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P35396 (PPARD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Ppard
Synonyms:Nr1c2, Pparb
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length440 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Subunit structure

Heterodimer with the retinoid X receptor.

Subcellular location

Nucleus.

Tissue specificity

Heart, adrenal and intestine.

Sequence similarities

Belongs to the nuclear hormone receptor family. NR1 subfamily.

Contains 1 nuclear receptor DNA-binding domain.

Sequence caution

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

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
Receptor
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processadipose tissue development

Inferred from mutant phenotype. Source: MGI

anagen

Inferred from mutant phenotype. Source: MGI

axon ensheathment

Inferred from mutant phenotype. Source: MGI

cell differentiation

Inferred from direct assay. Source: MGI

cell-substrate adhesion

Inferred from mutant phenotype. Source: MGI

embryo implantation

Traceable author statement. Source: UniProtKB

fatty acid beta-oxidation

Inferred from expression pattern. Source: UniProtKB

fatty acid transport

Inferred from expression pattern. Source: UniProtKB

keratinocyte migration

Inferred from mutant phenotype. Source: MGI

keratinocyte proliferation

Inferred from mutant phenotype. Source: MGI

negative regulation of epithelial cell proliferation

Inferred from genetic interaction. Source: MGI

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.2. Source: MGI

placenta development

Inferred from mutant phenotype. Source: MGI

positive regulation of cell proliferation

Inferred from mutant phenotype. Source: MGI

positive regulation of phosphatidylinositol 3-kinase cascade

Inferred from direct assay. Source: MGI

positive regulation of transcription, DNA-dependent

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of fat cell differentiation

Inferred from mutant phenotype. Source: MGI

regulation of insulin secretion

Non-traceable author statement. Source: UniProtKB

transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

wound healing

Inferred from mutant phenotype. Source: MGI

   Cellular componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiondrug binding

Inferred from sequence or structural similarity. Source: UniProtKB

enzyme activator activity

Traceable author statement. Source: UniProtKB

linoleic acid binding

Inferred from sequence or structural similarity. Source: UniProtKB

prostacyclin receptor activity

Traceable author statement. Source: UniProtKB

protein heterodimerization activity

Traceable author statement. Source: UniProtKB

retinoid X receptor binding

Traceable author statement. Source: UniProtKB

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

steroid hormone receptor activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 440440Peroxisome proliferator-activated receptor delta
PRO_0000053487

Regions

DNA binding70 – 14475Nuclear receptor
Zinc finger73 – 9321NR C4-type
Zinc finger110 – 13223NR C4-type
Region253 – 440188Ligand-binding Potential

Experimental info

Sequence conflict149 – 1502EA → DG in AAA19972. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P35396 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 58E0F595DD193FDA

FASTA44049,715
        10         20         30         40         50         60 
MEQPQEETPE AREEEKEEVA MGDGAPELNG GPEHTLPSSS CADLSQNSSP SSLLDQLQMG 

        70         80         90        100        110        120 
CDGASGGSLN MECRVCGDKA SGFHYGVHAC EGCKGFFRRT IRMKLEYEKC DRICKIQKKN 

       130        140        150        160        170        180 
RNKCQYCRFQ KCLALGMSHN AIRFGRMPEA EKRKLVAGLT ASEGCQHNPQ LADLKAFSKH 

       190        200        210        220        230        240 
IYNAYLKNFN MTKKKARSIL TGKSSHNAPF VIHDIETLWQ AEKGLVWKQL VNGLPPYNEI 

       250        260        270        280        290        300 
SVHVFYRCQS TTVETVRELT EFAKNIPNFS SLFLNDQVTL LKYGVHEAIF AMLASIVNKD 

       310        320        330        340        350        360 
GLLVANGSGF VTHEFLRSLR KPFSDIIEPK FEFAVKFNAL ELDDSDLALF IAAIILCGDR 

       370        380        390        400        410        420 
PGLMNVPQVE AIQDTILRAL EFHLQVNHPD SQYLFPKLLQ KMADLRQLVT EHAQMMQWLK 

       430        440 
KTESETLLHP LLQEIYKDMY 

« Hide

References

« Hide 'large scale' references
[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(1995) [PubMed: 7836471] [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(1994) [PubMed: 8041794] [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(2004) [PubMed: 15489334] [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(1993) [PubMed: 8240342] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-145.
Strain: BALB/c.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L28116 mRNA. Translation: AAA63394.1.
U10375 mRNA. Translation: AAA19972.1.
BC070398 mRNA. Translation: AAH70398.1.
U01665 mRNA. Translation: AAA03332.1. Different initiation.
IPIIPI00271799.
PIRI55442.
RefSeqNP_035275.1. NM_011145.3.
UniGeneMm.328914.

3D structure databases

ProteinModelPortalP35396.
SMRP35396. Positions 64-440.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-29851N.
IntActP35396. 2 interactions.
STRINGP35396.

PTM databases

PhosphoSiteP35396.

Proteomic databases

PRIDEP35396.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000002320; ENSMUSP00000002320; ENSMUSG00000002250.
GeneID19015.
KEGGmmu:19015.

Organism-specific databases

CTD5467.
MGIMGI:101884. Ppard.

Phylogenomic databases

eggNOGroNOG14696.
HOGENOMHBG446936.
HOVERGENHBG106004.
InParanoidP35396.
OMASSLFLND.
OrthoDBEOG4FFD1Q.
PhylomeDBP35396.

Gene expression databases

ArrayExpressP35396.
BgeeP35396.
CleanExMM_PPARD.
GenevestigatorP35396.
GermOnlineENSMUSG00000002250. Mus musculus.

Family and domain databases

InterProIPR003074. 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]
Gene3DG3DSA:1.10.565.10. Nucl_hrmn_rcpt_lig_bd. 2 hits.
G3DSA:3.30.50.10. Znf_NHR/GATA. 1 hit.
KOK04504.
PfamPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSPR01288. PROXISOMEPAR.
PR01290. PROXISOMPABR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMSSF48508. Str_ncl_receptor. 1 hit.
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio295440.
SOURCESearch...

Entry information

Entry namePPARD_MOUSE
AccessionPrimary (citable) accession number: P35396
Secondary accession number(s): P37239
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: December 14, 2011
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families