PPARD_MOUSE
ID PPARD_MOUSE Reviewed; 440 AA.
AC P35396; P37239;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Peroxisome proliferator-activated receptor delta;
DE Short=PPAR-delta;
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Adipocyte;
RX PubMed=7836471; DOI=10.1074/jbc.270.5.2367;
RA Amri E.-Z., Bonino F., Ailhaud G., Abumrad N.A., Grimaldi P.A.;
RT "Cloning of a protein that mediates transcriptional effects of fatty acids
RT in preadipocytes. Homology to peroxisome proliferator-activated
RT receptors.";
RL J. Biol. Chem. 270:2367-2371(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8041794; DOI=10.1073/pnas.91.15.7355;
RA Kliewer S.A., Forman B.M., Blumberg B., Ong E.S., Borgmeyer U.,
RA Mangelsdorf D.J., Umesono K., Evans R.M.;
RT "Differential expression and activation of a family of murine peroxisome
RT proliferator-activated receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:7355-7359(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-145.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=8240342; DOI=10.1006/bbrc.1993.2302;
RA Chen F., Law S.W., O'Malley B.W.;
RT "Identification of two mPPAR related receptors and evidence for the
RT existence of five subfamily members.";
RL Biochem. Biophys. Res. Commun. 196:671-677(1993).
RN [5]
RP INTERACTION WITH CRY1 AND CRY2.
RX PubMed=28683290; DOI=10.1016/j.cmet.2017.06.002;
RA Jordan S.D., Kriebs A., Vaughan M., Duglan D., Fan W., Henriksson E.,
RA Huber A.L., Papp S.J., Nguyen M., Afetian M., Downes M., Yu R.T.,
RA Kralli A., Evans R.M., Lamia K.A.;
RT "CRY1/2 selectively repress PPARdelta and limit exercise capacity.";
RL Cell Metab. 26:243-255(2017).
RN [6]
RP INTERACTION WITH CRY1 AND CRY2.
RX PubMed=28751364; DOI=10.1073/pnas.1704955114;
RA Kriebs A., Jordan S.D., Soto E., Henriksson E., Sandate C.R., Vaughan M.E.,
RA Chan A.B., Duglan D., Papp S.J., Huber A.L., Afetian M.E., Yu R.T.,
RA Zhao X., Downes M., Evans R.M., Lamia K.A.;
RT "Circadian repressors CRY1 and CRY2 broadly interact with nuclear receptors
RT and modulate transcriptional activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:8776-8781(2017).
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 (PubMed:28683290, PubMed:28751364).
CC {ECO:0000250|UniProtKB:Q03181, ECO:0000269|PubMed:28683290,
CC ECO:0000269|PubMed:28751364}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Heart, adrenal and intestine.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA03332.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L28116; AAA63394.1; -; mRNA.
DR EMBL; U10375; AAA19972.1; -; mRNA.
DR EMBL; BC070398; AAH70398.1; -; mRNA.
DR EMBL; U01665; AAA03332.1; ALT_INIT; mRNA.
DR CCDS; CCDS28575.1; -.
DR PIR; I55442; I55442.
DR RefSeq; NP_035275.1; NM_011145.3.
DR AlphaFoldDB; P35396; -.
DR SMR; P35396; -.
DR BioGRID; 202319; 12.
DR DIP; DIP-29851N; -.
DR IntAct; P35396; 6.
DR STRING; 10090.ENSMUSP00000002320; -.
DR BindingDB; P35396; -.
DR ChEMBL; CHEMBL2458; -.
DR SwissLipids; SLP:000000397; -.
DR PhosphoSitePlus; P35396; -.
DR EPD; P35396; -.
DR PaxDb; P35396; -.
DR PRIDE; P35396; -.
DR ProteomicsDB; 291646; -.
DR Antibodypedia; 4322; 645 antibodies from 43 providers.
DR DNASU; 19015; -.
DR Ensembl; ENSMUST00000002320; ENSMUSP00000002320; ENSMUSG00000002250.
DR GeneID; 19015; -.
DR KEGG; mmu:19015; -.
DR UCSC; uc008bqk.1; mouse.
DR CTD; 5467; -.
DR MGI; MGI:101884; Ppard.
DR VEuPathDB; HostDB:ENSMUSG00000002250; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000156676; -.
DR HOGENOM; CLU_007368_4_1_1; -.
DR InParanoid; P35396; -.
DR OMA; RVNGYCE; -.
DR OrthoDB; 1240230at2759; -.
DR PhylomeDB; P35396; -.
DR TreeFam; TF316304; -.
DR Reactome; R-MMU-200425; Carnitine metabolism.
DR Reactome; R-MMU-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
DR Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-MMU-5362517; Signaling by Retinoic Acid.
DR BioGRID-ORCS; 19015; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Ppard; mouse.
DR PRO; PR:P35396; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P35396; protein.
DR Bgee; ENSMUSG00000002250; Expressed in ectoplacental cone and 171 other tissues.
DR ExpressionAtlas; P35396; baseline and differential.
DR Genevisible; P35396; MM.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:BHF-UCL.
DR GO; GO:0008047; F:enzyme activator activity; TAS:UniProtKB.
DR GO; GO:0005504; F:fatty acid binding; ISO:MGI.
DR GO; GO:0070539; F:linoleic acid binding; ISS:UniProtKB.
DR GO; GO:0008289; F:lipid binding; ISS:UniProtKB.
DR GO; GO:0051059; F:NF-kappaB binding; ISO:MGI.
DR GO; GO:0004879; F:nuclear receptor activity; ISS:UniProtKB.
DR GO; GO:0016501; F:prostacyclin receptor activity; TAS: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; ISO:MGI.
DR GO; GO:0001223; F:transcription coactivator binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0060612; P:adipose tissue development; IMP:MGI.
DR GO; GO:0006915; P:apoptotic process; ISO:MGI.
DR GO; GO:0097190; P:apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0008366; P:axon ensheathment; IMP:MGI.
DR GO; GO:0030154; P:cell differentiation; IDA:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0031589; P:cell-substrate adhesion; IMP:MGI.
DR GO; GO:0071456; P:cellular response to hypoxia; IGI:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:MGI.
DR GO; GO:0046697; P:decidualization; IEA:Ensembl.
DR GO; GO:0007566; P:embryo implantation; IDA:MGI.
DR GO; GO:0008544; P:epidermis development; TAS:MGI.
DR GO; GO:0050673; P:epithelial cell proliferation; IGI:MGI.
DR GO; GO:0070341; P:fat cell proliferation; IMP:MGI.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEP:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0019395; P:fatty acid oxidation; ISO:MGI.
DR GO; GO:0015908; P:fatty acid transport; IEP: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; IMP:MGI.
DR GO; GO:0043616; P:keratinocyte proliferation; IMP:MGI.
DR GO; GO:0006629; P:lipid metabolic process; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR GO; GO:0010887; P:negative regulation of cholesterol storage; IBA:GO_Central.
DR GO; GO:0032966; P:negative regulation of collagen biosynthetic process; ISO:MGI.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IGI:MGI.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISO:MGI.
DR GO; GO:1902894; P:negative regulation of miRNA transcription; IDA:BHF-UCL.
DR GO; GO:0045662; P:negative regulation of myoblast differentiation; IMP:CACAO.
DR GO; GO:0014912; P:negative regulation of smooth muscle cell migration; ISO:MGI.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IDA:MGI.
DR GO; GO:0008654; P:phospholipid biosynthetic process; ISO:MGI.
DR GO; GO:0001890; P:placenta development; IMP:MGI.
DR GO; GO:0045684; P:positive regulation of epidermis development; ISO:MGI.
DR GO; GO:0070346; P:positive regulation of fat cell proliferation; IMP:MGI.
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; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:CACAO.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISO:MGI.
DR GO; GO:2000288; P:positive regulation of myoblast proliferation; IMP:CACAO.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:MGI.
DR GO; GO:0043415; P:positive regulation of skeletal muscle tissue regeneration; IMP:CACAO.
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:0006029; P:proteoglycan metabolic process; ISO:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; IGI:MGI.
DR GO; GO:0050678; P:regulation of epithelial cell proliferation; IMP:MGI.
DR GO; GO:0045598; P:regulation of fat cell differentiation; IMP:MGI.
DR GO; GO:0050796; P:regulation of insulin secretion; NAS:UniProtKB.
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; IMP:CACAO.
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; ISO:MGI.
DR GO; GO:0006776; P:vitamin A metabolic process; ISO:MGI.
DR GO; GO:0042060; P:wound healing; IMP:MGI.
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 Activator; DNA-binding; Metal-binding; Nucleus; Receptor;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..440
FT /note="Peroxisome proliferator-activated receptor delta"
FT /id="PRO_0000053487"
FT DOMAIN 210..438
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 70..144
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 73..93
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 110..132
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 149..150
FT /note="EA -> DG (in Ref. 2; AAA19972)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 440 AA; 49715 MW; 58E0F595DD193FDA CRC64;
MEQPQEETPE AREEEKEEVA MGDGAPELNG GPEHTLPSSS CADLSQNSSP SSLLDQLQMG
CDGASGGSLN MECRVCGDKA SGFHYGVHAC EGCKGFFRRT IRMKLEYEKC DRICKIQKKN
RNKCQYCRFQ KCLALGMSHN AIRFGRMPEA EKRKLVAGLT ASEGCQHNPQ LADLKAFSKH
IYNAYLKNFN MTKKKARSIL TGKSSHNAPF VIHDIETLWQ AEKGLVWKQL VNGLPPYNEI
SVHVFYRCQS TTVETVRELT EFAKNIPNFS SLFLNDQVTL LKYGVHEAIF AMLASIVNKD
GLLVANGSGF VTHEFLRSLR KPFSDIIEPK FEFAVKFNAL ELDDSDLALF IAAIILCGDR
PGLMNVPQVE AIQDTILRAL EFHLQVNHPD SQYLFPKLLQ KMADLRQLVT EHAQMMQWLK
KTESETLLHP LLQEIYKDMY
