; GO:0045600; P:positive regulation of fat cell differentia...; NAS:UniProtKB. DR GO; GO:0006350; P:transcription; IEA:UniProtKB-KW. DR InterPro; IPR003074; 1Cnucl_rcpt. DR InterPro; IPR003075; 1Cnucl_rcpt_B. DR InterPro; IPR008946; Nucl_hormone_rcpt_ligand-bd. DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd_core. DR InterPro; IPR001723; Str_hrmn_rcpt. DR InterPro; IPR001628; Znf_hrmn_rcpt. DR InterPro; IPR013088; Znf_NHR/GATA. DR Gene3D; G3DSA:1.10.565.10; Nucl_hrmn_rcpt_lig_bd; 1. DR Gene3D; G3DSA:3.30.50.10; Znf_NHR/GATA; 1. DR Pfam; PF00104; Hormone_recep; 1. DR Pfam; PF00105; zf-C4; 1. DR PRINTS; PR01288; PROXISOMEPAR. DR PRINTS; PR01290; PROXISOMPABR. DR PRINTS; PR00398; STRDHORMONER. DR PRINTS; PR00047; STROIDFINGER. DR SMART; SM00430; HOLI; 1. DR SMART; SM00399; ZnF_C4; 1. DR SUPFAM; SSF48508; Str_ncl_receptor; 1. DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1. DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Activator; Alternative splicing; Complete proteome; KW DNA-binding; Metal-binding; Nucleus; Receptor; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1 441 Peroxisome proliferator-activated FT receptor delta. FT /FTId=PRO_0000053486. FT DNA_BIND 71 145 Nuclear receptor. FT ZN_FING 74 94 NR C4-type. FT ZN_FING 111 133 NR C4-type. FT REGION 254 441 Ligand-binding. FT VAR_SEQ 360 361 DR -> GE (in isoform 2). FT /FTId=VSP_010133. FT VAR_SEQ 362 441 Missing (in isoform 2). FT /FTId=VSP_010134. FT CONFLICT 79 79 D -> G (in Ref. 5; BAF84350). FT CONFLICT 134 134 L -> P (in Ref. 3; BAH02282). FT HELIX 170 173 FT HELIX 175 189 FT HELIX 194 200 FT STRAND 211 213 FT HELIX 216 223 FT TURN 224 226 FT HELIX 241 264 FT TURN 268 272 FT HELIX 275 294 FT HELIX 295 297 FT STRAND 302 305 FT HELIX 306 308 FT STRAND 310 313 FT HELIX 314 318 FT HELIX 322 339 FT HELIX 345 356 FT HELIX 367 388 FT HELIX 395 423 FT HELIX 431 437 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 //