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Q9QYK2

- PRGC1_RAT

UniProt

Q9QYK2 - PRGC1_RAT

Protein

Peroxisome proliferator-activated receptor gamma coactivator 1-alpha

Gene

Ppargc1a

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Transcriptional coactivator for steroid receptors and nuclear receptors. Greatly increases the transcriptional activity of PPARG and thyroid hormone receptor on the uncoupling protein promoter. Can regulate key mitochondrial genes that contribute to the program of adaptive thermogenesis. Plays an essential role in metabolic reprogramming in response to dietary availability through coordination of the expression of a wide array of genes involved in glucose and fatty acid metabolism. Induces the expression of PERM1 in the skeletal muscle in an ESRRA-dependent manner. Also involved in the integration of the circadian rhythms and energy metabolism. Required for oscillatory expression of clock genes, such as ARNTL/BMAL1 and NR1D1, through the coactivation of RORA and RORC, and metabolic genes, such as PDK4 and PEPCK By similarity.By similarity

    GO - Molecular functioni

    1. chromatin binding Source: RGD
    2. chromatin DNA binding Source: UniProtKB
    3. DNA binding Source: UniProtKB
    4. ligand-dependent nuclear receptor transcription coactivator activity Source: Ensembl
    5. nucleotide binding Source: InterPro
    6. RNA binding Source: UniProtKB-KW
    7. sequence-specific DNA binding Source: UniProtKB
    8. transcription coactivator activity Source: RGD

    GO - Biological processi

    1. androgen metabolic process Source: RGD
    2. cellular response to fatty acid Source: RGD
    3. cellular response to hypoxia Source: RGD
    4. cellular response to nitrite Source: RGD
    5. cellular response to oxidative stress Source: UniProtKB
    6. cellular response to thyroid hormone stimulus Source: RGD
    7. cellular response to tumor necrosis factor Source: RGD
    8. circadian regulation of gene expression Source: UniProtKB
    9. flavone metabolic process Source: RGD
    10. galactose metabolic process Source: RGD
    11. mitochondrion organization Source: RGD
    12. negative regulation of glycolytic process Source: RGD
    13. negative regulation of neuron apoptotic process Source: UniProtKB
    14. negative regulation of receptor activity Source: RGD
    15. neuron death Source: UniProtKB
    16. positive regulation of ATP biosynthetic process Source: UniProtKB
    17. positive regulation of cellular metabolic process Source: RGD
    18. positive regulation of cellular respiration Source: Ensembl
    19. positive regulation of energy homeostasis Source: UniProtKB
    20. positive regulation of fatty acid oxidation Source: RGD
    21. positive regulation of mitochondrial DNA metabolic process Source: Ensembl
    22. positive regulation of mitochondrion organization Source: UniProtKB
    23. positive regulation of muscle tissue development Source: Ensembl
    24. positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
    25. positive regulation of smooth muscle cell proliferation Source: RGD
    26. positive regulation of transcription, DNA-templated Source: RGD
    27. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    28. regulation of cell death Source: UniProtKB
    29. regulation of circadian rhythm Source: UniProtKB
    30. regulation of N-methyl-D-aspartate selective glutamate receptor activity Source: RGD
    31. regulation of transcription, DNA-templated Source: UniProtKB
    32. respiratory electron transport chain Source: UniProtKB
    33. response to activity Source: RGD
    34. response to cold Source: RGD
    35. response to drug Source: RGD
    36. response to epinephrine Source: RGD
    37. response to hypoxia Source: RGD
    38. response to leucine Source: RGD
    39. response to muscle activity Source: UniProtKB
    40. response to norepinephrine Source: RGD
    41. response to nutrient levels Source: RGD
    42. response to organic cyclic compound Source: RGD
    43. response to starvation Source: RGD
    44. response to statin Source: RGD
    45. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Biological rhythms, Transcription, Transcription regulation

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_196405. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
    REACT_196408. PPARA activates gene expression.
    REACT_196852. REV-ERBA represses gene expression.
    REACT_196856. RORA activates circadian gene expression.
    REACT_209077. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
    REACT_216049. Transcriptional activation of mitochondrial biogenesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
    Short name:
    PGC-1-alpha
    Short name:
    PPAR-gamma coactivator 1-alpha
    Short name:
    PPARGC-1-alpha
    Gene namesi
    Name:Ppargc1a
    Synonyms:Pgc1, Pgc1a, Ppargc1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 14

    Organism-specific databases

    RGDi620925. Ppargc1a.

    Subcellular locationi

    Nucleus By similarity. NucleusPML body By similarity

    GO - Cellular componenti

    1. cytosol Source: RGD
    2. nucleus Source: RGD
    3. PML body Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 796796Peroxisome proliferator-activated receptor gamma coactivator 1-alphaPRO_0000081735Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei77 – 771N6-acetyllysineBy similarity
    Modified residuei144 – 1441N6-acetyllysineBy similarity
    Modified residuei176 – 1761Phosphothreonine; by AMPKBy similarity
    Modified residuei182 – 1821N6-acetyllysineBy similarity
    Modified residuei252 – 2521N6-acetyllysineBy similarity
    Modified residuei269 – 2691N6-acetyllysineBy similarity
    Modified residuei276 – 2761N6-acetyllysineBy similarity
    Modified residuei319 – 3191N6-acetyllysineBy similarity
    Modified residuei345 – 3451N6-acetyllysineBy similarity
    Modified residuei411 – 4111N6-acetyllysineBy similarity
    Modified residuei440 – 4401N6-acetyllysineBy similarity
    Modified residuei449 – 4491N6-acetyllysineBy similarity
    Modified residuei537 – 5371Phosphoserine; by AMPKBy similarity
    Modified residuei756 – 7561N6-acetyllysineBy similarity
    Modified residuei777 – 7771N6-acetyllysineBy similarity

    Post-translational modificationi

    Phosphorylation by AMPK in skeletal muscle increases activation of its own promoter. Phosphorylated by CLK2.By similarity
    Heavily acetylated by GCN5 and biologically inactive under conditions of high nutrients. Deacetylated by SIRT1 in low nutrients/high NAD conditions By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiQ9QYK2.

    PTM databases

    PhosphoSiteiQ9QYK2.

    Expressioni

    Inductioni

    Up-regulated in brown adipose tissue of diabetic fatty (fa/fa) rats. Exposure of fa/fa rats to cold resulted in a much smaller increase as compared to lean rats in which a 2.6 fold increase was seen. Leptin is required for normal basal and cold-stimulated expression in brown adipose tissue and hyperleptinemia rapidly up-regulates its expression. It is induced not only by cold exposure but also by prolonged low-intensity physical exercise in epitrochlearis muscle.2 Publications

    Gene expression databases

    GenevestigatoriQ9QYK2.

    Interactioni

    Subunit structurei

    Homooligomer. Interacts with MYBBP1A; inhibits MYBBP1A transcriptional activation. Interacts with LRPPRC, PRDM16, LPIN1 and PML. Interacts (via LXXLL motif) with RORA and RORC (via AF-2 motif); activates RORA and RORC transcriptional activation By similarity.By similarity

    Protein-protein interaction databases

    IntActiQ9QYK2. 1 interaction.
    STRINGi10116.ENSRNOP00000006071.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9QYK2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini675 – 75177RRMPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni291 – 33747Interaction with PPARGBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi142 – 1465LXXLL motif

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi564 – 59734Arg/Ser-richAdd
    BLAST
    Compositional biasi619 – 63113Arg/Ser-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG78353.
    GeneTreeiENSGT00530000063196.
    HOGENOMiHOG000037431.
    HOVERGENiHBG053678.
    InParanoidiQ9QYK2.
    KOiK07202.
    OMAiENGYTLR.
    OrthoDBiEOG7S4X5H.
    PhylomeDBiQ9QYK2.
    TreeFamiTF343068.

    Family and domain databases

    Gene3Di3.30.70.330. 1 hit.
    InterProiIPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view]
    PfamiPF00076. RRM_1. 1 hit.
    [Graphical view]
    SMARTiSM00360. RRM. 1 hit.
    [Graphical view]
    PROSITEiPS50102. RRM. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9QYK2-1 [UniParc]FASTAAdd to Basket

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    MAWDMCSQDS VWSDIECAAL VGEDQPLCPD LPELDLSELD VNDLDTDSFL    50
    GGLKWCSDQS EIISNQYNNE PANIFEKIDE ENEANLLAVL TETLDSLPVD 100
    EDGLPSFDAL TDGDVTTDNE ASPSSMPDGT PPPQEAEEPS LLKKLLLAPA 150
    NTQLSYNECS GLSTQNHANH THRIRTNPAI VKTENSWSNK AKSICQQQKP 200
    QRRPCSELLK YLTTNDDPPH TKPTENRNSS RDKCASKKKS HTQPQSQHAQ 250
    AKPTTLSLPL TPESPNDPKG SPFENKTIER TLSVELSGTA GLTPPTTPPH 300
    KANQDNPFKA SPKLKPSCKT VVPPPTKRAR YSECSGTQGS HSTKKGPEQS 350
    ELYAQLSKSS VLSRGHEERK TKRPSLRLFG DHDYCQSVNS KTDILINISQ 400
    ELQDSRQLDF KDASCDWQGH ICSSTDSSQC YLRETLEASK QVSPCSTRKQ 450
    LQDQEIRAEL NKHFGHPSQA VFDDKVDKTS ELRDGNFSNE QFSKLPVFIN 500
    SGLAMDGLFD DSEDENDKLS YPWDGTQSYS LFDVSPSCSS FNSPCRDSVS 550
    PPKSLFSQRP QRMRSRSRSF SRHRSCSRSP YSRSRSRSPG SRSSSRSCYY 600
    YESSHYRHRT HRNSPLYVRS RSRSPYSRRP RYDSYEANEH ERLKRDEYRR 650
    EYEKRESERA KQRERQKQKA IEERRVIYVG KIRPDTTRTE LRDRFEVFGE 700
    IEECTVNLRD DGDSYGFITY RYTCDAFAAL ENGYTLRRSN ETDFELYFCG 750
    RKQFFKSNYA DLDSNSDDFD PASTKSKYDS LDFDSLLKEA QRSLRR 796
    Length:796
    Mass (Da):90,622
    Last modified:May 1, 2000 - v1
    Checksum:iCF30A35F95088240
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti427 – 4271S → L(PubMed:10913342)Curated
    Sequence conflicti564 – 5641R → H(PubMed:10913342)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB025784 mRNA. Translation: BAA88982.1.
    AY237127 mRNA. Translation: AAO89279.1.
    PIRiJC7355.
    RefSeqiNP_112637.1. NM_031347.1.
    UniGeneiRn.19172.

    Genome annotation databases

    EnsembliENSRNOT00000006071; ENSRNOP00000006071; ENSRNOG00000004473.
    GeneIDi83516.
    KEGGirno:83516.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB025784 mRNA. Translation: BAA88982.1 .
    AY237127 mRNA. Translation: AAO89279.1 .
    PIRi JC7355.
    RefSeqi NP_112637.1. NM_031347.1.
    UniGenei Rn.19172.

    3D structure databases

    ProteinModelPortali Q9QYK2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9QYK2. 1 interaction.
    STRINGi 10116.ENSRNOP00000006071.

    PTM databases

    PhosphoSitei Q9QYK2.

    Proteomic databases

    PaxDbi Q9QYK2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000006071 ; ENSRNOP00000006071 ; ENSRNOG00000004473 .
    GeneIDi 83516.
    KEGGi rno:83516.

    Organism-specific databases

    CTDi 10891.
    RGDi 620925. Ppargc1a.

    Phylogenomic databases

    eggNOGi NOG78353.
    GeneTreei ENSGT00530000063196.
    HOGENOMi HOG000037431.
    HOVERGENi HBG053678.
    InParanoidi Q9QYK2.
    KOi K07202.
    OMAi ENGYTLR.
    OrthoDBi EOG7S4X5H.
    PhylomeDBi Q9QYK2.
    TreeFami TF343068.

    Enzyme and pathway databases

    Reactomei REACT_196405. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
    REACT_196408. PPARA activates gene expression.
    REACT_196852. REV-ERBA represses gene expression.
    REACT_196856. RORA activates circadian gene expression.
    REACT_209077. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
    REACT_216049. Transcriptional activation of mitochondrial biogenesis.

    Miscellaneous databases

    NextBioi 615978.
    PROi Q9QYK2.

    Gene expression databases

    Genevestigatori Q9QYK2.

    Family and domain databases

    Gene3Di 3.30.70.330. 1 hit.
    InterProi IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view ]
    Pfami PF00076. RRM_1. 1 hit.
    [Graphical view ]
    SMARTi SM00360. RRM. 1 hit.
    [Graphical view ]
    PROSITEi PS50102. RRM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Role of leptin in peroxisome proliferator-activated receptor gamma coactivator-1 expression."
      Kakuma T., Wang Z.-W., Pan W., Unger R.H., Zhou Y.-T.
      Endocrinology 141:4576-4582(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
      Strain: Zucker.
      Tissue: Heart.
    2. "cDNA cloning and mRNA analysis of PGC-1 in epitrochlearis muscle in swimming-exercised rats."
      Goto M., Terada S., Kato M., Katoh M., Yokozeki T., Tabata I., Shimokawa T.
      Biochem. Biophys. Res. Commun. 274:350-354(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
    3. "Rattus norvegicus PGC1 mRNA."
      Kofman A.V.
      Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiPRGC1_RAT
    AccessioniPrimary (citable) accession number: Q9QYK2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2004
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 108 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