[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=C57BL/6J; TISSUE=Adipocyte; DOI=10.1074/jbc.270.5.2367; PubMed=7836471 [NCBI, ExPASy, EBI, Israel, Japan] Amri E.-Z., Bonino F., Ailhaud G., Abumrad N.A., Grimaldi P.A.; "Cloning of a protein that mediates transcriptional effects of fatty acids in preadipocytes. Homology to peroxisome proliferator-activated receptors."; J. Biol. Chem. 270:2367-2371(1995).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; PubMed=8041794 [NCBI, ExPASy, EBI, Israel, Japan] Kliewer S.A., Forman B.M., Blumberg B., Ong E.S., Borgmeyer U., Mangelsdorf D.J., Umesono K., Evans R.M.; "Differential expression and activation of a family of murine peroxisome proliferator-activated receptors."; Proc. Natl. Acad. Sci. U.S.A. 91:7355-7359(1994).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=C57BL/6; TISSUE=Brain; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	NUCLEOTIDE SEQUENCE [MRNA] OF 1-145. STRAIN=BALB/c; TISSUE=Brain; DOI=10.1006/bbrc.1993.2302; PubMed=8240342 [NCBI, ExPASy, EBI, Israel, Japan] Chen F., Law S.W., O'Malley B.W.; "Identification of two mPPAR related receptors and evidence for the existence of five subfamily members."; Biochem. Biophys. Res. Commun. 196:671-677(1993).

Comments

FUNCTION: Receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the receptor binds to a promoter element in the gene for acyl-CoA oxidase and activates its transcription. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids.
SUBUNIT: Heterodimer with the retinoid X receptor.
SUBCELLULAR LOCATION: Nucleus.
TISSUE SPECIFICITY: Heart, adrenal and intestine.
SIMILARITY: Belongs to the nuclear hormone receptor family. NR1 subfamily.
SIMILARITY: Contains 1 nuclear receptor DNA-binding domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

L28116; AAA63394.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U10375; AAA19972.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC070398; AAH70398.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U01665; AAA03332.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

I55442; I55442.

NP_035275.1; -.

3D structure databases

HSSP

Q03181; 3GWX. [HSSP ENTRY / PDB]

SMR

P35396; 170-440.

ModBase

P35396.

Organism-specific databases

MGI

MGI:101884; Ppard.

Gene expression databases

ArrayExpress

P35396; -.

CleanEx

MM_PPARD; -.

GermOnline

ENSMUSG00000002250; Mus musculus.

Ontologies

GO:0003677;	Molecular function: DNA binding (inferred from direct assay from MGI).
GO:0008047;	Molecular function: enzyme activator activity (traceable author statement from UniProtKB).
GO:0004879;	Molecular function: ligand-dependent nuclear receptor activity (traceable author statement from MGI).
GO:0016501;	Molecular function: prostacyclin receptor activity (traceable author statement from UniProtKB).
GO:0046982;	Molecular function: protein heterodimerization activity (traceable author statement from UniProtKB).
GO:0046965;	Molecular function: retinoid X receptor binding (traceable author statement from UniProtKB).
GO:0016564;	Molecular function: transcription repressor activity (inferred from direct assay from MGI).
GO:0042640;	Biological process: anagen (inferred from mutant phenotype from MGI).
GO:0008366;	Biological process: axon ensheathment (inferred from mutant phenotype from MGI).
GO:0030154;	Biological process: cell differentiation (inferred from direct assay from MGI).
GO:0031589;	Biological process: cell-substrate adhesion (inferred from mutant phenotype from MGI).
GO:0007566;	Biological process: embryo implantation (traceable author statement from UniProtKB).
GO:0006635;	Biological process: fatty acid beta-oxidation (inferred from expression pattern from UniProtKB).
GO:0015908;	Biological process: fatty acid transport (inferred from expression pattern from UniProtKB).
GO:0051546;	Biological process: keratinocyte migration (inferred from mutant phenotype from MGI).
GO:0043616;	Biological process: keratinocyte proliferation (inferred from mutant phenotype from MGI).
GO:0000122;	Biological process: negative regulation of transcription from RNA polymerase II promoter (inferred from direct assay from MGI).
GO:0014068;	Biological process: positive regulation of phosphoinositide 3-kinase cascade (inferred from direct assay from MGI).
GO:0050796;	Biological process: regulation of insulin secretion (non-traceable author statement from UniProtKB).
GO:0042060;	Biological process: wound healing (inferred from mutant phenotype from MGI).
QuickGo view.

Family and domain databases

InterPro

IPR003074; 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 of domain structure.

Gene3D

G3DSA:1.10.565.10; Nucl_hrmn_rcpt_lig_bd; 1.
G3DSA:3.30.50.10; Znf_NHR/GATA; 1.

Pfam

PF00104; Hormone_recep; 1.
PF00105; zf-C4; 1.
Pfam graphical view of domain structure.

PRINTS

PR01288; PROXISOMEPAR.
PR01290; PROXISOMPABR.
PR00398; STRDHORMONER.
PR00047; STROIDFINGER.

ProDom

PD000035; Znf_C4steroid; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00430; HOLI; 1.
SM00399; ZnF_C4; 1.
SMART graphical view of domain structure.

PROSITE

PS00031; NUCLEAR_REC_DBD_1; 1.
PS51030; NUCLEAR_REC_DBD_2; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

P35396.

Genome annotation databases

Ensembl

ENSMUSG00000002250; Mus musculus. [Contig view]

GeneID

19015; -.

KEGG

mmu:19015; -.

Phylogenomic databases

HOVERGEN

P35396; -.

Other

Ppard; Mus musculus.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Activator; DNA-binding; Metal-binding; Nucleus; Receptor; Transcription; Transcription regulation; Zinc; Zinc-finger.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 440`	`440`	`Peroxisome proliferator-activated receptor delta.`	`PRO_0000053487`
`DNA_BIND`	`70 144`	`75`	`Nuclear receptor.`
`ZN_FING`	`73 93`	`21`	`NR C4-type.`
`ZN_FING`	`110 132`	`23`	`NR C4-type.`
`REGION`	`253 440`	`188`	`Ligand-binding (Potential).`
`CONFLICT`	`149 150`		`EA -> DG (in Ref. 2; AAA19972).`

Sequence information

Length: 440 AA [This is the length of the unprocessed precursor]

Molecular weight: 49715 Da [This is the MW of the unprocessed precursor]

CRC64: 58E0F595DD193FDA [This is a checksum on the sequence]

        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

P35396 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools