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O88275

- PPARG_RAT

UniProt

O88275 - PPARG_RAT

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Protein
Peroxisome proliferator-activated receptor gamma
Gene
Pparg, Nr1c3
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Nuclear receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the nuclear receptor binds to DNA specific PPAR response elements (PPRE) and modulates the transcription of its target genes, such as acyl-CoA oxidase. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Key regulator of adipocyte differentiation and glucose homeostasis. ARF6 acts as a key regulator of the tissue-specific adipocyte P2 (aP2) enhancer. Acts as a critical regulator of gut homeostasis by suppressing NF-kappa-B-mediated proinflammatory responses By similarity.

Enzyme regulationi

PDPK1 activates its transcriptional activity independently of its kinase activity By similarity.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi136 – 21075Nuclear receptor
Add
BLAST
Zinc fingeri139 – 15921NR C4-type
Add
BLAST
Zinc fingeri176 – 19823NR C4-type
Add
BLAST

GO - Molecular functioni

  1. DNA binding Source: RGD
  2. RNA polymerase II regulatory region DNA binding Source: Ensembl
  3. chromatin binding Source: UniProtKB
  4. drug binding Source: Ensembl
  5. estrogen receptor binding Source: RGD
  6. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: InterPro
  7. ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
  8. protein binding Source: RGD
  9. protein phosphatase binding Source: RGD
  10. sequence-specific DNA binding Source: InterPro
  11. sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  12. steroid hormone receptor activity Source: InterPro
  13. transcription factor binding Source: RGD
  14. transcription regulatory region DNA binding Source: BHF-UCL
  15. zinc ion binding Source: InterPro

GO - Biological processi

  1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
  2. brown fat cell differentiation Source: Ensembl
  3. cell fate commitment Source: Ensembl
  4. cell maturation Source: Ensembl
  5. cellular response to hyperoxia Source: RGD
  6. cellular response to insulin stimulus Source: Ensembl
  7. cellular response to lithium ion Source: Ensembl
  8. cellular response to prostaglandin E stimulus Source: RGD
  9. cellular response to prostaglandin stimulus Source: RGD
  10. cellular response to retinoic acid Source: RGD
  11. cellular response to vitamin E Source: RGD
  12. epithelial cell differentiation Source: Ensembl
  13. fatty acid metabolic process Source: RGD
  14. fatty acid oxidation Source: RGD
  15. glucose homeostasis Source: Ensembl
  16. heart development Source: RGD
  17. lipoprotein transport Source: Ensembl
  18. long-chain fatty acid transport Source: Ensembl
  19. low-density lipoprotein particle receptor biosynthetic process Source: Ensembl
  20. monocyte differentiation Source: Ensembl
  21. negative regulation of acute inflammatory response Source: RGD
  22. negative regulation of cell growth Source: RGD
  23. negative regulation of cell proliferation Source: RGD
  24. negative regulation of cholesterol storage Source: Ensembl
  25. negative regulation of collagen biosynthetic process Source: RGD
  26. negative regulation of interferon-gamma-mediated signaling pathway Source: Ensembl
  27. negative regulation of pancreatic stellate cell proliferation Source: RGD
  28. negative regulation of receptor biosynthetic process Source: Ensembl
  29. negative regulation of sequestering of triglyceride Source: Ensembl
  30. negative regulation of smooth muscle cell proliferation Source: Ensembl
  31. negative regulation of telomerase activity Source: RGD
  32. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  33. organ regeneration Source: RGD
  34. peroxisome proliferator activated receptor signaling pathway Source: Ensembl
  35. placenta development Source: Ensembl
  36. positive regulation of apoptotic process Source: RGD
  37. positive regulation of fat cell differentiation Source: HGNC
  38. positive regulation of fatty acid oxidation Source: RGD
  39. positive regulation of oligodendrocyte differentiation Source: RGD
  40. positive regulation of phagocytosis, engulfment Source: RGD
  41. positive regulation of sequence-specific DNA binding transcription factor activity Source: Ensembl
  42. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  43. positive regulation of transcription, DNA-templated Source: UniProtKB
  44. regulation of blood pressure Source: Ensembl
  45. regulation of fat cell differentiation Source: RGD
  46. regulation of lipid metabolic process Source: RGD
  47. regulation of transcription from RNA polymerase II promoter Source: RGD
  48. regulation of transcription involved in cell fate commitment Source: UniProtKB
  49. response to caffeine Source: RGD
  50. response to cold Source: RGD
  51. response to diuretic Source: RGD
  52. response to drug Source: RGD
  53. response to estrogen Source: RGD
  54. response to immobilization stress Source: RGD
  55. response to lipid Source: RGD
  56. response to low-density lipoprotein particle Source: Ensembl
  57. response to mechanical stimulus Source: RGD
  58. response to metformin Source: RGD
  59. response to organic cyclic compound Source: RGD
  60. response to organic substance Source: RGD
  61. response to retinoic acid Source: UniProtKB
  62. response to starvation Source: RGD
  63. response to vitamin A Source: RGD
  64. white fat cell differentiation Source: HGNC
Complete GO annotation...

Keywords - Molecular functioni

Activator, Receptor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_196408. PPARA activates gene expression.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisome proliferator-activated receptor gamma
Short name:
PPAR-gamma
Alternative name(s):
Nuclear receptor subfamily 1 group C member 3
Gene namesi
Name:Pparg
Synonyms:Nr1c3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 4

Organism-specific databases

RGDi3371. Pparg.

Subcellular locationi

Nucleus By similarity. Cytoplasm By similarity
Note: Redistributed from the nucleus to the cytosol through a MAP2K1/MEK1-dependent manner. CCRN4L/NOC enhances its nuclear translocation By similarity.

GO - Cellular componenti

  1. cytosol Source: RGD
  2. nucleus Source: RGD
  3. perinuclear region of cytoplasm Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi112 – 1121S → A: Increases adipogenic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 505505Peroxisome proliferator-activated receptor gamma
PRO_0000053497Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi84 – 841O-linked (GlcNAc) By similarity
Modified residuei112 – 1121Phosphoserine; by MAPK1 Publication

Post-translational modificationi

Phosphorylated by MAPK. The phosphorylation inhibits PPAR gamma activity.3 Publications
O-GlcNAcylation at Thr-84 reduces transcriptional activity in adipocytes By similarity.
Phosphorylated at basal conditions and dephosphorylated when treated with the ligand. May be dephosphorylated by PPP5C. The phosphorylated form may be inactive and dephosphorylation at induces adipogenic activity By similarity.3 Publications

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PRIDEiO88275.

PTM databases

PhosphoSiteiO88275.

Expressioni

Tissue specificityi

Highest expression in adipose tissue.

Gene expression databases

GenevestigatoriO88275.

Interactioni

Subunit structurei

Heterodimer with other nuclear receptors, such as RXRA. The heterodimer with the retinoic acid receptor RXRA is called adipocyte-specific transcription factor ARF6. Interacts with NCOA6 coactivator, leading to a strong increase in transcription of target genes. Interacts with coactivator PPARBP, leading to a mild increase in transcription of target genes. Interacts with NOCA7 in a ligand-inducible manner. Interacts with NCOA1 and NCOA2 LXXLL motifs. Interacts with ASXL1, ASXL2, DNTTIP2, FAM120B, MAP2K1/MEK1, NR0B2, PDPK1, PRDM16, PRMT2 and TGFB1I1. Interacts (when activated by agonist) with PPP5C. Interacts with HELZ2 and THRAP3; the interaction stimulates the transcriptional activity of PPARG. Interacts with PER2, the interaction is ligand dependent and blocks PPARG recruitment to target promoters. Interacts with CCRN4L/NOC. Interacts with FOXO1 (acetylated form) By similarity.

Structurei

3D structure databases

ProteinModelPortaliO88275.
SMRiO88275. Positions 131-216, 234-505.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni205 – 28076Interaction with FAM120B By similarity
Add
BLAST
Regioni317 – 505189Ligand-binding By similarity
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG266867.
GeneTreeiENSGT00740000115076.
HOGENOMiHOG000261626.
HOVERGENiHBG106004.
InParanoidiO88275.
KOiK08530.
OMAiSTPHYED.
OrthoDBiEOG7X9G7F.
PhylomeDBiO88275.
TreeFamiTF316304.

Family and domain databases

Gene3Di1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProiIPR003074. 1Cnucl_rcpt.
IPR003077. 1Cnucl_rcpt_G.
IPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR022590. PPARgamma_N.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamiPF00104. Hormone_recep. 1 hit.
PF12577. PPARgamma_N. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR01288. PROXISOMEPAR.
PR01291. PROXISOMPAGR.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform 2 (identifier: O88275-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MGETLGDPPV DPEHGAFADA LPMSTSQEIT MVDTEMPFWP TNFGISSVDL    50
SVMDDHSHSF DIKPFTTVDF SSISAPHYED IPFTRADPMV ADYKYDLKLQ 100
EYQSAIKVEP ASPPYYSEKT QLYNRPHEEP SNSLMAIECR VCGDKASGFH 150
YGVHACEGCK GFFRRTIRLK LIYDRCDLNC RIHKKSRNKC QYCRFQKCLA 200
VGMSHNAIRF GRMPQAEKEK LLAEISSDID QLNPESADLR ALAKHLYDSY 250
IKSFPLTKAK ARAILTGKTT DKSPFVIYDM NSLMMGEDKI KFKHITPLQE 300
QSKEVAIRIF QGCQFRSVEA VQEITEYAKN IPGFINLDLN DQVTLLKYGV 350
HEIIYTMLAS LMNKDGVLIS EGQGFMTREF LKSLRKPFGD FMEPKFEFAV 400
KFNALELDDS DLAIFIAVII LSGDRPGLLN VKPIEDIQDN LLQALELQLK 450
LNHPESSQLF AKVLQKMTDL RQIVTEHVQL LHVIKKTETD MSLHPLLQEI 500
YKDLY 505
Length:505
Mass (Da):57,567
Last modified:August 1, 1999 - v2
Checksum:iF16E5CAB122EBB32
GO
Isoform 1 (identifier: O88275-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: Missing.

Show »
Length:475
Mass (Da):54,471
Checksum:iC761352FDF9C4395
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3030Missing in isoform 1.
VSP_003649Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti111 – 1111A → R in CAA73382. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF156666 mRNA. Translation: AAD40119.1.
AF156665 mRNA. Translation: AAD40118.1.
AB019561 mRNA. Translation: BAA36485.1.
Y12882 mRNA. Translation: CAA73382.2.
AB011365 mRNA. Translation: BAA32540.1.
AF246457 mRNA. Translation: AAF63385.1.
AF246458 mRNA. Translation: AAF63386.1.
RefSeqiNP_001138838.1. NM_001145366.1. [O88275-2]
NP_001138839.1. NM_001145367.1. [O88275-2]
NP_037256.1. NM_013124.3. [O88275-1]
XP_006237071.1. XM_006237009.1. [O88275-2]
UniGeneiRn.23443.

Genome annotation databases

EnsembliENSRNOT00000012137; ENSRNOP00000012137; ENSRNOG00000008839. [O88275-1]
ENSRNOT00000051858; ENSRNOP00000045012; ENSRNOG00000008839. [O88275-2]
GeneIDi25664.
KEGGirno:25664.
UCSCiRGD:3371. rat. [O88275-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF156666 mRNA. Translation: AAD40119.1 .
AF156665 mRNA. Translation: AAD40118.1 .
AB019561 mRNA. Translation: BAA36485.1 .
Y12882 mRNA. Translation: CAA73382.2 .
AB011365 mRNA. Translation: BAA32540.1 .
AF246457 mRNA. Translation: AAF63385.1 .
AF246458 mRNA. Translation: AAF63386.1 .
RefSeqi NP_001138838.1. NM_001145366.1. [O88275-2 ]
NP_001138839.1. NM_001145367.1. [O88275-2 ]
NP_037256.1. NM_013124.3. [O88275-1 ]
XP_006237071.1. XM_006237009.1. [O88275-2 ]
UniGenei Rn.23443.

3D structure databases

ProteinModelPortali O88275.
SMRi O88275. Positions 131-216, 234-505.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi O88275.
ChEMBLi CHEMBL4797.

PTM databases

PhosphoSitei O88275.

Proteomic databases

PRIDEi O88275.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000012137 ; ENSRNOP00000012137 ; ENSRNOG00000008839 . [O88275-1 ]
ENSRNOT00000051858 ; ENSRNOP00000045012 ; ENSRNOG00000008839 . [O88275-2 ]
GeneIDi 25664.
KEGGi rno:25664.
UCSCi RGD:3371. rat. [O88275-1 ]

Organism-specific databases

CTDi 5468.
RGDi 3371. Pparg.

Phylogenomic databases

eggNOGi NOG266867.
GeneTreei ENSGT00740000115076.
HOGENOMi HOG000261626.
HOVERGENi HBG106004.
InParanoidi O88275.
KOi K08530.
OMAi STPHYED.
OrthoDBi EOG7X9G7F.
PhylomeDBi O88275.
TreeFami TF316304.

Enzyme and pathway databases

Reactomei REACT_196408. PPARA activates gene expression.

Miscellaneous databases

NextBioi 607577.
PROi O88275.

Gene expression databases

Genevestigatori O88275.

Family and domain databases

Gene3Di 1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProi IPR003074. 1Cnucl_rcpt.
IPR003077. 1Cnucl_rcpt_G.
IPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR022590. PPARgamma_N.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view ]
Pfami PF00104. Hormone_recep. 1 hit.
PF12577. PPARgamma_N. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view ]
PRINTSi PR01288. PROXISOMEPAR.
PR01291. PROXISOMPAGR.
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

  1. "Rat peroxisome proliferator-activated receptors and brown adipose tissue function during cold acclimatization."
    Guardiola-Diaz H.M., Rehnmark S., Usuda N., Albrektsen T., Feltkamp D., Gustafsson J.-A., Alexson S.E.H.
    J. Biol. Chem. 274:23368-23377(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Strain: Sprague-Dawley.
    Tissue: Brown adipose tissue.
  2. "Down-regulation of PPAR gammma."
    Tanaka T., Itoh H.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: Sprague-Dawley.
    Tissue: Adipose tissue.
  3. Escher P.
    Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  4. "Molecular cloning of rat PPAR-gamma gene."
    Miyakita A., Okuno S., Watanabe T.K., Oga K., Tsuji A., Hishigaki H., Suto T., Nakagawa K., Nakahara Y., Higashi K.
    Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Adipocyte.
  5. "Photoreceptor phagocytosis selectively activates PPARgamma expression in retinal pigment epithelial cells."
    Ershov A.V., Bazan N.G.
    J. Neurosci. Res. 60:328-337(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: Long Evans.
  6. "Inhibition of adipogenesis through MAP kinase-mediated phosphorylation of PPARgamma."
    Hu E., Kim J.B., Sarraf P., Spiegelman B.M.
    Science 274:2100-2103(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  7. "Transcriptional activation by peroxisome proliferator-activated receptor gamma is inhibited by phosphorylation at a consensus mitogen-activated protein kinase site."
    Adams M., Reginato M.J., Shao D., Lazar M.A., Chatterjee V.K.
    J. Biol. Chem. 272:5128-5132(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-112, MUTAGENESIS OF SER-112.
  8. "Insulin- and mitogen-activated protein kinase-mediated phosphorylation and activation of peroxisome proliferator-activated receptor gamma."
    Zhang B., Berger J., Zhou G., Elbrecht A., Biswas S., White-Carrington S., Szalkowski D., Moller D.E.
    J. Biol. Chem. 271:31771-31774(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.

Entry informationi

Entry nameiPPARG_RAT
AccessioniPrimary (citable) accession number: O88275
Secondary accession number(s): Q9QWG0, Q9R197
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: August 1, 1999
Last modified: September 3, 2014
This is version 144 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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