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Protein

Peroxisome proliferator-activated receptor alpha

Gene

Ppara

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei433 – 4331Essential for heterodimerization with RXRABy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi99 – 17375Nuclear receptorPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri102 – 12221NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri139 – 16123NR C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • behavioral response to nicotine Source: RGD
  • circadian regulation of gene expression Source: UniProtKB
  • enamel mineralization Source: Ensembl
  • epidermis development Source: Ensembl
  • fatty acid metabolic process Source: RGD
  • heart development Source: RGD
  • intracellular receptor signaling pathway Source: GOC
  • lipoprotein metabolic process Source: RGD
  • negative regulation of appetite Source: UniProtKB
  • negative regulation of blood pressure Source: RGD
  • negative regulation of cholesterol storage Source: Ensembl
  • negative regulation of neuron death Source: RGD
  • negative regulation of protein binding Source: RGD
  • negative regulation of receptor biosynthetic process Source: Ensembl
  • negative regulation of sequestering of triglyceride Source: Ensembl
  • negative regulation of transcription regulatory region DNA binding Source: RGD
  • positive regulation of fatty acid oxidation Source: Ensembl
  • positive regulation of gluconeogenesis Source: Ensembl
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • regulation of cellular ketone metabolic process by positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  • regulation of circadian rhythm Source: UniProtKB
  • regulation of fatty acid metabolic process Source: RGD
  • regulation of glycolytic process by positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  • regulation of lipid transport by positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  • regulation of transcription, DNA-templated Source: RGD
  • response to hypoxia Source: HGNC
  • response to insulin Source: RGD
  • wound healing Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Activator, Receptor

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Lipid-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_329374. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
REACT_334119. Nuclear Receptor transcription pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisome proliferator-activated receptor alpha
Short name:
PPAR-alpha
Alternative name(s):
Nuclear receptor subfamily 1 group C member 1
Gene namesi
Name:Ppara
Synonyms:Nr1c1, Ppar
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 7

Organism-specific databases

RGDi3369. Ppara.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 468468Peroxisome proliferator-activated receptor alphaPRO_0000053484Add
BLAST

Post-translational modificationi

Phosphorylated.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP37230.

PTM databases

PhosphoSiteiP37230.

Expressioni

Tissue specificityi

Expressed predominantly in liver and kidney.

Gene expression databases

GenevisibleiP37230. RN.

Interactioni

Subunit structurei

Heterodimer; with RXRA. This heterodimerization is required for DNA binding and transactivation activity. Interacts with NCOA3 coactivator (By similarity). Interacts with CITED2; the interaction stimulates its transcriptional activity (PubMed:15051727). Also interacts with PPARBP in vitro. Interacts with AKAP13, LPIN1, PRDM16 and coactivator NCOA6. Interacts with ASXL1 and ASXL2. Interacts with PER2. Interacts with SIRT1; the interaction seems to be modulated by NAD+ levels (By similarity).By similarity1 Publication

Protein-protein interaction databases

BioGridi247775. 5 interactions.
DIPiDIP-29529N.
STRINGi10116.ENSRNOP00000038651.

Structurei

3D structure databases

ProteinModelPortaliP37230.
SMRiP37230. Positions 100-179, 200-468.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni280 – 468189Ligand-bindingBy similarityAdd
BLAST
Regioni304 – 433130Required for heterodimerization with RXRABy similarityAdd
BLAST

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri102 – 12221NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri139 – 16123NR C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG266867.
GeneTreeiENSGT00780000121834.
HOGENOMiHOG000261626.
HOVERGENiHBG106004.
InParanoidiP37230.
KOiK07294.
OMAiNNNPPFV.
OrthoDBiEOG7X9G7F.
PhylomeDBiP37230.
TreeFamiTF316304.

Family and domain databases

Gene3Di1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProiIPR003074. 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]
PfamiPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR01288. PROXISOMEPAR.
PR01289. PROXISOMPAAR.
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.

P37230-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVDTESPICP LSPLEADDLE SPLSEEFLQE MGNIQEISQS LGEESSGSFS
60 70 80 90 100
FADYQYLGSC PGSEGSVITD TLSPASSPSS VSCPAVPTST DESPGNALNI
110 120 130 140 150
ECRICGDKAS GYHYGVHACE GCKGFFRRTI RLKLAYDKCD RSCKIQKKNR
160 170 180 190 200
NKCQYCRFHK CLSVGMSHNA IRFGRMPRSE KAKLKAEILT CEHDLKDSET
210 220 230 240 250
ADLKSLAKRI HEAYLKNFNM NKVKARVILA GKTSNNPPFV IHDMETLCMA
260 270 280 290 300
EKTLVAKMVA NGVENKEAEV RFFHCCQCMS VETVTELTEF AKAIPGFANL
310 320 330 340 350
DLNDQVTLLK YGVYEAIFTM LSSLMNKDGM LIAYGNGFIT REFLKNLRKP
360 370 380 390 400
FCDIMEPKFD FAMKFNALEL DDSDISLFVA AIICCGDRPG LLNIGYIEKL
410 420 430 440 450
QEGIVHVLKL HLQSNHPDDT FLFPKLLQKM VDLRQLVTEH AQLVQVIKKT
460
ESDAALHPLL QEIYRDMY
Length:468
Mass (Da):52,377
Last modified:October 1, 1994 - v1
Checksum:i2A89E7D715C8DBA9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M88592 mRNA. Translation: AAA41918.1.
PIRiA45288.
RefSeqiNP_037328.1. NM_013196.1.
XP_006242218.1. XM_006242156.2.
UniGeneiRn.9753.

Genome annotation databases

EnsembliENSRNOT00000030082; ENSRNOP00000038651; ENSRNOG00000021463.
ENSRNOT00000078928; ENSRNOP00000074329; ENSRNOG00000021463.
GeneIDi25747.
KEGGirno:25747.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M88592 mRNA. Translation: AAA41918.1.
PIRiA45288.
RefSeqiNP_037328.1. NM_013196.1.
XP_006242218.1. XM_006242156.2.
UniGeneiRn.9753.

3D structure databases

ProteinModelPortaliP37230.
SMRiP37230. Positions 100-179, 200-468.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247775. 5 interactions.
DIPiDIP-29529N.
STRINGi10116.ENSRNOP00000038651.

Chemistry

BindingDBiP37230.
ChEMBLiCHEMBL2129.

PTM databases

PhosphoSiteiP37230.

Proteomic databases

PRIDEiP37230.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000030082; ENSRNOP00000038651; ENSRNOG00000021463.
ENSRNOT00000078928; ENSRNOP00000074329; ENSRNOG00000021463.
GeneIDi25747.
KEGGirno:25747.

Organism-specific databases

CTDi5465.
RGDi3369. Ppara.

Phylogenomic databases

eggNOGiNOG266867.
GeneTreeiENSGT00780000121834.
HOGENOMiHOG000261626.
HOVERGENiHBG106004.
InParanoidiP37230.
KOiK07294.
OMAiNNNPPFV.
OrthoDBiEOG7X9G7F.
PhylomeDBiP37230.
TreeFamiTF316304.

Enzyme and pathway databases

ReactomeiREACT_329374. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
REACT_334119. Nuclear Receptor transcription pathway.

Miscellaneous databases

NextBioi607925.
PROiP37230.

Gene expression databases

GenevisibleiP37230. RN.

Family and domain databases

Gene3Di1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProiIPR003074. 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]
PfamiPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR01288. PROXISOMEPAR.
PR01289. PROXISOMPAAR.
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

  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.

Entry informationi

Entry nameiPPARA_RAT
AccessioniPrimary (citable) accession number: P37230
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: July 22, 2015
This is version 146 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. 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.