PPARD_HUMAN
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 03-AUG-2022, entry version 244.
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";
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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 PDB; 7VWE; X-ray; 3.00 A; A/B=170-441.
DR PDB; 7VWF; X-ray; 1.90 A; A/B=170-441.
DR PDB; 7VWG; X-ray; 2.20 A; A/B=170-441.
DR PDB; 7VWH; X-ray; 2.10 A; A/B=170-441.
DR PDB; 7W0G; X-ray; 2.44 A; A/B=173-441.
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 PDBsum; 7VWE; -.
DR PDBsum; 7VWF; -.
DR PDBsum; 7VWG; -.
DR PDBsum; 7VWH; -.
DR PDBsum; 7W0G; -.
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; 645 antibodies from 43 providers.
DR DNASU; 5467; -.
DR Ensembl; ENST00000311565.4; ENSP00000310928.4; ENSG00000112033.14. [Q03181-1]
DR Ensembl; ENST00000337400.6; ENSP00000337063.2; ENSG00000112033.14. [Q03181-2]
DR Ensembl; ENST00000360694.8; ENSP00000353916.3; ENSG00000112033.14. [Q03181-1]
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 lower esophagus mucosa and 188 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:0003707; F:nuclear steroid receptor activity; TAS:ProtInc.
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: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:0070341; P:fat cell proliferation; IEA:Ensembl.
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:0014065; P:phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
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:0070346; P:positive regulation of fat cell proliferation; IEA:Ensembl.
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
