Q9QYK2 (PRGC1_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Ppargc1a
Synonyms:	Pgc1, Pgc1a, Ppargc1

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	796 AA.
Sequence status	Complete.
Protein existence	Evidence 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 By similarity.
Subunit structure	Homooligomer. Binds MYBBP1A, which inhibits transcriptional activation by this protein By similarity. Interacts with LRPPRC By similarity. Interacts with PRDM16 By similarity. Interacts with LPIN1 By similarity. Interacts with PML By similarity.
Subcellular location	Nucleus By similarity. Nucleus › PML 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 process	Transcription Transcription regulation
Cellular component	Nucleus
Ligand	RNA-binding
Molecular function	Activator
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	androgen 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 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 17099248. Source: RGD negative regulation of glycolysis 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 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 mitochondrion organization Inferred from sequence or structural similarity. Source: UniProtKB 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 regulation of N-methyl-D-aspartate selective glutamate receptor activity Inferred from mutant phenotype PubMed 22593067. Source: RGD respiratory electron transport chain Inferred from sequence or structural similarity. Source: UniProtKB response to cold Inferred from expression pattern PubMed 23100029. Source: RGD response to epinephrine stimulus Inferred from expression pattern PubMed 22496244. 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 stimulus Inferred from expression pattern PubMed 23443926. 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-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	PML 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_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW chromatin DNA binding Inferred from sequence or structural similarity. Source: UniProtKB ligand-dependent nuclear receptor transcription coactivator activity Inferred from electronic annotation. Source: Compara nucleotide binding Inferred from electronic annotation. Source: InterPro transcription coactivator activity Inferred from direct assay PubMed 12107181. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 796	796	Peroxisome proliferator-activated receptor gamma coactivator 1-alpha		PRO_0000081735
Regions
	Domain	675 – 751	77	RRM
	Region	291 – 337	47	Interaction with PPARG By similarity
	Motif	142 – 146	5	LXXLL motif
	Compositional bias	564 – 597	34	Arg/Ser-rich
	Compositional bias	619 – 631	13	Arg/Ser-rich
Amino acid modifications
	Modified residue	77	1	N6-acetyllysine By similarity
	Modified residue	144	1	N6-acetyllysine By similarity
	Modified residue	176	1	Phosphothreonine; by AMPK By similarity
	Modified residue	182	1	N6-acetyllysine By similarity
	Modified residue	252	1	N6-acetyllysine By similarity
	Modified residue	269	1	N6-acetyllysine By similarity
	Modified residue	276	1	N6-acetyllysine By similarity
	Modified residue	319	1	N6-acetyllysine By similarity
	Modified residue	345	1	N6-acetyllysine By similarity
	Modified residue	411	1	N6-acetyllysine By similarity
	Modified residue	440	1	N6-acetyllysine By similarity
	Modified residue	449	1	N6-acetyllysine By similarity
	Modified residue	537	1	Phosphoserine; by AMPK By similarity
	Modified residue	756	1	N6-acetyllysine By similarity
	Modified residue	777	1	N6-acetyllysine By similarity
Experimental info
	Sequence conflict	427	1	S → L Ref.2
	Sequence conflict	564	1	R → H Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9QYK2 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: CF30A35F95088240	FASTA	796	90,622
	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

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.
IPI	IPI00214207.
PIR	JC7355.
RefSeq	NP_112637.1. NM_031347.1.
UniGene	Rn.19172.
3D structure databases
ProteinModelPortal	Q9QYK2.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9QYK2. 1 interaction.
STRING	10116.ENSRNOP00000006071.
PTM databases
PhosphoSite	Q9QYK2.
Proteomic databases
PaxDb	Q9QYK2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000006071; ENSRNOP00000006071; ENSRNOG00000004473.
GeneID	83516.
KEGG	rno:83516.
Organism-specific databases
CTD	10891.
RGD	620925. Ppargc1a.
Phylogenomic databases
eggNOG	NOG78353.
GeneTree	ENSGT00530000063196.
HOGENOM	HOG000037431.
HOVERGEN	HBG053678.
InParanoid	Q9QYK2.
KO	K07202.
OMA	RLFGDHD.
OrthoDB	EOG4T782R.
Gene expression databases
ArrayExpress	Q9QYK2.
Genevestigator	Q9QYK2.
GermOnline	ENSRNOG00000004473. Rattus norvegicus.
Family and domain databases
Gene3D	3.30.70.330. 1 hit.
InterPro	IPR012677. Nucleotide-bd_a/b_plait. IPR000504. RRM_dom. [Graphical view]
Pfam	PF00076. RRM_1. 1 hit. [Graphical view]
SMART	SM00360. RRM. 1 hit. [Graphical view]
PROSITE	PS50102. RRM. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	615978.

Entry information

Entry name

PRGC1_RAT

Accession

Primary (citable) accession number: Q9QYK2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2004
Last sequence update:	May 1, 2000
Last modified:	May 29, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program