Q9QYK2 · PRGC1_RAT

  • Protein
    Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
  • Gene
    Ppargc1a
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    5/5

Function

function

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. Acts as a key regulator of gluconeogenesis: stimulates hepatic gluconeogenesis by increasing the expression of gluconeogenic enzymes, and acting together with FOXO1 to promote the fasting gluconeogenic program (By similarity).
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 BMAL1 and NR1D1, through the coactivation of RORA and RORC, and metabolic genes, such as PDK4 and PEPCK (By similarity).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentapical dendrite
Cellular Componentcytosolic ribosome
Cellular Componenteuchromatin
Cellular Componentneuronal cell body
Cellular Componentnucleus
Cellular ComponentPML body
Molecular Functionalpha-tubulin binding
Molecular Functionchromatin binding
Molecular Functionchromatin DNA binding
Molecular FunctionDNA binding
Molecular FunctionlncRNA binding
Molecular Functionnuclear estrogen receptor binding
Molecular Functionnuclear receptor binding
Molecular Functionnuclear receptor coactivator activity
Molecular Functionperoxisome proliferator activated receptor binding
Molecular Functionpromoter-specific chromatin binding
Molecular FunctionRNA polymerase II-specific DNA-binding transcription factor binding
Molecular Functionsequence-specific DNA binding
Molecular Functiontranscription coactivator activity
Molecular Functiontranscription coregulator activity
Molecular Functionubiquitin protein ligase binding
Biological Processadaptive thermogenesis
Biological Processadipose tissue development
Biological Processandrogen metabolic process
Biological Processautophagy of mitochondrion
Biological Processcellular response to caffeine
Biological Processcellular response to estradiol stimulus
Biological Processcellular response to fatty acid
Biological Processcellular response to follicle-stimulating hormone stimulus
Biological Processcellular response to fructose stimulus
Biological Processcellular response to glucose stimulus
Biological Processcellular response to hypoxia
Biological Processcellular response to interleukin-6
Biological Processcellular response to ionomycin
Biological Processcellular response to lipopolysaccharide
Biological Processcellular response to nitrite
Biological Processcellular response to oxidative stress
Biological Processcellular response to potassium ion
Biological Processcellular response to resveratrol
Biological Processcellular response to thyroid hormone stimulus
Biological Processcellular response to transforming growth factor beta stimulus
Biological Processcellular response to tumor necrosis factor
Biological Processcerebellum development
Biological Processcircadian regulation of gene expression
Biological Processenergy homeostasis
Biological Processfatty acid oxidation
Biological Processflavone metabolic process
Biological Processforebrain development
Biological Processgalactose metabolic process
Biological Processgluconeogenesis
Biological Processmitochondrion organization
Biological Processnegative regulation of glycolytic process
Biological Processnegative regulation of mitochondrial fission
Biological Processnegative regulation of neuron apoptotic process
Biological Processnegative regulation of smooth muscle cell migration
Biological Processnegative regulation of smooth muscle cell proliferation
Biological Processneuron apoptotic process
Biological Processpositive regulation of cold-induced thermogenesis
Biological Processpositive regulation of DNA-binding transcription factor activity
Biological Processpositive regulation of DNA-templated transcription
Biological Processpositive regulation of fatty acid oxidation
Biological Processpositive regulation of gene expression
Biological Processpositive regulation of podocyte apoptotic process
Biological Processpositive regulation of progesterone biosynthetic process
Biological Processpositive regulation of transcription by RNA polymerase II
Biological Processpositive regulation of vascular associated smooth muscle cell proliferation
Biological Processregulation of circadian rhythm
Biological Processregulation of DNA-templated transcription
Biological Processrespiratory electron transport chain
Biological Processresponse to activity
Biological Processresponse to dehydroepiandrosterone
Biological Processresponse to dietary excess
Biological Processresponse to electrical stimulus
Biological Processresponse to electrical stimulus involved in regulation of muscle adaptation
Biological Processresponse to epinephrine
Biological Processresponse to fructose
Biological Processresponse to hypobaric hypoxia
Biological Processresponse to hypoxia
Biological Processresponse to ischemia
Biological Processresponse to L-leucine
Biological Processresponse to methionine
Biological Processresponse to muscle activity
Biological Processresponse to norepinephrine
Biological Processresponse to nutrient
Biological Processresponse to nutrient levels
Biological Processresponse to organic cyclic compound
Biological Processresponse to reactive oxygen species
Biological Processresponse to starvation
Biological Processresponse to thyroid hormone
Biological Processresponse to xenobiotic stimulus
Biological Processskeletal muscle atrophy

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
  • Short names
    PGC-1-alpha; PPAR-gamma coactivator 1-alpha; PPARGC-1-alpha

Gene names

    • Name
      Ppargc1a
    • Synonyms
      Pgc1, Pgc1a, Ppargc1

Organism names

  • Taxonomic identifier
  • Strain
    • Zucker
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    Q9QYK2

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_00000817351-796Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
Modified residue77N6-acetyllysine
Modified residue144N6-acetyllysine
Modified residue176Phosphothreonine; by AMPK
Modified residue182N6-acetyllysine
Modified residue252N6-acetyllysine
Modified residue269N6-acetyllysine
Modified residue276N6-acetyllysine
Modified residue319N6-acetyllysine
Modified residue345N6-acetyllysine
Modified residue411N6-acetyllysine
Modified residue440N6-acetyllysine
Modified residue449N6-acetyllysine
Modified residue537Phosphoserine; by AMPK
Modified residue756N6-acetyllysine
Modified residue777N6-acetyllysine

Post-translational modification

Phosphorylation by AMPK in skeletal muscle increases activation of its own promoter. Phosphorylated by CLK2.
Heavily acetylated by KAT2A/GCN5 under conditions of high nutrients, leading to inactivation of PPARGC1A. Deacetylated by SIRT1 in low nutrients/high NAD conditions, leading to its activation.
Ubiquitinated. Ubiquitination by RNF34 induces proteasomal degradation.

Keywords

Proteomic databases

PTM databases

Expression

Induction

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.

Gene expression databases

Interaction

Subunit

Homooligomer (By similarity).
Interacts with MYBBP1A; inhibits MYBBP1A transcriptional activation. Interacts with PRDM16, LPIN1 and PML. Interacts (via LXXLL motif) with RORA and RORC (via AF-2 motif); activates RORA and RORC transcriptional activation (By similarity).
Interacts with LRPPRC (By similarity).
Interacts with FOXO1 (By similarity).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, motif, compositional bias, domain.

Type
IDPosition(s)Description
Region98-138Disordered
Motif142-146LXXLL motif
Region211-275Disordered
Compositional bias220-239Basic and acidic residues
Compositional bias240-275Polar residues
Compositional bias288-304Polar residues
Region288-350Disordered
Region291-337Interaction with PPARG
Compositional bias331-350Polar residues
Region348-796Mediates interaction with RNF34
Compositional bias541-564Polar residues
Region541-597Disordered
Compositional bias574-597Polar residues
Region611-669Disordered
Compositional bias626-669Basic and acidic residues
Domain675-751RRM

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    796
  • Mass (Da)
    90,622
  • Last updated
    2000-05-01 v1
  • Checksum
    CF30A35F95088240
MAWDMCSQDSVWSDIECAALVGEDQPLCPDLPELDLSELDVNDLDTDSFLGGLKWCSDQSEIISNQYNNEPANIFEKIDEENEANLLAVLTETLDSLPVDEDGLPSFDALTDGDVTTDNEASPSSMPDGTPPPQEAEEPSLLKKLLLAPANTQLSYNECSGLSTQNHANHTHRIRTNPAIVKTENSWSNKAKSICQQQKPQRRPCSELLKYLTTNDDPPHTKPTENRNSSRDKCASKKKSHTQPQSQHAQAKPTTLSLPLTPESPNDPKGSPFENKTIERTLSVELSGTAGLTPPTTPPHKANQDNPFKASPKLKPSCKTVVPPPTKRARYSECSGTQGSHSTKKGPEQSELYAQLSKSSVLSRGHEERKTKRPSLRLFGDHDYCQSVNSKTDILINISQELQDSRQLDFKDASCDWQGHICSSTDSSQCYLRETLEASKQVSPCSTRKQLQDQEIRAELNKHFGHPSQAVFDDKVDKTSELRDGNFSNEQFSKLPVFINSGLAMDGLFDDSEDENDKLSYPWDGTQSYSLFDVSPSCSSFNSPCRDSVSPPKSLFSQRPQRMRSRSRSFSRHRSCSRSPYSRSRSRSPGSRSSSRSCYYYESSHYRHRTHRNSPLYVRSRSRSPYSRRPRYDSYEANEHERLKRDEYRREYEKRESERAKQRERQKQKAIEERRVIYVGKIRPDTTRTELRDRFEVFGEIEECTVNLRDDGDSYGFITYRYTCDAFAALENGYTLRRSNETDFELYFCGRKQFFKSNYADLDSNSDDFDPASTKSKYDSLDFDSLLKEAQRSLRR

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A8L2Q1Y2A0A8L2Q1Y2_RATPpargc1a723
A0A8I6AWK0A0A8I6AWK0_RATPpargc1a786
A0A8I5Y905A0A8I5Y905_RATPpargc1a785
A0A8I6A531A0A8I6A531_RATPpargc1a695

Features

Showing features for compositional bias, sequence conflict.

Type
IDPosition(s)Description
Compositional bias220-239Basic and acidic residues
Compositional bias240-275Polar residues
Compositional bias288-304Polar residues
Compositional bias331-350Polar residues
Sequence conflict427in Ref. 2
Compositional bias541-564Polar residues
Sequence conflict564in Ref. 2
Compositional bias574-597Polar residues
Compositional bias626-669Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB025784
EMBL· GenBank· DDBJ
BAA88982.1
EMBL· GenBank· DDBJ
mRNA
AY237127
EMBL· GenBank· DDBJ
AAO89279.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help