ID   PPARD_CANLF             Reviewed;         441 AA.
AC   Q0ZAQ8;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Peroxisome proliferator-activated receptor delta;
DE            Short=PPAR-delta;
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   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Nishii N., Takasu M., Soe O., Maeda S., Ohba Y., Kitagawa H.;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer with the retinoid X receptor (By similarity).
CC       Interacts (via domain NR LBD) with CRY1 and CRY2 in a ligand-dependent
CC       manner (By similarity). {ECO:0000250|UniProtKB:P35396,
CC       ECO:0000250|UniProtKB:Q03181}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; DQ648277; ABG36929.1; -; mRNA.
DR   RefSeq; NP_001041567.1; NM_001048102.1.
DR   RefSeq; XP_005627131.1; XM_005627074.2.
DR   RefSeq; XP_005627132.1; XM_005627075.2.
DR   RefSeq; XP_005627134.1; XM_005627077.2.
DR   AlphaFoldDB; Q0ZAQ8; -.
DR   SMR; Q0ZAQ8; -.
DR   STRING; 9615.ENSCAFP00000052536; -.
DR   BindingDB; Q0ZAQ8; -.
DR   ChEMBL; CHEMBL1932904; -.
DR   PaxDb; Q0ZAQ8; -.
DR   PRIDE; Q0ZAQ8; -.
DR   Ensembl; ENSCAFT00030028553; ENSCAFP00030024904; ENSCAFG00030015370.
DR   Ensembl; ENSCAFT00040029299; ENSCAFP00040025452; ENSCAFG00040015805.
DR   GeneID; 481756; -.
DR   KEGG; cfa:481756; -.
DR   CTD; 5467; -.
DR   eggNOG; KOG3575; Eukaryota.
DR   HOGENOM; CLU_007368_4_1_1; -.
DR   InParanoid; Q0ZAQ8; -.
DR   OMA; RVNGYCE; -.
DR   OrthoDB; 1240230at2759; -.
DR   TreeFam; TF316304; -.
DR   Reactome; R-CFA-200425; Carnitine metabolism.
DR   Reactome; R-CFA-383280; Nuclear Receptor transcription pathway.
DR   Reactome; R-CFA-5362517; Signaling by Retinoic Acid.
DR   PRO; PR:Q0ZAQ8; -.
DR   Proteomes; UP000002254; Unplaced.
DR   Bgee; ENSCAFG00000001310; Expressed in placenta and 47 other tissues.
DR   GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:Ensembl.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0070539; F:linoleic acid binding; ISS:UniProtKB.
DR   GO; GO:0008289; F:lipid binding; ISS:UniProtKB.
DR   GO; GO:0004879; F:nuclear receptor activity; ISS:UniProtKB.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0001223; F:transcription coactivator binding; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0060612; P:adipose tissue development; IEA:Ensembl.
DR   GO; GO:0097190; P:apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:0008366; P:axon ensheathment; IEA:Ensembl.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0031589; P:cell-substrate adhesion; IEA:Ensembl.
DR   GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR   GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
DR   GO; GO:0070341; P:fat cell proliferation; IEA:Ensembl.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:Ensembl.
DR   GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR   GO; GO:0015908; P:fatty acid transport; 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:0010887; P:negative regulation of cholesterol storage; IBA:GO_Central.
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; IEA:Ensembl.
DR   GO; GO:0045662; P:negative regulation of myoblast differentiation; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
DR   GO; GO:0001890; P:placenta development; IEA:Ensembl.
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:0010628; P:positive regulation of gene expression; 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; ISS:UniProtKB.
DR   GO; GO:0045598; P:regulation of fat cell differentiation; 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:0033993; P:response to lipid; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Activator; DNA-binding; Metal-binding; Nucleus; Receptor;
KW   Reference proteome; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..441
FT                   /note="Peroxisome proliferator-activated receptor delta"
FT                   /id="PRO_0000250457"
FT   DOMAIN          211..439
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        70..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..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   441 AA;  49776 MW;  901CA84AD41F4FC2 CRC64;
     MEQPPGEAAE VREEEEKKEV AEAEGAPELN GGPERSLPSS SYTDLSRSSS PPSLLDQLQM
     GGDGASCGSL NMECRVCGDK ASGFHYGVHA CEGCKGFFRR TIRMKLEYEK CERICKIQKK
     NRNKCQYCRF QKCVALGMSH NAIRFGRMPE AEKRKLVAGL TANEGTQHNP QVADLKAFSK
     HIYNAYLKNF NMTKKKARGI LTGKASHTAP FVIHDIETLW QAEKGLVWKQ LVNGLPPYKE
     ISVHVFYRCQ CTTVETVREL TEFAKSIPSF SNLFLNDQVT LLKYGVHEAI FAMLASIVNK
     DGLLVANGTG FVTREFLRSL RKPFSDIIEP KFEFAVKFNA LELDDSDLAL FIAAIILCGD
     RPGLINVPQV EAIQDTILRA LEFHLQANHP YAQYLFPKLL QKMADLRQLV TEHAQMMQRI
     KKTETETSLH PLLQEIYKDM Y