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P23204

- PPARA_MOUSE

UniProt

P23204 - PPARA_MOUSE

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Protein

Peroxisome proliferator-activated receptor alpha

Gene

Ppara

Organism
Mus musculus (Mouse)
Status
Reviewed - 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 PER2.3 Publications

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

  1. DNA binding Source: MGI
  2. drug binding Source: UniProtKB
  3. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: Ensembl
  4. lipid binding Source: UniProtKB
  5. protein heterodimerization activity Source: UniProtKB
  6. receptor activity Source: MGI
  7. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
  8. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: Ensembl
  9. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: Ensembl
  10. RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription Source: MGI
  11. sequence-specific DNA binding Source: UniProtKB
  12. sequence-specific DNA binding transcription factor activity Source: UniProtKB
  13. steroid hormone receptor activity Source: MGI
  14. zinc ion binding Source: InterPro

GO - Biological processi

  1. behavioral response to nicotine Source: Ensembl
  2. circadian regulation of gene expression Source: UniProtKB
  3. enamel mineralization Source: MGI
  4. epidermis development Source: MGI
  5. fatty acid metabolic process Source: MGI
  6. glucose metabolic process Source: MGI
  7. heart development Source: Ensembl
  8. lipid metabolic process Source: MGI
  9. lipoprotein metabolic process Source: Ensembl
  10. negative regulation of appetite Source: UniProtKB
  11. negative regulation of blood pressure Source: Ensembl
  12. negative regulation of cholesterol storage Source: Ensembl
  13. negative regulation of neuron death Source: Ensembl
  14. negative regulation of protein binding Source: Ensembl
  15. negative regulation of receptor biosynthetic process Source: Ensembl
  16. negative regulation of sequestering of triglyceride Source: Ensembl
  17. negative regulation of transcription regulatory region DNA binding Source: Ensembl
  18. positive regulation of fatty acid oxidation Source: BHF-UCL
  19. positive regulation of gluconeogenesis Source: MGI
  20. positive regulation of transcription, DNA-templated Source: UniProtKB
  21. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  22. regulation of cellular ketone metabolic process by positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  23. regulation of circadian rhythm Source: UniProtKB
  24. regulation of fatty acid metabolic process Source: MGI
  25. regulation of gene expression Source: MGI
  26. regulation of glycolytic by positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  27. regulation of lipid transport by positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  28. regulation of transcription, DNA-templated Source: MGI
  29. response to hypoxia Source: Ensembl
  30. response to insulin Source: Ensembl
  31. wound healing Source: MGI
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_115781. Bmal1:Clock,Npas2 activates circadian gene expression.
REACT_118837. Rora activates circadian gene expression.
REACT_196516. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
REACT_198351. RORA activates circadian gene expression.
REACT_198352. REV-ERBA represses gene expression.
REACT_198602. PPARA activates gene expression.
REACT_198620. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_198969. Activation of gene expression by SREBF (SREBP).
REACT_205251. Transcriptional activation of mitochondrial biogenesis.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:104740. Ppara.

Subcellular locationi

Nucleus 1 PublicationPROSITE-ProRule annotation

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
  2. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Peroxisome proliferators are a diverse group of chemicals that include hypolipidaemic drugs, herbicides and industrial plasticisers. Administration of these chemicals to rodents results in the dramatic proliferation of hepatic peroxisomes as well as liver hyperplasia.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi119 – 1191C → A: Reduces DNA binding and strongly decreases transcriptional activation; when associated with A-122. 1 Publication
Mutagenesisi122 – 1221C → A: Reduces DNA binding and strongly decreases transcriptional activation; when associated with A-119. 1 Publication
Mutagenesisi292 – 2921K → A: No effect on interaction with PER2. 1 Publication
Mutagenesisi459 – 46810Missing: Slightly reduces interaction with PER2. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 468468Peroxisome proliferator-activated receptor alphaPRO_0000053482Add
BLAST

Proteomic databases

PRIDEiP23204.

PTM databases

PhosphoSiteiP23204.

Expressioni

Tissue specificityi

Highly expressed in liver, kidney and heart. Very weakly expressed in brain and testis.

Developmental stagei

It appears first at 13.5 dpc and increases until birth.

Gene expression databases

BgeeiP23204.
CleanExiMM_PPARA.
ExpressionAtlasiP23204. baseline and differential.
GenevestigatoriP23204.

Interactioni

Subunit structurei

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 PER2.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Men1O885592EBI-5273083,EBI-3990176

Protein-protein interaction databases

BioGridi202317. 15 interactions.
DIPiDIP-5958N.
IntActiP23204. 3 interactions.
STRINGi10090.ENSMUSP00000059719.

Structurei

3D structure databases

ProteinModelPortaliP23204.
SMRiP23204. Positions 93-468.
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.
HOGENOMiHOG000261626.
HOVERGENiHBG106004.
InParanoidiP23204.
KOiK07294.
OMAiTESPICP.
OrthoDBiEOG7X9G7F.
PhylomeDBiP23204.
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.

P23204-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVDTESPICP LSPLEADDLE SPLSEEFLQE MGNIQEISQS IGEESSGSFG
60 70 80 90 100
FADYQYLGSC PGSEGSVITD TLSPASSPSS VSCPVIPAST DESPGSALNI
110 120 130 140 150
ECRICGDKAS GYHYGVHACE GCKGFFRRTI RLKLVYDKCD RSCKIQKKNR
160 170 180 190 200
NKCQYCRFHK CLSVGMSHNA IRFGRMPRSE KAKLKAEILT CEHDLKDSET
210 220 230 240 250
ADLKSLGKRI HEAYLKNFNM NKVKARVILA GKTSNNPPFV IHDMETLCMA
260 270 280 290 300
EKTLVAKMVA NGVEDKEAEV 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):52,347
Last modified:October 1, 1996 - v2
Checksum:i2930A5191C610B6B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti75 – 751A → R in CAA40856. (PubMed:2129546)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X57638 mRNA. Translation: CAA40856.1.
X75289
, X75290, X75291, X75292, X75293, X75294 Genomic DNA. Translation: CAA53042.1.
BC016892 mRNA. Translation: AAH16892.1.
X89577 mRNA. Translation: CAA61754.1.
CCDSiCCDS27721.1.
PIRiJC2085.
RefSeqiNP_001106889.1. NM_001113418.1.
NP_035274.2. NM_011144.6.
XP_006520682.1. XM_006520619.1.
XP_006520683.1. XM_006520620.1.
XP_006520684.1. XM_006520621.1.
XP_006520685.1. XM_006520622.1.
XP_006520686.1. XM_006520623.1.
UniGeneiMm.212789.

Genome annotation databases

EnsembliENSMUST00000057979; ENSMUSP00000059719; ENSMUSG00000022383.
ENSMUST00000109422; ENSMUSP00000105049; ENSMUSG00000022383.
ENSMUST00000109423; ENSMUSP00000105050; ENSMUSG00000022383.
GeneIDi19013.
KEGGimmu:19013.
UCSCiuc007xdj.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X57638 mRNA. Translation: CAA40856.1 .
X75289
, X75290 , X75291 , X75292 , X75293 , X75294 Genomic DNA. Translation: CAA53042.1 .
BC016892 mRNA. Translation: AAH16892.1 .
X89577 mRNA. Translation: CAA61754.1 .
CCDSi CCDS27721.1.
PIRi JC2085.
RefSeqi NP_001106889.1. NM_001113418.1.
NP_035274.2. NM_011144.6.
XP_006520682.1. XM_006520619.1.
XP_006520683.1. XM_006520620.1.
XP_006520684.1. XM_006520621.1.
XP_006520685.1. XM_006520622.1.
XP_006520686.1. XM_006520623.1.
UniGenei Mm.212789.

3D structure databases

ProteinModelPortali P23204.
SMRi P23204. Positions 93-468.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202317. 15 interactions.
DIPi DIP-5958N.
IntActi P23204. 3 interactions.
STRINGi 10090.ENSMUSP00000059719.

Chemistry

BindingDBi P23204.
ChEMBLi CHEMBL2128.
GuidetoPHARMACOLOGYi 593.

PTM databases

PhosphoSitei P23204.

Proteomic databases

PRIDEi P23204.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000057979 ; ENSMUSP00000059719 ; ENSMUSG00000022383 .
ENSMUST00000109422 ; ENSMUSP00000105049 ; ENSMUSG00000022383 .
ENSMUST00000109423 ; ENSMUSP00000105050 ; ENSMUSG00000022383 .
GeneIDi 19013.
KEGGi mmu:19013.
UCSCi uc007xdj.2. mouse.

Organism-specific databases

CTDi 5465.
MGIi MGI:104740. Ppara.

Phylogenomic databases

eggNOGi NOG266867.
HOGENOMi HOG000261626.
HOVERGENi HBG106004.
InParanoidi P23204.
KOi K07294.
OMAi TESPICP.
OrthoDBi EOG7X9G7F.
PhylomeDBi P23204.
TreeFami TF316304.

Enzyme and pathway databases

Reactomei REACT_115781. Bmal1:Clock,Npas2 activates circadian gene expression.
REACT_118837. Rora activates circadian gene expression.
REACT_196516. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
REACT_198351. RORA activates circadian gene expression.
REACT_198352. REV-ERBA represses gene expression.
REACT_198602. PPARA activates gene expression.
REACT_198620. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_198969. Activation of gene expression by SREBF (SREBP).
REACT_205251. Transcriptional activation of mitochondrial biogenesis.

Miscellaneous databases

NextBioi 295428.
PROi P23204.
SOURCEi Search...

Gene expression databases

Bgeei P23204.
CleanExi MM_PPARA.
ExpressionAtlasi P23204. baseline and differential.
Genevestigatori P23204.

Family and domain databases

Gene3Di 1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProi IPR003074. 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 ]
Pfami PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view ]
PRINTSi PR01288. PROXISOMEPAR.
PR01289. PROXISOMPAAR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTi SM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view ]
SUPFAMi SSF48508. SSF48508. 1 hit.
PROSITEi PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Activation of a member of the steroid hormone receptor superfamily by peroxisome proliferators."
    Issemann I., Green S.
    Nature 347:645-650(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Structure of the mouse peroxisome proliferator activated receptor alpha gene."
    Gearing K.L., Crickmore A., Gustafsson J.-A.
    Biochem. Biophys. Res. Commun. 199:255-263(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/Sv.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Kidney.
  4. "Chromosomal localisation, inducibility, tissue-specific expression and strain differences in three murine peroxisome-proliferator-activated-receptor genes."
    Jones P.S., Savory R., Barratt P., Bell A.R., Gray T.J.B., Jenkins N.A., Gilbert D.J., Copeland N.G., Bell D.R.
    Eur. J. Biochem. 233:219-226(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 413-468.
    Strain: Swiss Webster.
    Tissue: Liver.
  5. "Isolation and characterization of PBP, a protein that interacts with peroxisome proliferator-activated receptor."
    Zhu Y., Qi C., Jain S., Rao M.S., Reddy J.K.
    J. Biol. Chem. 272:25500-25506(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PPARBP.
  6. "Characterization of Brx, a novel Dbl family member that modulates estrogen receptor action."
    Rubino D., Driggers P., Arbit D., Kemp L., Miller B., Coso O., Pagliai K., Gray K., Gutkind S., Segars J.
    Oncogene 16:2513-2526(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AKAP13.
  7. "Isolation and characterization of peroxisome proliferator-activated receptor (PPAR) interacting protein (PRIP) as a coactivator for PPAR."
    Zhu Y.-J., Kan L., Qi C., Kanwar Y.S., Yeldandi A.V., Rao M.S., Reddy J.K.
    J. Biol. Chem. 275:13510-13516(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NCOA6.
  8. "Oleylethanolamide regulates feeding and body weight through activation of the nuclear receptor PPAR-alpha."
    Fu J., Gaetani S., Oveisi F., Lo Verme J., Serrano A., Rodriguez De Fonseca F., Rosengarth A., Luecke H., Di Giacomo B., Tarzia G., Piomelli D.
    Nature 425:90-93(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION AS RECEPTOR FOR OLEYLETHANOLAMIDE, FUNCTION.
  9. "Lipin 1 is an inducible amplifier of the hepatic PGC-1alpha/PPARalpha regulatory pathway."
    Finck B.N., Gropler M.C., Chen Z., Leone T.C., Croce M.A., Harris T.E., Lawrence J.C. Jr., Kelly D.P.
    Cell Metab. 4:199-210(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LIPN1.
  10. Cited for: INTERACTION WITH PRDM16.
  11. "Identification of a physiologically relevant endogenous ligand for PPARalpha in liver."
    Chakravarthy M.V., Lodhi I.J., Yin L., Malapaka R.R., Xu H.E., Turk J., Semenkovich C.F.
    Cell 138:476-488(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF 1-PALMITOYL-2-OLEOYL-SN-GLYCEROL-3-PHOSPHOCHOLINE AS A PHYSIOLOGICAL LIGAND, DNA-BINDING, FUNCTION, MUTAGENESIS OF CYS-119 AND CYS-122.
  12. "The mammalian clock component PERIOD2 coordinates circadian output by interaction with nuclear receptors."
    Schmutz I., Ripperger J.A., Baeriswyl-Aebischer S., Albrecht U.
    Genes Dev. 24:345-357(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CIRCADIAN RHYTHMS, INTERACTION WITH PER2, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-292 AND 459-LEU--TYR-468.

Entry informationi

Entry nameiPPARA_MOUSE
AccessioniPrimary (citable) accession number: P23204
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 157 of the entry and version 2 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