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P37230 (PPARA_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 alpha

Short name=PPAR-alpha
Alternative name(s):
Nuclear receptor subfamily 1 group C member 1
Gene names
Name:Ppara
Synonyms:Nr1c1, Ppar
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length468 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Ligand-activated transcription factor. Key regulator of lipid metabolism. Activated by the endogenous ligand 1-palmitoyl-2-oleoyl-sn-glycerol-3-phosphocholine (16:0/18:1-GPC). Activated by oleylethanolamide, a naturally occurring lipid that regulates satiety. Receptor for peroxisome proliferators such as hypolipidemic drugs and fatty acids. Regulates the peroxisomal beta-oxidation pathway of fatty acids. Functions as transcription activator for the ACOX1 and P450 genes. Transactivation activity requires heterodimerization with RXRA and is antagonized by NR2C2. May be required for the propagation of clock information to metabolic pathways regulated by PER2 By similarity.

Subunit structure

Heterodimer; with RXRA. This heterodimerization is required for DNA binding and transactivation activity. Interacts with NCOA3 coactivator. Interacts with CITED2; the interaction stimulates its transcriptional activity. Also interacts with PPARBP in vitro. Interacts with AKAP13, LPIN1, PRDM16 and coactivator NCOA6. Interacts with ASXL1 AND ASXL2. Interacts with PER2 By similarity. Ref.3

Subcellular location

Nucleus.

Tissue specificity

Expressed predominantly in liver and kidney.

Post-translational modification

Phosphorylated. Ref.2

Sequence similarities

Belongs to the nuclear hormone receptor family. NR1 subfamily.

Contains 1 nuclear receptor DNA-binding domain.

Ontologies

Keywords
   Biological processBiological rhythms
Transcription
Transcription regulation
   Cellular componentNucleus
   DomainZinc-finger
   LigandDNA-binding
Lipid-binding
Metal-binding
Zinc
   Molecular functionActivator
Receptor
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbehavioral response to nicotine

Inferred from direct assay PubMed 20801430. Source: RGD

circadian regulation of gene expression

Inferred from sequence or structural similarity. Source: UniProtKB

enamel mineralization

Inferred from electronic annotation. Source: Ensembl

epidermis development

Inferred from electronic annotation. Source: Ensembl

fatty acid metabolic process

Inferred from mutant phenotype PubMed 12600885PubMed 12853447PubMed 16183630. Source: RGD

heart development

Inferred from expression pattern PubMed 15754086. Source: RGD

lipoprotein metabolic process

Inferred from mutant phenotype PubMed 15537571. Source: RGD

negative regulation of appetite

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of blood pressure

Inferred from mutant phenotype PubMed 15967866. Source: RGD

negative regulation of cholesterol storage

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron death

Inferred from mutant phenotype PubMed 20221904. Source: RGD

negative regulation of protein binding

Inferred from mutant phenotype PubMed 22198280. Source: RGD

negative regulation of receptor biosynthetic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of sequestering of triglyceride

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription regulatory region DNA binding

Inferred from mutant phenotype PubMed 22198280. Source: RGD

positive regulation of fatty acid oxidation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cellular ketone metabolic process by positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

regulation of circadian rhythm

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of fatty acid metabolic process

Traceable author statement PubMed 12189208. Source: RGD

regulation of glycolytic by positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

regulation of lipid transport by positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

regulation of transcription, DNA-templated

Inferred from direct assay PubMed 12189208. Source: RGD

response to hypoxia

Inferred from direct assay PubMed 15292030. Source: HGNC

response to insulin

Inferred from mutant phenotype PubMed 16183630. Source: RGD

wound healing

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentnucleus

Inferred from direct assay PubMed 12189208PubMed 22198280. Source: RGD

   Molecular_functionMDM2/MDM4 family protein binding

Inferred from physical interaction PubMed 19103650. Source: RGD

NFAT protein binding

Inferred from physical interaction PubMed 22198280. Source: RGD

drug binding

Inferred from sequence or structural similarity. Source: UniProtKB

ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from mutant phenotype PubMed 12189208PubMed 12966092. Source: RGD

lipid binding

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatase binding

Inferred from physical interaction PubMed 8910358. Source: RGD

protein binding

Inferred from physical interaction Ref.3. Source: UniProtKB

protein complex binding

Inferred from mutant phenotype PubMed 20132223. Source: RGD

protein domain specific binding

Inferred from direct assay PubMed 12189208. Source: RGD

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

steroid hormone receptor activity

Traceable author statement PubMed 12189208. Source: RGD

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 468468Peroxisome proliferator-activated receptor alpha
PRO_0000053484

Regions

DNA binding99 – 17375Nuclear receptor
Zinc finger102 – 12221NR C4-type
Zinc finger139 – 16123NR C4-type
Region280 – 468189Ligand-binding By similarity
Region304 – 433130Required for heterodimerization with RXRA By similarity

Sites

Site4331Essential for heterodimerization with RXRA By similarity

Sequences

Sequence LengthMass (Da)Tools
P37230 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 2A89E7D715C8DBA9

FASTA46852,377
        10         20         30         40         50         60 
MVDTESPICP LSPLEADDLE SPLSEEFLQE MGNIQEISQS LGEESSGSFS FADYQYLGSC 

        70         80         90        100        110        120 
PGSEGSVITD TLSPASSPSS VSCPAVPTST DESPGNALNI ECRICGDKAS GYHYGVHACE 

       130        140        150        160        170        180 
GCKGFFRRTI RLKLAYDKCD RSCKIQKKNR NKCQYCRFHK CLSVGMSHNA IRFGRMPRSE 

       190        200        210        220        230        240 
KAKLKAEILT CEHDLKDSET ADLKSLAKRI HEAYLKNFNM NKVKARVILA GKTSNNPPFV 

       250        260        270        280        290        300 
IHDMETLCMA EKTLVAKMVA NGVENKEAEV RFFHCCQCMS VETVTELTEF AKAIPGFANL 

       310        320        330        340        350        360 
DLNDQVTLLK YGVYEAIFTM LSSLMNKDGM LIAYGNGFIT REFLKNLRKP FCDIMEPKFD 

       370        380        390        400        410        420 
FAMKFNALEL DDSDISLFVA AIICCGDRPG LLNIGYIEKL QEGIVHVLKL HLQSNHPDDT 

       430        440        450        460 
FLFPKLLQKM VDLRQLVTEH AQLVQVIKKT ESDAALHPLL QEIYRDMY 

« Hide

References

[1]"Fatty acids activate a chimera of the clofibric acid-activated receptor and the glucocorticoid receptor."
Goettlicher M., Widmark E., Li Q., Gustafsson J.-A.
Proc. Natl. Acad. Sci. U.S.A. 89:4653-4657(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The peroxisome proliferator-activated receptor alpha is a phosphoprotein: regulation by insulin."
Shalev A., Siegrist-Kaiser C.A., Yen P.M., Wahli W., Burger A.G., Chin W.W., Meier C.A.
Endocrinology 137:4499-4502(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[3]"Identification of the CREB-binding protein/p300-interacting protein CITED2 as a peroxisome proliferator-activated receptor alpha coregulator."
Tien E.S., Davis J.W., Vanden Heuvel J.P.
J. Biol. Chem. 279:24053-24063(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CITED2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M88592 mRNA. Translation: AAA41918.1.
PIRA45288.
RefSeqNP_037328.1. NM_013196.1.
XP_006242218.1. XM_006242156.1.
UniGeneRn.9753.

3D structure databases

ProteinModelPortalP37230.
SMRP37230. Positions 100-179, 200-468.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid247775. 5 interactions.
DIPDIP-29529N.
STRING10116.ENSRNOP00000038651.

Chemistry

BindingDBP37230.
ChEMBLCHEMBL2129.

PTM databases

PhosphoSiteP37230.

Proteomic databases

PRIDEP37230.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000030082; ENSRNOP00000038651; ENSRNOG00000021463.
GeneID25747.
KEGGrno:25747.

Organism-specific databases

CTD5465.
RGD3369. Ppara.

Phylogenomic databases

eggNOGNOG266867.
GeneTreeENSGT00740000115076.
HOGENOMHOG000261626.
HOVERGENHBG106004.
InParanoidP37230.
KOK07294.
OMATESPICP.
OrthoDBEOG7X9G7F.
PhylomeDBP37230.
TreeFamTF316304.

Gene expression databases

GenevestigatorP37230.

Family and domain databases

Gene3D1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProIPR003074. 1Cnucl_rcpt.
IPR003076. 1Cnucl_rcpt_A.
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]
PfamPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSPR01288. PROXISOMEPAR.
PR01289. PROXISOMPAAR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMSSF48508. SSF48508. 1 hit.
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio607925.
PROP37230.

Entry information

Entry namePPARA_RAT
AccessionPrimary (citable) accession number: P37230
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: July 9, 2014
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families