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O88275

- PPARG_RAT

UniProt

O88275 - PPARG_RAT

Protein

Peroxisome proliferator-activated receptor gamma

Gene

Pparg

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 2 (01 Aug 1999)
      Previous versions | rss
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    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.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 receptorPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri139 – 15921NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri176 – 19823NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: UniProtKB
    2. DNA binding Source: RGD
    3. drug binding Source: Ensembl
    4. estrogen receptor binding Source: RGD
    5. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: InterPro
    6. ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
    7. protein binding Source: RGD
    8. protein phosphatase binding Source: RGD
    9. RNA polymerase II regulatory region DNA binding Source: Ensembl
    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, DNA-templated Source: UniProtKB
    43. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    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

    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 PROSITE-ProRule annotation. 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.By similarity

    GO - Cellular componenti

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

    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 gammaPRO_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.By similarity

    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.By similarity

    Structurei

    3D structure databases

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

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni205 – 28076Interaction with FAM120BBy similarityAdd
    BLAST
    Regioni317 – 505189Ligand-bindingBy similarityAdd
    BLAST

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri139 – 15921NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri176 – 19823NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    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

    Experimental Info

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

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3030Missing in isoform 1. 3 PublicationsVSP_003649Add
    BLAST

    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: October 1, 2014
    This is version 145 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