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Q9QYK2 (PRGC1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Ppargc1a
Synonyms:Pgc1, Pgc1a, Ppargc1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length796 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

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. 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.

Subunit structure

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.

Subcellular location

Nucleus By similarity. NucleusPML body By similarity.

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. Ref.1 Ref.2

Post-translational modification

Phosphorylation by AMPK in skeletal muscle increases activation of its own promoter By similarity. 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.

Sequence similarities

Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
   Biological processBiological rhythms
Transcription
Transcription regulation
   Cellular componentNucleus
   LigandRNA-binding
   Molecular functionActivator
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processandrogen metabolic process

Inferred from expression pattern PubMed 23338851. Source: RGD

cellular response to fatty acid

Inferred from expression pattern PubMed 22676303. Source: RGD

cellular response to hypoxia

Inferred from expression pattern PubMed 22527940. Source: RGD

cellular response to nitrite

Inferred from expression pattern PubMed 22892143. Source: RGD

cellular response to oxidative stress

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to thyroid hormone stimulus

Inferred from expression pattern PubMed 23209300. Source: RGD

cellular response to tumor necrosis factor

Inferred from expression pattern PubMed 22343369. Source: RGD

circadian regulation of gene expression

Inferred from sequence or structural similarity. Source: UniProtKB

flavone metabolic process

Inferred from expression pattern PubMed 22767158. Source: RGD

galactose metabolic process

Inferred from expression pattern PubMed 23022596PubMed 23159434. Source: RGD

mitochondrion organization

Inferred from mutant phenotype PubMed 17099248PubMed 22633948. Source: RGD

negative regulation of glycolytic process

Inferred from mutant phenotype PubMed 22343369. Source: RGD

negative regulation of neuron apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of receptor activity

Inferred from mutant phenotype PubMed 22593067. Source: RGD

neuron death

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of ATP biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cellular metabolic process

Inferred from mutant phenotype PubMed 22527940. Source: RGD

positive regulation of cellular respiration

Inferred from electronic annotation. Source: Ensembl

positive regulation of energy homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of fatty acid oxidation

Inferred from mutant phenotype PubMed 16139565PubMed 23250358. Source: RGD

positive regulation of mitochondrial DNA metabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of mitochondrion organization

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of muscle tissue development

Inferred from electronic annotation. Source: Ensembl

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of smooth muscle cell proliferation

Inferred from mutant phenotype PubMed 22527940. Source: RGD

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 16139565. Source: RGD

regulation of N-methyl-D-aspartate selective glutamate receptor activity

Inferred from mutant phenotype PubMed 22593067. Source: RGD

regulation of cell death

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of circadian rhythm

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

respiratory electron transport chain

Inferred from sequence or structural similarity. Source: UniProtKB

response to activity

Inferred from expression pattern PubMed 20433743. Source: RGD

response to cold

Inferred from expression pattern PubMed 23100029. Source: RGD

response to drug

Inferred from expression pattern PubMed 23443926. Source: RGD

response to epinephrine

Inferred from expression pattern PubMed 22496244. Source: RGD

response to hypoxia

Inferred from expression pattern PubMed 20875806. Source: RGD

response to leucine

Inferred from expression pattern PubMed 22612562. Source: RGD

response to muscle activity

Inferred from sequence or structural similarity. Source: UniProtKB

response to norepinephrine

Inferred from expression pattern PubMed 23443926. Source: RGD

response to nutrient levels

Inferred from expression pattern PubMed 22773756. Source: RGD

response to organic cyclic compound

Inferred from expression pattern PubMed 23104933. Source: RGD

response to starvation

Inferred from expression pattern PubMed 22117073. Source: RGD

response to statin

Inferred from expression pattern PubMed 22343369. Source: RGD

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentPML body

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from direct assay PubMed 17099248. Source: RGD

nucleus

Inferred from direct assay PubMed 17099248. Source: RGD

   Molecular_functionDNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

chromatin DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

chromatin binding

Inferred from direct assay PubMed 22705949. Source: RGD

ligand-dependent nuclear receptor transcription coactivator activity

Inferred from electronic annotation. Source: Ensembl

nucleotide binding

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

transcription coactivator activity

Inferred from direct assay PubMed 12107181. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 796796Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
PRO_0000081735

Regions

Domain675 – 75177RRM
Region291 – 33747Interaction with PPARG By similarity
Motif142 – 1465LXXLL motif
Compositional bias564 – 59734Arg/Ser-rich
Compositional bias619 – 63113Arg/Ser-rich

Amino acid modifications

Modified residue771N6-acetyllysine By similarity
Modified residue1441N6-acetyllysine By similarity
Modified residue1761Phosphothreonine; by AMPK By similarity
Modified residue1821N6-acetyllysine By similarity
Modified residue2521N6-acetyllysine By similarity
Modified residue2691N6-acetyllysine By similarity
Modified residue2761N6-acetyllysine By similarity
Modified residue3191N6-acetyllysine By similarity
Modified residue3451N6-acetyllysine By similarity
Modified residue4111N6-acetyllysine By similarity
Modified residue4401N6-acetyllysine By similarity
Modified residue4491N6-acetyllysine By similarity
Modified residue5371Phosphoserine; by AMPK By similarity
Modified residue7561N6-acetyllysine By similarity
Modified residue7771N6-acetyllysine By similarity

Experimental info

Sequence conflict4271S → L Ref.2
Sequence conflict5641R → H Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9QYK2 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: CF30A35F95088240

FASTA79690,622
        10         20         30         40         50         60 
MAWDMCSQDS VWSDIECAAL VGEDQPLCPD LPELDLSELD VNDLDTDSFL GGLKWCSDQS 

        70         80         90        100        110        120 
EIISNQYNNE PANIFEKIDE ENEANLLAVL TETLDSLPVD EDGLPSFDAL TDGDVTTDNE 

       130        140        150        160        170        180 
ASPSSMPDGT PPPQEAEEPS LLKKLLLAPA NTQLSYNECS GLSTQNHANH THRIRTNPAI 

       190        200        210        220        230        240 
VKTENSWSNK AKSICQQQKP QRRPCSELLK YLTTNDDPPH TKPTENRNSS RDKCASKKKS 

       250        260        270        280        290        300 
HTQPQSQHAQ AKPTTLSLPL TPESPNDPKG SPFENKTIER TLSVELSGTA GLTPPTTPPH 

       310        320        330        340        350        360 
KANQDNPFKA SPKLKPSCKT VVPPPTKRAR YSECSGTQGS HSTKKGPEQS ELYAQLSKSS 

       370        380        390        400        410        420 
VLSRGHEERK TKRPSLRLFG DHDYCQSVNS KTDILINISQ ELQDSRQLDF KDASCDWQGH 

       430        440        450        460        470        480 
ICSSTDSSQC YLRETLEASK QVSPCSTRKQ LQDQEIRAEL NKHFGHPSQA VFDDKVDKTS 

       490        500        510        520        530        540 
ELRDGNFSNE QFSKLPVFIN SGLAMDGLFD DSEDENDKLS YPWDGTQSYS LFDVSPSCSS 

       550        560        570        580        590        600 
FNSPCRDSVS PPKSLFSQRP QRMRSRSRSF SRHRSCSRSP YSRSRSRSPG SRSSSRSCYY 

       610        620        630        640        650        660 
YESSHYRHRT HRNSPLYVRS RSRSPYSRRP RYDSYEANEH ERLKRDEYRR EYEKRESERA 

       670        680        690        700        710        720 
KQRERQKQKA IEERRVIYVG KIRPDTTRTE LRDRFEVFGE IEECTVNLRD DGDSYGFITY 

       730        740        750        760        770        780 
RYTCDAFAAL ENGYTLRRSN ETDFELYFCG RKQFFKSNYA DLDSNSDDFD PASTKSKYDS 

       790 
LDFDSLLKEA QRSLRR 

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References

[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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB025784 mRNA. Translation: BAA88982.1.
AY237127 mRNA. Translation: AAO89279.1.
PIRJC7355.
RefSeqNP_112637.1. NM_031347.1.
UniGeneRn.19172.

3D structure databases

ProteinModelPortalQ9QYK2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9QYK2. 1 interaction.
STRING10116.ENSRNOP00000006071.

PTM databases

PhosphoSiteQ9QYK2.

Proteomic databases

PaxDbQ9QYK2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000006071; ENSRNOP00000006071; ENSRNOG00000004473.
GeneID83516.
KEGGrno:83516.

Organism-specific databases

CTD10891.
RGD620925. Ppargc1a.

Phylogenomic databases

eggNOGNOG78353.
GeneTreeENSGT00530000063196.
HOGENOMHOG000037431.
HOVERGENHBG053678.
InParanoidQ9QYK2.
KOK07202.
OMAENGYTLR.
OrthoDBEOG7S4X5H.
PhylomeDBQ9QYK2.
TreeFamTF343068.

Gene expression databases

GenevestigatorQ9QYK2.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio615978.
PROQ9QYK2.

Entry information

Entry namePRGC1_RAT
AccessionPrimary (citable) accession number: Q9QYK2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 1, 2000
Last modified: June 11, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families