Q9QYK2 · PRGC1_RAT
- ProteinPeroxisome proliferator-activated receptor gamma coactivator 1-alpha
- GenePpargc1a
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids796 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
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).
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 annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended namePeroxisome proliferator-activated receptor gamma coactivator 1-alpha
- Short namesPGC-1-alpha; PPAR-gamma coactivator 1-alpha; PPARGC-1-alpha
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ9QYK2
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000081735 | 1-796 | Peroxisome proliferator-activated receptor gamma coactivator 1-alpha | ||
Modified residue | 77 | N6-acetyllysine | |||
Modified residue | 144 | N6-acetyllysine | |||
Modified residue | 176 | Phosphothreonine; by AMPK | |||
Modified residue | 182 | N6-acetyllysine | |||
Modified residue | 252 | N6-acetyllysine | |||
Modified residue | 269 | N6-acetyllysine | |||
Modified residue | 276 | N6-acetyllysine | |||
Modified residue | 319 | N6-acetyllysine | |||
Modified residue | 345 | N6-acetyllysine | |||
Modified residue | 411 | N6-acetyllysine | |||
Modified residue | 440 | N6-acetyllysine | |||
Modified residue | 449 | N6-acetyllysine | |||
Modified residue | 537 | Phosphoserine; by AMPK | |||
Modified residue | 756 | N6-acetyllysine | |||
Modified residue | 777 | N6-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
- PTM
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).
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 | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 98-138 | Disordered | |||
Motif | 142-146 | LXXLL motif | |||
Region | 211-275 | Disordered | |||
Compositional bias | 220-239 | Basic and acidic residues | |||
Compositional bias | 240-275 | Polar residues | |||
Compositional bias | 288-304 | Polar residues | |||
Region | 288-350 | Disordered | |||
Region | 291-337 | Interaction with PPARG | |||
Compositional bias | 331-350 | Polar residues | |||
Region | 348-796 | Mediates interaction with RNF34 | |||
Compositional bias | 541-564 | Polar residues | |||
Region | 541-597 | Disordered | |||
Compositional bias | 574-597 | Polar residues | |||
Region | 611-669 | Disordered | |||
Compositional bias | 626-669 | Basic and acidic residues | |||
Domain | 675-751 | RRM | |||
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length796
- Mass (Da)90,622
- Last updated2000-05-01 v1
- ChecksumCF30A35F95088240
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8L2Q1Y2 | A0A8L2Q1Y2_RAT | Ppargc1a | 723 | ||
A0A8I6AWK0 | A0A8I6AWK0_RAT | Ppargc1a | 786 | ||
A0A8I5Y905 | A0A8I5Y905_RAT | Ppargc1a | 785 | ||
A0A8I6A531 | A0A8I6A531_RAT | Ppargc1a | 695 |
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 220-239 | Basic and acidic residues | |||
Compositional bias | 240-275 | Polar residues | |||
Compositional bias | 288-304 | Polar residues | |||
Compositional bias | 331-350 | Polar residues | |||
Sequence conflict | 427 | in Ref. 2 | |||
Compositional bias | 541-564 | Polar residues | |||
Sequence conflict | 564 | in Ref. 2 | |||
Compositional bias | 574-597 | Polar residues | |||
Compositional bias | 626-669 | Basic and acidic residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB025784 EMBL· GenBank· DDBJ | BAA88982.1 EMBL· GenBank· DDBJ | mRNA | ||
AY237127 EMBL· GenBank· DDBJ | AAO89279.1 EMBL· GenBank· DDBJ | mRNA |