Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Peroxisome proliferator-activated receptor delta

Gene

Ppard

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Ligand-activated transcription factor. Receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Has a preference for poly-unsaturated fatty acids, such as gamma-linoleic acid and eicosapentanoic acid. Once activated by a ligand, the receptor binds to promoter elements of target genes. Regulates the peroxisomal beta-oxidation pathway of fatty acids. Functions as transcription activator for the acyl-CoA oxidase gene. Decreases expression of NPC1L1 once activated by a ligand (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi70 – 14475Nuclear receptorPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri73 – 9321NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri110 – 13223NR C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: MGI
  2. drug binding Source: UniProtKB
  3. enzyme activator activity Source: UniProtKB
  4. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: UniProtKB
  5. linoleic acid binding Source: UniProtKB
  6. lipid binding Source: UniProtKB
  7. prostacyclin receptor activity Source: UniProtKB
  8. protein heterodimerization activity Source: UniProtKB
  9. retinoid X receptor binding Source: UniProtKB
  10. sequence-specific DNA binding Source: InterPro
  11. sequence-specific DNA binding transcription factor activity Source: MGI
  12. steroid hormone receptor activity Source: InterPro
  13. transcription coactivator activity Source: Ensembl
  14. zinc ion binding Source: InterPro

GO - Biological processi

  1. adipose tissue development Source: MGI
  2. apoptotic signaling pathway Source: MGI
  3. axon ensheathment Source: MGI
  4. cell differentiation Source: MGI
  5. cell proliferation Source: MGI
  6. cell-substrate adhesion Source: MGI
  7. cellular process Source: MGI
  8. cellular response to hypoxia Source: MGI
  9. decidualization Source: Ensembl
  10. embryo implantation Source: UniProtKB
  11. epidermis development Source: MGI
  12. fatty acid beta-oxidation Source: UniProtKB
  13. fatty acid transport Source: UniProtKB
  14. G-protein coupled receptor signaling pathway Source: GOC
  15. heart development Source: Ensembl
  16. intracellular receptor signaling pathway Source: MGI
  17. keratinocyte migration Source: MGI
  18. keratinocyte proliferation Source: MGI
  19. lipid metabolic process Source: MGI
  20. mRNA transcription Source: Ensembl
  21. negative regulation of apoptotic process Source: Ensembl
  22. negative regulation of cell growth Source: Ensembl
  23. negative regulation of collagen biosynthetic process Source: Ensembl
  24. negative regulation of epithelial cell proliferation Source: MGI
  25. negative regulation of inflammatory response Source: Ensembl
  26. negative regulation of smooth muscle cell migration Source: Ensembl
  27. negative regulation of smooth muscle cell proliferation Source: Ensembl
  28. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  29. phospholipid biosynthetic process Source: Ensembl
  30. placenta development Source: MGI
  31. positive regulation of catalytic activity Source: GOC
  32. positive regulation of cell proliferation Source: MGI
  33. positive regulation of epidermis development Source: Ensembl
  34. positive regulation of insulin secretion Source: Ensembl
  35. positive regulation of phosphatidylinositol 3-kinase signaling Source: MGI
  36. positive regulation of transcription, DNA-templated Source: UniProtKB
  37. positive regulation of vasodilation Source: Ensembl
  38. proteoglycan metabolic process Source: Ensembl
  39. regulation of cell proliferation Source: MGI
  40. regulation of fat cell differentiation Source: MGI
  41. regulation of insulin secretion Source: UniProtKB
  42. response to activity Source: Ensembl
  43. response to glucose Source: Ensembl
  44. response to vitamin A Source: Ensembl
  45. vitamin A metabolic process Source: Ensembl
  46. wound healing Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Activator, Receptor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_276696. Nuclear Receptor transcription pathway.
REACT_278177. Regulation of pyruvate dehydrogenase (PDH) complex.
REACT_293784. Import of palmitoyl-CoA into the mitochondrial matrix.
REACT_306383. Signaling by Retinoic Acid.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisome proliferator-activated receptor delta
Short name:
PPAR-delta
Alternative name(s):
Nuclear hormone receptor 1
Short name:
NUC1
Nuclear receptor subfamily 1 group C member 2
Peroxisome proliferator-activated receptor beta
Short name:
PPAR-beta
Gene namesi
Name:Ppard
Synonyms:Nr1c2, Pparb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:101884. Ppard.

Subcellular locationi

GO - Cellular componenti

  1. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 440440Peroxisome proliferator-activated receptor deltaPRO_0000053487Add
BLAST

Proteomic databases

PRIDEiP35396.

PTM databases

PhosphoSiteiP35396.

Expressioni

Tissue specificityi

Heart, adrenal and intestine.

Gene expression databases

BgeeiP35396.
CleanExiMM_PPARD.
ExpressionAtlasiP35396. baseline and differential.
GenevestigatoriP35396.

Interactioni

Subunit structurei

Heterodimer with the retinoid X receptor.

Protein-protein interaction databases

BioGridi202319. 12 interactions.
DIPiDIP-29851N.
IntActiP35396. 3 interactions.

Structurei

3D structure databases

ProteinModelPortaliP35396.
SMRiP35396. Positions 64-440.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni253 – 440188Ligand-bindingSequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri73 – 9321NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri110 – 13223NR C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG266867.
HOGENOMiHOG000261626.
HOVERGENiHBG106004.
InParanoidiP35396.
KOiK04504.
OMAiMNVPQVE.
OrthoDBiEOG7X9G7F.
PhylomeDBiP35396.
TreeFamiTF316304.

Family and domain databases

Gene3Di1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProiIPR003074. 1Cnucl_rcpt.
IPR003075. 1Cnucl_rcpt_B.
IPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamiPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR01288. PROXISOMEPAR.
PR01290. PROXISOMPABR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 1 hit.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P35396-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEQPQEETPE AREEEKEEVA MGDGAPELNG GPEHTLPSSS CADLSQNSSP
60 70 80 90 100
SSLLDQLQMG CDGASGGSLN MECRVCGDKA SGFHYGVHAC EGCKGFFRRT
110 120 130 140 150
IRMKLEYEKC DRICKIQKKN RNKCQYCRFQ KCLALGMSHN AIRFGRMPEA
160 170 180 190 200
EKRKLVAGLT ASEGCQHNPQ LADLKAFSKH IYNAYLKNFN MTKKKARSIL
210 220 230 240 250
TGKSSHNAPF VIHDIETLWQ AEKGLVWKQL VNGLPPYNEI SVHVFYRCQS
260 270 280 290 300
TTVETVRELT EFAKNIPNFS SLFLNDQVTL LKYGVHEAIF AMLASIVNKD
310 320 330 340 350
GLLVANGSGF VTHEFLRSLR KPFSDIIEPK FEFAVKFNAL ELDDSDLALF
360 370 380 390 400
IAAIILCGDR PGLMNVPQVE AIQDTILRAL EFHLQVNHPD SQYLFPKLLQ
410 420 430 440
KMADLRQLVT EHAQMMQWLK KTESETLLHP LLQEIYKDMY
Length:440
Mass (Da):49,715
Last modified:May 31, 1994 - v1
Checksum:i58E0F595DD193FDA
GO

Sequence cautioni

The sequence AAA03332.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti149 – 1502EA → DG in AAA19972 (PubMed:8041794).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L28116 mRNA. Translation: AAA63394.1.
U10375 mRNA. Translation: AAA19972.1.
BC070398 mRNA. Translation: AAH70398.1.
U01665 mRNA. Translation: AAA03332.1. Different initiation.
CCDSiCCDS28575.1.
PIRiI55442.
RefSeqiNP_035275.1. NM_011145.3.
XP_006523922.1. XM_006523859.1.
XP_006536796.1. XM_006536733.1.
UniGeneiMm.328914.

Genome annotation databases

EnsembliENSMUST00000002320; ENSMUSP00000002320; ENSMUSG00000002250.
GeneIDi19015.
KEGGimmu:19015.
UCSCiuc008bqk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L28116 mRNA. Translation: AAA63394.1.
U10375 mRNA. Translation: AAA19972.1.
BC070398 mRNA. Translation: AAH70398.1.
U01665 mRNA. Translation: AAA03332.1. Different initiation.
CCDSiCCDS28575.1.
PIRiI55442.
RefSeqiNP_035275.1. NM_011145.3.
XP_006523922.1. XM_006523859.1.
XP_006536796.1. XM_006536733.1.
UniGeneiMm.328914.

3D structure databases

ProteinModelPortaliP35396.
SMRiP35396. Positions 64-440.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202319. 12 interactions.
DIPiDIP-29851N.
IntActiP35396. 3 interactions.

Chemistry

BindingDBiP35396.
ChEMBLiCHEMBL2458.

PTM databases

PhosphoSiteiP35396.

Proteomic databases

PRIDEiP35396.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000002320; ENSMUSP00000002320; ENSMUSG00000002250.
GeneIDi19015.
KEGGimmu:19015.
UCSCiuc008bqk.1. mouse.

Organism-specific databases

CTDi5467.
MGIiMGI:101884. Ppard.

Phylogenomic databases

eggNOGiNOG266867.
HOGENOMiHOG000261626.
HOVERGENiHBG106004.
InParanoidiP35396.
KOiK04504.
OMAiMNVPQVE.
OrthoDBiEOG7X9G7F.
PhylomeDBiP35396.
TreeFamiTF316304.

Enzyme and pathway databases

ReactomeiREACT_276696. Nuclear Receptor transcription pathway.
REACT_278177. Regulation of pyruvate dehydrogenase (PDH) complex.
REACT_293784. Import of palmitoyl-CoA into the mitochondrial matrix.
REACT_306383. Signaling by Retinoic Acid.

Miscellaneous databases

NextBioi295440.
PROiP35396.
SOURCEiSearch...

Gene expression databases

BgeeiP35396.
CleanExiMM_PPARD.
ExpressionAtlasiP35396. baseline and differential.
GenevestigatoriP35396.

Family and domain databases

Gene3Di1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProiIPR003074. 1Cnucl_rcpt.
IPR003075. 1Cnucl_rcpt_B.
IPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamiPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR01288. PROXISOMEPAR.
PR01290. PROXISOMPABR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 1 hit.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of a protein that mediates transcriptional effects of fatty acids in preadipocytes. Homology to peroxisome proliferator-activated receptors."
    Amri E.-Z., Bonino F., Ailhaud G., Abumrad N.A., Grimaldi P.A.
    J. Biol. Chem. 270:2367-2371(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
    Tissue: Adipocyte.
  2. "Differential expression and activation of a family of murine peroxisome proliferator-activated receptors."
    Kliewer S.A., Forman B.M., Blumberg B., Ong E.S., Borgmeyer U., Mangelsdorf D.J., Umesono K., Evans R.M.
    Proc. Natl. Acad. Sci. U.S.A. 91:7355-7359(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6.
    Tissue: Brain.
  4. "Identification of two mPPAR related receptors and evidence for the existence of five subfamily members."
    Chen F., Law S.W., O'Malley B.W.
    Biochem. Biophys. Res. Commun. 196:671-677(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-145.
    Strain: BALB/c.
    Tissue: Brain.

Entry informationi

Entry nameiPPARD_MOUSE
AccessioniPrimary (citable) accession number: P35396
Secondary accession number(s): P37239
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 31, 1994
Last sequence update: May 31, 1994
Last modified: March 31, 2015
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.