ID PPARD_HUMAN Reviewed; 441 AA. AC Q03181; A8K6J6; B4E3V3; B6ZGS1; B7Z3W1; E9PE18; Q5D1P0; Q7Z5K0; Q9BUD4; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 25-MAY-2022, entry version 243. 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; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND FATTY ACID BINDING. RX PubMed=1333051; DOI=10.1210/mend.6.10.1333051; 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 superfamily RT that is activated by a peroxisome proliferator and fatty acids."; RL Mol. Endocrinol. 6:1634-1641(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1). RC TISSUE=Placenta; RX PubMed=10851270; DOI=10.3892/ijmm.6.1.73; RA Skogsberg J., Kannisto K., Roshani L., Gagne E., Hamsten A., Larsson C., RA Ehrenborg E.; RT "Characterization of the human peroxisome proliferator activated receptor RT 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 fluorescence RT 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] (ISOFORMS 1; 3 AND 4). RC TISSUE=Placenta, and Thalamus; 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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 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., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., 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., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA 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., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., 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 project: RT 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 with RT 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 UNSATURATED RP 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-activated RT 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/mend.14.5.0456; 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-activated RT receptor-alpha (PPAR alpha) generates a PPAR delta phenotype."; RL Mol. Endocrinol. 14:733-740(2000). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 165-441 IN COMPLEX WITH SYNTHETIC RP 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 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 an RT 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 reveals RT 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 SYNTHETIC RP 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 THE RP 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-activated RT receptor (PPAR) pan agonists revealed from crystal structures."; RL Acta Crystallogr. D 65:786-795(2009). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 171-439 IN COMPLEX WITH SYNTHETIC RP 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., Walker N.P., RA Chai A., Siegler K., Li Y., Coward P.; RT "Identification of a PPARdelta agonist with partial agonistic activity on RT 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., Erbe D., RA Krupka H.I., England B.P., Arnold J., Plotnikov A.N., Marimuthu A., RA Nguyen H., Will S., Signaevsky M., Kral J., Cantwell J., Settachatgull C., RA Yan D.S., Fong D., Oh A., Shi S., Womack P., Powell B., Habets G., RA West B.L., Zhang K.Y.J., Milburn M.V., Vlasuk G.P., Hirth K.P., Nolop K., RA Bollag G., Ibrahim P.N., Tobin J.F.; RT "Scaffold-based discovery of indeglitazar, a PPAR pan-active anti-diabetic RT 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 structure of the C4-type zinc finger domain from human peroxisome RT proliferator-activated receptor delta."; RL Submitted (APR-2008) to the PDB data bank. CC -!- FUNCTION: Ligand-activated transcription factor. Receptor that binds CC peroxisome proliferators such as hypolipidemic drugs and fatty acids. CC Has a preference for poly-unsaturated fatty acids, such as gamma- CC linoleic acid and eicosapentanoic acid. Once activated by a ligand, the CC receptor binds to promoter elements of target genes. Regulates the CC peroxisomal beta-oxidation pathway of fatty acids. Functions as CC transcription activator for the acyl-CoA oxidase gene. Decreases CC expression of NPC1L1 once activated by a ligand. CC {ECO:0000269|PubMed:1333051, ECO:0000269|PubMed:15604518}. CC -!- SUBUNIT: Heterodimer with the retinoid X receptor. Interacts (via CC domain NR LBD) with CRY1 and CRY2 in a ligand-dependent manner (By CC similarity). {ECO:0000250|UniProtKB:P35396, CC ECO:0000269|PubMed:10809235, ECO:0000269|PubMed:16405912, CC ECO:0000269|PubMed:16931011, ECO:0000269|PubMed:17560785, CC ECO:0000269|PubMed:19116277, ECO:0000269|PubMed:19464171}. CC -!- INTERACTION: CC Q03181; O60341: KDM1A; NbExp=2; IntAct=EBI-6426768, EBI-710124; CC Q03181; P55055-1: NR1H2; NbExp=2; IntAct=EBI-6426768, EBI-21458417; CC Q03181; Q13133: NR1H3; NbExp=2; IntAct=EBI-6426768, EBI-781356; CC Q03181-2; P42858: HTT; NbExp=3; IntAct=EBI-10223258, EBI-466029; CC Q03181-2; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-10223258, EBI-10172290; CC Q03181-2; P02545: LMNA; NbExp=3; IntAct=EBI-10223258, EBI-351935; CC Q03181-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-10223258, EBI-5235340; CC Q03181-2; Q96EG3: ZNF837; NbExp=3; IntAct=EBI-10223258, EBI-11962574; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q03181-1; Sequence=Displayed; CC Name=2; CC IsoId=Q03181-2; Sequence=VSP_010133, VSP_010134; CC Name=3; CC IsoId=Q03181-3; Sequence=VSP_043787; CC Name=4; CC IsoId=Q03181-4; Sequence=VSP_046104; 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. {ECO:0000305}. CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/ppard/"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Peroxisome proliferator-activated CC receptor entry; CC URL="https://en.wikipedia.org/wiki/Peroxisome_proliferator-activated_receptor"; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/PPARDID41794ch6p21.html"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) 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; AK296425; BAH12347.1; -; mRNA. DR EMBL; AK304878; BAG65615.1; -; mRNA. DR EMBL; AK122614; BAG53624.1; -; mRNA. DR EMBL; AY442342; AAR05439.1; -; Genomic_DNA. DR EMBL; AL022721; -; NOT_ANNOTATED_CDS; 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 CCDS; CCDS4803.1; -. [Q03181-1] DR CCDS; CCDS4804.1; -. [Q03181-2] DR CCDS; CCDS54994.1; -. [Q03181-3] DR CCDS; CCDS54995.1; -. [Q03181-4] DR PIR; A45360; A45360. DR RefSeq; NP_001165289.1; NM_001171818.1. [Q03181-1] DR RefSeq; NP_001165290.1; NM_001171819.1. [Q03181-3] DR RefSeq; NP_001165291.1; NM_001171820.1. [Q03181-4] DR RefSeq; NP_006229.1; NM_006238.4. [Q03181-1] DR RefSeq; NP_803184.1; NM_177435.2. [Q03181-2] DR RefSeq; XP_005249250.1; XM_005249193.1. [Q03181-1] DR RefSeq; XP_006715183.1; XM_006715120.1. [Q03181-1] DR RefSeq; XP_006715186.1; XM_006715123.1. [Q03181-1] DR RefSeq; XP_011513009.1; XM_011514707.1. [Q03181-1] DR RefSeq; XP_011513011.1; XM_011514709.1. DR RefSeq; XP_011513012.1; XM_011514710.1. [Q03181-1] DR RefSeq; XP_016866460.1; XM_017010971.1. DR RefSeq; XP_016866461.1; XM_017010972.1. [Q03181-1] DR RefSeq; XP_016866462.1; XM_017010973.1. [Q03181-1] DR RefSeq; XP_016866463.1; XM_017010974.1. [Q03181-1] 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; 2XYJ; X-ray; 2.30 A; A/B=165-441. DR PDB; 2XYW; X-ray; 3.14 A; A/B=165-441. DR PDB; 2XYX; 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 PDB; 3OZ0; X-ray; 3.00 A; A=165-441. DR PDB; 3PEQ; X-ray; 2.40 A; A/B=171-441. DR PDB; 3SP9; X-ray; 2.30 A; A/B=173-441. DR PDB; 3TKM; X-ray; 1.95 A; A=171-441. DR PDB; 5U3Q; X-ray; 1.50 A; A/B=170-441. DR PDB; 5U3R; X-ray; 1.95 A; A/B=170-441. DR PDB; 5U3S; X-ray; 2.00 A; A/B=170-441. DR PDB; 5U3T; X-ray; 1.70 A; A/B=170-441. DR PDB; 5U3U; X-ray; 2.10 A; A/B=170-441. DR PDB; 5U3V; X-ray; 1.84 A; A/B=170-441. DR PDB; 5U3W; X-ray; 1.80 A; A/B=170-441. DR PDB; 5U3X; X-ray; 2.10 A; A/B=170-441. DR PDB; 5U3Y; X-ray; 1.90 A; A/B=170-441. DR PDB; 5U3Z; X-ray; 1.72 A; A/B=170-441. DR PDB; 5U40; X-ray; 2.00 A; A/B=170-441. DR PDB; 5U41; X-ray; 1.90 A; A/B=170-441. DR PDB; 5U42; X-ray; 1.70 A; A/B=170-441. DR PDB; 5U43; X-ray; 1.90 A; A/B=170-441. DR PDB; 5U44; X-ray; 2.15 A; A/B=170-441. DR PDB; 5U45; X-ray; 1.95 A; A/B=170-441. DR PDB; 5U46; X-ray; 2.00 A; A/B=170-441. DR PDB; 5XMX; X-ray; 2.00 A; A/B=171-441. DR PDB; 5Y7X; X-ray; 1.70 A; A/B=171-441. DR PDB; 5ZXI; X-ray; 2.10 A; A/B=171-441. DR PDB; 6A6P; X-ray; 2.10 A; A/B=171-440. 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; 2XYJ; -. DR PDBsum; 2XYW; -. DR PDBsum; 2XYX; -. DR PDBsum; 2ZNP; -. DR PDBsum; 2ZNQ; -. DR PDBsum; 3D5F; -. DR PDBsum; 3DY6; -. DR PDBsum; 3ET2; -. DR PDBsum; 3GWX; -. DR PDBsum; 3GZ9; -. DR PDBsum; 3OZ0; -. DR PDBsum; 3PEQ; -. DR PDBsum; 3SP9; -. DR PDBsum; 3TKM; -. DR PDBsum; 5U3Q; -. DR PDBsum; 5U3R; -. DR PDBsum; 5U3S; -. DR PDBsum; 5U3T; -. DR PDBsum; 5U3U; -. DR PDBsum; 5U3V; -. DR PDBsum; 5U3W; -. DR PDBsum; 5U3X; -. DR PDBsum; 5U3Y; -. DR PDBsum; 5U3Z; -. DR PDBsum; 5U40; -. DR PDBsum; 5U41; -. DR PDBsum; 5U42; -. DR PDBsum; 5U43; -. DR PDBsum; 5U44; -. DR PDBsum; 5U45; -. DR PDBsum; 5U46; -. DR PDBsum; 5XMX; -. DR PDBsum; 5Y7X; -. DR PDBsum; 5ZXI; -. DR PDBsum; 6A6P; -. DR AlphaFoldDB; Q03181; -. DR SMR; Q03181; -. DR BioGRID; 111463; 128. DR IntAct; Q03181; 24. DR MINT; Q03181; -. DR STRING; 9606.ENSP00000310928; -. DR BindingDB; Q03181; -. DR ChEMBL; CHEMBL3979; -. DR DrugBank; DB07070; (2S)-2-{3-[({[2-fluoro-4-(trifluoromethyl)phenyl]carbonyl}amino)methyl]-4-methoxybenzyl}butanoic acid. DR DrugBank; DB07691; 2-({[3-(3,4-dihydroisoquinolin-2(1H)-ylsulfonyl)phenyl]carbonyl}amino)benzoic acid. DR DrugBank; DB00132; alpha-Linolenic acid. DR DrugBank; DB01393; Bezafibrate. DR DrugBank; DB05416; Cardarine. DR DrugBank; DB04801; cis-Vaccenic acid. DR DrugBank; DB09006; Clinofibrate. DR DrugBank; DB05187; Elafibranor. DR DrugBank; DB13873; Fenofibric acid. DR DrugBank; DB13961; Fish oil. DR DrugBank; DB09462; Glycerin. DR DrugBank; DB03338; Heptyl glucoside. DR DrugBank; DB00159; Icosapent. DR DrugBank; DB07724; Indeglitazar. DR DrugBank; DB05188; KD3010. DR DrugBank; DB04224; Oleic Acid. DR DrugBank; DB02746; Phthalic Acid. DR DrugBank; DB00412; Rosiglitazone. DR DrugBank; DB00605; Sulindac. DR DrugBank; DB00374; Treprostinil. DR DrugBank; DB00197; Troglitazone. DR DrugBank; DB00313; Valproic acid. DR DrugBank; DB08078; {4-[3-(4-acetyl-3-hydroxy-2-propylphenoxy)propoxy]phenoxy}acetic acid. DR DrugCentral; Q03181; -. DR GuidetoPHARMACOLOGY; 594; -. DR SwissLipids; SLP:000001645; -. DR iPTMnet; Q03181; -. DR PhosphoSitePlus; Q03181; -. DR BioMuta; PPARD; -. DR DMDM; 417522; -. DR EPD; Q03181; -. DR jPOST; Q03181; -. DR MassIVE; Q03181; -. DR MaxQB; Q03181; -. DR PaxDb; Q03181; -. DR PeptideAtlas; Q03181; -. DR PRIDE; Q03181; -. DR ProteomicsDB; 19792; -. DR ProteomicsDB; 58200; -. [Q03181-1] DR ProteomicsDB; 58201; -. [Q03181-2] DR ProteomicsDB; 58202; -. [Q03181-3] DR Antibodypedia; 4322; 635 antibodies from 43 providers. DR DNASU; 5467; -. DR Ensembl; ENST00000311565.4; ENSP00000310928.4; ENSG00000112033.14. DR Ensembl; ENST00000337400.6; ENSP00000337063.2; ENSG00000112033.14. [Q03181-2] DR Ensembl; ENST00000360694.8; ENSP00000353916.3; ENSG00000112033.14. DR Ensembl; ENST00000418635.6; ENSP00000413314.2; ENSG00000112033.14. [Q03181-4] DR Ensembl; ENST00000448077.6; ENSP00000414372.2; ENSG00000112033.14. [Q03181-3] DR GeneID; 5467; -. DR KEGG; hsa:5467; -. DR MANE-Select; ENST00000360694.8; ENSP00000353916.3; NM_006238.5; NP_006229.1. DR UCSC; uc003okm.3; human. [Q03181-1] DR CTD; 5467; -. DR DisGeNET; 5467; -. DR GeneCards; PPARD; -. DR HGNC; HGNC:9235; PPARD. DR HPA; ENSG00000112033; Low tissue specificity. DR MIM; 600409; gene. DR neXtProt; NX_Q03181; -. DR OpenTargets; ENSG00000112033; -. DR PharmGKB; PA33557; -. DR VEuPathDB; HostDB:ENSG00000112033; -. DR eggNOG; KOG3575; Eukaryota. DR GeneTree; ENSGT00940000156676; -. DR HOGENOM; CLU_007368_4_0_1; -. DR InParanoid; Q03181; -. DR OMA; RVNGYCE; -. DR PhylomeDB; Q03181; -. DR TreeFam; TF316304; -. DR PathwayCommons; Q03181; -. DR Reactome; R-HSA-200425; Carnitine metabolism. DR Reactome; R-HSA-204174; Regulation of pyruvate dehydrogenase (PDH) complex. DR Reactome; R-HSA-383280; Nuclear Receptor transcription pathway. DR Reactome; R-HSA-5362517; Signaling by Retinoic Acid. DR SignaLink; Q03181; -. DR SIGNOR; Q03181; -. DR BioGRID-ORCS; 5467; 12 hits in 1106 CRISPR screens. DR ChiTaRS; PPARD; human. DR EvolutionaryTrace; Q03181; -. DR GeneWiki; Peroxisome_proliferator-activated_receptor_delta; -. DR GenomeRNAi; 5467; -. DR Pharos; Q03181; Tchem. DR PRO; PR:Q03181; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q03181; protein. DR Bgee; ENSG00000112033; Expressed in vagina and 236 other tissues. DR ExpressionAtlas; Q03181; baseline and differential. DR Genevisible; Q03181; HS. DR GO; GO:0000785; C:chromatin; ISS:BHF-UCL. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; NAS:UniProtKB. DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB. DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISS:BHF-UCL. DR GO; GO:0070539; F:linoleic acid binding; IDA:UniProtKB. DR GO; GO:0008289; F:lipid binding; IDA:UniProtKB. DR GO; GO:0051059; F:NF-kappaB binding; IEA:Ensembl. DR GO; GO:0004879; F:nuclear receptor activity; IDA:UniProtKB. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL. DR GO; GO:0003707; F:steroid hormone receptor activity; TAS:ProtInc. DR GO; GO:0001223; F:transcription coactivator binding; IPI:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0060612; P:adipose tissue development; IEA:Ensembl. DR GO; GO:0006915; P:apoptotic process; IMP:CACAO. DR GO; GO:0097190; P:apoptotic signaling pathway; IMP:UniProtKB. DR GO; GO:0008366; P:axon ensheathment; ISS:UniProtKB. DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central. DR GO; GO:0008283; P:cell population proliferation; ISS:UniProtKB. DR GO; GO:0031589; P:cell-substrate adhesion; IEA:Ensembl. DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl. 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; ISS:UniProtKB. DR GO; GO:0009062; P:fatty acid catabolic process; TAS:UniProtKB. DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central. 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:1904659; P:glucose transmembrane transport; NAS:UniProtKB. DR GO; GO:0007507; P:heart development; IEA:Ensembl. DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central. DR GO; GO:0051546; P:keratinocyte migration; IEA:Ensembl. DR GO; GO:0043616; P:keratinocyte proliferation; IEA:Ensembl. DR GO; GO:0006629; P:lipid metabolic process; ISS:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl. DR GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl. DR GO; GO:0010887; P:negative regulation of cholesterol storage; IBA:GO_Central. DR GO; GO:0032966; P:negative regulation of collagen biosynthetic process; IEA:Ensembl. DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl. DR GO; GO:0050728; P:negative regulation of inflammatory response; IBA:GO_Central. DR GO; GO:1902894; P:negative regulation of miRNA transcription; ISS:BHF-UCL. DR GO; GO:0045662; P:negative regulation of myoblast differentiation; IEA:Ensembl. DR GO; GO:0014912; P:negative regulation of smooth muscle cell migration; IEA:Ensembl. DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IEA:Ensembl. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB. DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:Ensembl. DR GO; GO:0045684; P:positive regulation of epidermis development; IEA:Ensembl. DR GO; GO:0045600; P:positive regulation of fat cell differentiation; NAS:UniProtKB. DR GO; GO:0045923; P:positive regulation of fatty acid metabolic process; IBA:GO_Central. DR GO; GO:0046321; P:positive regulation of fatty acid oxidation; IEA:Ensembl. DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl. DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl. DR GO; GO:2000288; P:positive regulation of myoblast proliferation; IEA:Ensembl. DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl. DR GO; GO:0043415; P:positive regulation of skeletal muscle tissue regeneration; IEA:Ensembl. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB. DR GO; GO:0006029; P:proteoglycan metabolic process; IEA:Ensembl. DR GO; GO:0019216; P:regulation of lipid metabolic process; IBA:GO_Central. DR GO; GO:0014842; P:regulation of skeletal muscle satellite cell proliferation; IEA:Ensembl. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:ProtInc. DR GO; GO:0014823; P:response to activity; IEA:Ensembl. DR GO; GO:0009749; P:response to glucose; IEA:Ensembl. DR GO; GO:0033993; P:response to lipid; IBA:GO_Central. DR GO; GO:0033189; P:response to vitamin A; IEA:Ensembl. DR GO; GO:0042311; P:vasodilation; IEA:Ensembl. DR GO; GO:0006776; P:vitamin A metabolic process; IEA:Ensembl. DR GO; GO:0042060; P:wound healing; IEA:Ensembl. DR Gene3D; 1.10.565.10; -; 1. DR Gene3D; 3.30.50.10; -; 1. DR InterPro; IPR003074; 1Cnucl_rcpt. DR InterPro; IPR003075; 1Cnucl_rcpt_B. DR InterPro; IPR035500; NHR-like_dom_sf. DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd. DR InterPro; IPR001723; Nuclear_hrmn_rcpt. DR InterPro; IPR001628; Znf_hrmn_rcpt. DR InterPro; IPR013088; Znf_NHR/GATA. 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; SSF48508; 1. DR PROSITE; PS51843; NR_LBD; 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; DNA-binding; Metal-binding; KW Nucleus; Receptor; Reference proteome; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1..441 FT /note="Peroxisome proliferator-activated receptor delta" FT /id="PRO_0000053486" FT DOMAIN 211..439 FT /note="NR LBD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189" FT DNA_BIND 71..145 FT /note="Nuclear receptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407" FT ZN_FING 74..94 FT /note="NR C4-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407" FT ZN_FING 111..133 FT /note="NR C4-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407" FT REGION 1..54 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..22 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 34..54 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 2..43 FT /note="EQPQEEAPEVREEEEKEEVAEAEGAPELNGGPQHALPSSSYT -> HQR FT (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043787" FT VAR_SEQ 44..141 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046104" FT VAR_SEQ 360..361 FT /note="DR -> GE (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_010133" FT VAR_SEQ 362..441 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_010134" FT CONFLICT 79 FT /note="D -> G (in Ref. 5; BAF84350)" FT /evidence="ECO:0000305" FT CONFLICT 134 FT /note="L -> P (in Ref. 3; BAH02282)" FT /evidence="ECO:0000305" FT CONFLICT 191 FT /note="N -> D (in Ref. 5; BAG65615)" FT /evidence="ECO:0000305" FT CONFLICT 217 FT /note="E -> K (in Ref. 5; BAG65615)" FT /evidence="ECO:0000305" FT STRAND 75..77 FT /evidence="ECO:0007829|PDB:2ENV" FT STRAND 83..85 FT /evidence="ECO:0007829|PDB:2ENV" FT STRAND 88..90 FT /evidence="ECO:0007829|PDB:2ENV" FT HELIX 92..103 FT /evidence="ECO:0007829|PDB:2ENV" FT STRAND 122..124 FT /evidence="ECO:0007829|PDB:2ENV" FT HELIX 127..136 FT /evidence="ECO:0007829|PDB:2ENV" FT HELIX 170..174 FT /evidence="ECO:0007829|PDB:2B50" FT HELIX 175..189 FT /evidence="ECO:0007829|PDB:5U3Q" FT HELIX 194..201 FT /evidence="ECO:0007829|PDB:5U3Q" FT STRAND 205..207 FT /evidence="ECO:0007829|PDB:3TKM" FT STRAND 211..213 FT /evidence="ECO:0007829|PDB:5U3Q" FT HELIX 216..225 FT /evidence="ECO:0007829|PDB:5U3Q" FT STRAND 229..231 FT /evidence="ECO:0007829|PDB:1GWX" FT HELIX 232..234 FT /evidence="ECO:0007829|PDB:5U3Q" FT STRAND 235..238 FT /evidence="ECO:0007829|PDB:2GWX" FT HELIX 241..265 FT /evidence="ECO:0007829|PDB:5U3Q" FT HELIX 268..271 FT /evidence="ECO:0007829|PDB:5U3Q" FT HELIX 275..294 FT /evidence="ECO:0007829|PDB:5U3Q" FT HELIX 295..297 FT /evidence="ECO:0007829|PDB:5U3Q" FT STRAND 302..305 FT /evidence="ECO:0007829|PDB:5U3Q" FT TURN 306..309 FT /evidence="ECO:0007829|PDB:5U3Q" FT STRAND 310..313 FT /evidence="ECO:0007829|PDB:5U3Q" FT HELIX 314..318 FT /evidence="ECO:0007829|PDB:5U3Q" FT HELIX 324..339 FT /evidence="ECO:0007829|PDB:5U3Q" FT HELIX 345..356 FT /evidence="ECO:0007829|PDB:5U3Q" FT HELIX 367..388 FT /evidence="ECO:0007829|PDB:5U3Q" FT HELIX 395..423 FT /evidence="ECO:0007829|PDB:5U3Q" FT TURN 424..426 FT /evidence="ECO:0007829|PDB:2ZNQ" FT HELIX 431..437 FT /evidence="ECO:0007829|PDB:5U3Q" 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 //