PRGC1_MOUSE
ID PRGC1_MOUSE Reviewed; 797 AA.
AC O70343; L0AM20; L0AN96; L0APB0; Q3UP72;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Peroxisome proliferator-activated receptor gamma coactivator 1-alpha;
DE Short=PGC-1-alpha;
DE Short=PPAR-gamma coactivator 1-alpha;
DE Short=PPARGC-1-alpha;
GN Name=Ppargc1a; Synonyms=Pgc1, Pgc1a, Ppargc1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INDUCTION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Brown adipose tissue;
RX PubMed=9529258; DOI=10.1016/s0092-8674(00)81410-5;
RA Puigserver P., Wu Z., Park C.W., Graves R., Wright M., Spiegelman B.M.;
RT "A cold-inducible coactivator of nuclear receptors linked to adaptive
RT thermogenesis.";
RL Cell 92:829-839(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), FUNCTION, SUBCELLULAR
RP LOCATION, ALTERNATIVE PROMOTER USAGE, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=C57BL/6J; TISSUE=Skeletal muscle;
RX PubMed=23217713; DOI=10.1016/j.cell.2012.10.050;
RA Ruas J.L., White J.P., Rao R.R., Kleiner S., Brannan K.T., Harrison B.C.,
RA Greene N.P., Wu J., Estall J.L., Irving B.A., Lanza I.R., Rasbach K.A.,
RA Okutsu M., Nair K.S., Yan Z., Leinwand L.A., Spiegelman B.M.;
RT "A PGC-1alpha isoform induced by resistance training regulates skeletal
RT muscle hypertrophy.";
RL Cell 151:1319-1331(2012).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Spinal cord, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=CD-1; TISSUE=Neural stem cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INDUCTION.
RX PubMed=11108270; DOI=10.1210/endo.141.12.7804;
RA Kakuma T., Wang Z.-W., Pan W., Unger R.H., Zhou Y.-T.;
RT "Role of leptin in peroxisome proliferator-activated receptor gamma
RT coactivator-1 expression.";
RL Endocrinology 141:4576-4582(2000).
RN [7]
RP INTERACTION WITH FOXO1, AND FUNCTION.
RX PubMed=12754525; DOI=10.1038/nature01667;
RA Puigserver P., Rhee J., Donovan J., Walkey C.J., Yoon J.C., Oriente F.,
RA Kitamura Y., Altomonte J., Dong H., Accili D., Spiegelman B.M.;
RT "Insulin-regulated hepatic gluconeogenesis through FOXO1-PGC-1alpha
RT interaction.";
RL Nature 423:550-555(2003).
RN [8]
RP INTERACTION WITH MYBBP1A.
RX PubMed=14744933; DOI=10.1101/gad.1152204;
RA Fan M., Rhee J., St Pierre J., Handschin C., Puigserver P., Lin J.,
RA Jaeger S., Erdjument-Bromage H., Tempst P., Spiegelman B.M.;
RT "Suppression of mitochondrial respiration through recruitment of p160 myb
RT binding protein to PGC-1alpha: modulation by p38 MAPK.";
RL Genes Dev. 18:278-289(2004).
RN [9]
RP ACETYLATION, AND DEACETYLATION BY SIRT1.
RX PubMed=15716268; DOI=10.1074/jbc.m501485200;
RA Nemoto S., Fergusson M.M., Finkel T.;
RT "SIRT1 functionally interacts with the metabolic regulator and
RT transcriptional coactivator PGC-1{alpha}.";
RL J. Biol. Chem. 280:16456-16460(2005).
RN [10]
RP FUNCTION, ACETYLATION AT LYS-77; LYS-144; LYS-183; LYS-253; LYS-270;
RP LYS-277; LYS-320; LYS-346; LYS-412; LYS-441; LYS-450; LYS-757 AND LYS-778,
RP AND DEACETYLATION BY SIRT1.
RX PubMed=15744310; DOI=10.1038/nature03354;
RA Rodgers J.T., Lerin C., Haas W., Gygi S.P., Spiegelman B.M., Puigserver P.;
RT "Nutrient control of glucose homeostasis through a complex of PGC-1alpha
RT and SIRT1.";
RL Nature 434:113-118(2005).
RN [11]
RP INTERACTION WITH LPIN1.
RX PubMed=16950137; DOI=10.1016/j.cmet.2006.08.005;
RA Finck B.N., Gropler M.C., Chen Z., Leone T.C., Croce M.A., Harris T.E.,
RA Lawrence J.C. Jr., Kelly D.P.;
RT "Lipin 1 is an inducible amplifier of the hepatic PGC-1alpha/PPARalpha
RT regulatory pathway.";
RL Cell Metab. 4:199-210(2006).
RN [12]
RP INTERACTION WITH PRDM16.
RX PubMed=17618855; DOI=10.1016/j.cmet.2007.06.001;
RA Seale P., Kajimura S., Yang W., Chin S., Rohas L.M., Uldry M.,
RA Tavernier G., Langin D., Spiegelman B.M.;
RT "Transcriptional control of brown fat determination by PRDM16.";
RL Cell Metab. 6:38-54(2007).
RN [13]
RP PHOSPHORYLATION AT THR-177 AND SER-538, AND MUTAGENESIS OF THR-177 AND
RP SER-538.
RX PubMed=17609368; DOI=10.1073/pnas.0705070104;
RA Jager S., Handschin C., St-Pierre J., Spiegelman B.M.;
RT "AMP-activated protein kinase (AMPK) action in skeletal muscle via direct
RT phosphorylation of PGC-1alpha.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12017-12022(2007).
RN [14]
RP FUNCTION IN CIRCADIAN RHYTHMS, INTERACTION WITH RORA AND RORC, TISSUE
RP SPECIFICITY, INDUCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 142-LEU--LEU-146.
RX PubMed=17476214; DOI=10.1038/nature05767;
RA Liu C., Li S., Liu T., Borjigin J., Lin J.D.;
RT "Transcriptional coactivator PGC-1alpha integrates the mammalian clock and
RT energy metabolism.";
RL Nature 447:477-481(2007).
RN [15]
RP INTERACTION WITH PRDM16.
RX PubMed=18483224; DOI=10.1101/gad.1666108;
RA Kajimura S., Seale P., Tomaru T., Erdjument-Bromage H., Cooper M.P.,
RA Ruas J.L., Chin S., Tempst P., Lazar M.A., Spiegelman B.M.;
RT "Regulation of the brown and white fat gene programs through a PRDM16/CtBP
RT transcriptional complex.";
RL Genes Dev. 22:1397-1409(2008).
RN [16]
RP PHOSPHORYLATION BY CLK2.
RX PubMed=20074525; DOI=10.1016/j.cmet.2009.11.006;
RA Rodgers J.T., Haas W., Gygi S.P., Puigserver P.;
RT "Cdc2-like kinase 2 is an insulin-regulated suppressor of hepatic
RT gluconeogenesis.";
RL Cell Metab. 11:23-34(2010).
RN [17]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH PML.
RX PubMed=22886304; DOI=10.1172/jci62129;
RA Carracedo A., Weiss D., Leliaert A.K., Bhasin M., de Boer V.C., Laurent G.,
RA Adams A.C., Sundvall M., Song S.J., Ito K., Finley L.S., Egia A.,
RA Libermann T., Gerhart-Hines Z., Puigserver P., Haigis M.C.,
RA Maratos-Flier E., Richardson A.L., Schafer Z.T., Pandolfi P.P.;
RT "A metabolic prosurvival role for PML in breast cancer.";
RL J. Clin. Invest. 122:3088-3100(2012).
RN [18]
RP INDUCTION.
RX PubMed=22237023; DOI=10.1038/nature10777;
RA Bostrom P., Wu J., Jedrychowski M.P., Korde A., Ye L., Lo J.C.,
RA Rasbach K.A., Bostrom E.A., Choi J.H., Long J.Z., Kajimura S.,
RA Zingaretti M.C., Vind B.F., Tu H., Cinti S., Hojlund K., Gygi S.P.,
RA Spiegelman B.M.;
RT "A PGC1-alpha-dependent myokine that drives brown-fat-like development of
RT white fat and thermogenesis.";
RL Nature 481:463-468(2012).
CC -!- FUNCTION: Transcriptional coactivator for steroid receptors and nuclear
CC receptors (PubMed:15744310, PubMed:12754525, PubMed:23217713,
CC PubMed:9529258). Greatly increases the transcriptional activity of
CC PPARG and thyroid hormone receptor on the uncoupling protein promoter
CC (PubMed:15744310, PubMed:12754525, PubMed:23217713, PubMed:9529258).
CC Can regulate key mitochondrial genes that contribute to the program of
CC adaptive thermogenesis (PubMed:15744310, PubMed:12754525,
CC PubMed:23217713, PubMed:9529258). Plays an essential role in metabolic
CC reprogramming in response to dietary availability through coordination
CC of the expression of a wide array of genes involved in glucose and
CC fatty acid metabolism (PubMed:15744310, PubMed:12754525,
CC PubMed:23217713, PubMed:9529258). Acts as a key regulator of
CC gluconeogenesis: stimulates hepatic gluconeogenesis by increasing the
CC expression of gluconeogenic enzymes, and acting together with FOXO1 to
CC promote the fasting gluconeogenic program (PubMed:12754525). Induces
CC the expression of PERM1 in the skeletal muscle in an ESRRA-dependent
CC manner (By similarity). Also involved in the integration of the
CC circadian rhythms and energy metabolism (PubMed:17476214). Required for
CC oscillatory expression of clock genes, such as ARNTL/BMAL1 and NR1D1,
CC through the coactivation of RORA and RORC, and metabolic genes, such as
CC PDK4 and PEPCK (PubMed:17476214). {ECO:0000250|UniProtKB:Q9UBK2,
CC ECO:0000269|PubMed:12754525, ECO:0000269|PubMed:15744310,
CC ECO:0000269|PubMed:17476214, ECO:0000269|PubMed:23217713,
CC ECO:0000269|PubMed:9529258}.
CC -!- SUBUNIT: Homooligomer (By similarity). Interacts with MYBBP1A; inhibits
CC MYBBP1A transcriptional activation (PubMed:14744933). Interacts with
CC PRDM16, LPIN1 and PML (PubMed:16950137, PubMed:17618855,
CC PubMed:18483224, PubMed:22886304). Interacts (via LXXLL motif) with
CC RORA and RORC (via AF-2 motif); activates RORA and RORC transcriptional
CC activation (PubMed:17476214). Interacts with LRPPRC (By similarity).
CC Interacts with FOXO1 (PubMed:12754525). {ECO:0000250|UniProtKB:Q9UBK2,
CC ECO:0000269|PubMed:12754525, ECO:0000269|PubMed:14744933,
CC ECO:0000269|PubMed:16950137, ECO:0000269|PubMed:17476214,
CC ECO:0000269|PubMed:17618855, ECO:0000269|PubMed:18483224,
CC ECO:0000269|PubMed:22886304}.
CC -!- INTERACTION:
CC O70343; Q64287: Irf4; NbExp=6; IntAct=EBI-1371053, EBI-6398485;
CC O70343; Q6PB66: Lrpprc; NbExp=2; IntAct=EBI-1371053, EBI-1371262;
CC O70343; Q923E4: Sirt1; NbExp=6; IntAct=EBI-1371053, EBI-1802585;
CC O70343; Q00899: Yy1; NbExp=5; IntAct=EBI-1371053, EBI-6921536;
CC O70343-1; Q60641-1: Nr1h4; NbExp=3; IntAct=EBI-11359934, EBI-11659377;
CC O70343-1; Q60641-2: Nr1h4; NbExp=2; IntAct=EBI-11359934, EBI-11659386;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22886304,
CC ECO:0000269|PubMed:23217713}. Nucleus, PML body
CC {ECO:0000269|PubMed:22886304}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=PGC-1a1;
CC IsoId=O70343-1; Sequence=Displayed;
CC Name=2; Synonyms=PGC-1a2;
CC IsoId=O70343-2; Sequence=VSP_053275, VSP_053277, VSP_053278,
CC VSP_053280;
CC Name=3; Synonyms=PGC-1a3;
CC IsoId=O70343-3; Sequence=VSP_053276, VSP_053277, VSP_053278,
CC VSP_053280;
CC Name=4; Synonyms=PGC-1a4;
CC IsoId=O70343-4; Sequence=VSP_053275, VSP_053279, VSP_053281;
CC -!- TISSUE SPECIFICITY: White quadriceps and red tibialis anterior (TA)
CC muscles, liver, kidney and brown adipose tissue (at protein level).
CC Skeletal muscle, brown adipose tissue, heart, kidney and brain.
CC {ECO:0000269|PubMed:17476214, ECO:0000269|PubMed:23217713,
CC ECO:0000269|PubMed:9529258}.
CC -!- INDUCTION: Dramatically induced in brown adipose tissue and skeletal
CC muscle by exposure of animals to cold. Up-regulated in brown adipose
CC tissue of obese leptin-deficient (ob/ob) and leptin-unresponsive
CC (db/db) mice. Leptin is required for normal basal and cold-stimulated
CC expression in brown adipose tissue and hyperleptinemia rapidly up-
CC regulates its expression. Induced in muscle by exercise. Oscillates
CC diurnally in liver and skeletal muscle. {ECO:0000269|PubMed:11108270,
CC ECO:0000269|PubMed:17476214, ECO:0000269|PubMed:22237023,
CC ECO:0000269|PubMed:23217713, ECO:0000269|PubMed:9529258}.
CC -!- PTM: Phosphorylation by AMPK in skeletal muscle increases activation of
CC its own promoter (PubMed:17609368). Phosphorylated by CLK2
CC (PubMed:20074525). {ECO:0000269|PubMed:17609368,
CC ECO:0000269|PubMed:20074525}.
CC -!- PTM: Heavily acetylated by KAT2A/GCN5 under conditions of high
CC nutrients, leading to inactivation of PPARGC1A (PubMed:15744310).
CC Deacetylated by SIRT1 in low nutrients/high NAD conditions, leading to
CC its activation (PubMed:15716268, PubMed:15744310).
CC {ECO:0000269|PubMed:15716268, ECO:0000269|PubMed:15744310}.
CC -!- PTM: Ubiquitinated. Ubiquitination by RNF34 induces proteasomal
CC degradation. {ECO:0000250|UniProtKB:Q9UBK2}.
CC -!- DISRUPTION PHENOTYPE: Mice show abnormal diurnal rhythms of activity,
CC body temperature and metabolic rate. {ECO:0000269|PubMed:17476214}.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative promoter usage and
CC alternative splicing. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative promoter usage and
CC alternative splicing. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative promoter usage and
CC alternative splicing. {ECO:0000305}.
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DR EMBL; AF049330; AAC13554.1; -; mRNA.
DR EMBL; JX866946; AFZ74947.1; -; mRNA.
DR EMBL; JX866947; AFZ74948.1; -; mRNA.
DR EMBL; JX866948; AFZ74949.1; -; mRNA.
DR EMBL; AK138668; BAE23740.1; -; mRNA.
DR EMBL; AK143753; BAE25525.1; -; mRNA.
DR EMBL; CH466524; EDL37647.1; -; Genomic_DNA.
DR EMBL; BC066868; AAH66868.1; -; mRNA.
DR CCDS; CCDS19282.1; -. [O70343-1]
DR RefSeq; NP_032930.1; NM_008904.2. [O70343-1]
DR PDB; 3F7D; X-ray; 2.20 A; B=137-150.
DR PDBsum; 3F7D; -.
DR AlphaFoldDB; O70343; -.
DR SMR; O70343; -.
DR BioGRID; 202321; 16.
DR CORUM; O70343; -.
DR DIP; DIP-38447N; -.
DR IntAct; O70343; 15.
DR STRING; 10090.ENSMUSP00000117040; -.
DR iPTMnet; O70343; -.
DR PhosphoSitePlus; O70343; -.
DR PaxDb; O70343; -.
DR PRIDE; O70343; -.
DR ProteomicsDB; 291873; -. [O70343-1]
DR ProteomicsDB; 291876; -. [O70343-4]
DR Antibodypedia; 10142; 357 antibodies from 40 providers.
DR DNASU; 19017; -.
DR Ensembl; ENSMUST00000132734; ENSMUSP00000117040; ENSMUSG00000029167. [O70343-1]
DR Ensembl; ENSMUST00000151104; ENSMUSP00000116566; ENSMUSG00000029167. [O70343-4]
DR GeneID; 19017; -.
DR KEGG; mmu:19017; -.
DR UCSC; uc008xkc.2; mouse. [O70343-1]
DR CTD; 10891; -.
DR MGI; MGI:1342774; Ppargc1a.
DR VEuPathDB; HostDB:ENSMUSG00000029167; -.
DR eggNOG; ENOG502QSXU; Eukaryota.
DR GeneTree; ENSGT00950000183137; -.
DR HOGENOM; CLU_020104_0_0_1; -.
DR InParanoid; O70343; -.
DR OMA; KCPSKKK; -.
DR OrthoDB; 94418at2759; -.
DR PhylomeDB; O70343; -.
DR TreeFam; TF343068; -.
DR BioGRID-ORCS; 19017; 2 hits in 78 CRISPR screens.
DR ChiTaRS; Ppargc1a; mouse.
DR EvolutionaryTrace; O70343; -.
DR PRO; PR:O70343; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; O70343; protein.
DR Bgee; ENSMUSG00000029167; Expressed in atrioventricular valve and 257 other tissues.
DR ExpressionAtlas; O70343; baseline and differential.
DR Genevisible; O70343; MM.
DR GO; GO:0097440; C:apical dendrite; ISO:MGI.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:MGI.
DR GO; GO:0000791; C:euchromatin; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0043014; F:alpha-tubulin binding; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; ISO:MGI.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISO:MGI.
DR GO; GO:0016922; F:nuclear receptor binding; ISO:MGI.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISO:MGI.
DR GO; GO:0042975; F:peroxisome proliferator activated receptor binding; ISO:MGI.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0060612; P:adipose tissue development; IMP:CACAO.
DR GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; ISO:MGI.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:MGI.
DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; ISO:MGI.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISO:MGI.
DR GO; GO:0032922; P:circadian regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0097009; P:energy homeostasis; IMP:UniProtKB.
DR GO; GO:0006094; P:gluconeogenesis; IDA:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; ISO:MGI.
DR GO; GO:0045820; P:negative regulation of glycolytic process; ISO:MGI.
DR GO; GO:0090258; P:negative regulation of mitochondrial fission; ISO:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
DR GO; GO:1901215; P:negative regulation of neuron death; ISS:UniProtKB.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:2000272; P:negative regulation of signaling receptor activity; ISO:MGI.
DR GO; GO:0014912; P:negative regulation of smooth muscle cell migration; ISO:MGI.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0051402; P:neuron apoptotic process; IMP:MGI.
DR GO; GO:2001171; P:positive regulation of ATP biosynthetic process; IMP:UniProtKB.
DR GO; GO:1901857; P:positive regulation of cellular respiration; IMP:UniProtKB.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
DR GO; GO:0046321; P:positive regulation of fatty acid oxidation; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:1901860; P:positive regulation of mitochondrial DNA metabolic process; IMP:UniProtKB.
DR GO; GO:0010822; P:positive regulation of mitochondrion organization; IMP:UniProtKB.
DR GO; GO:1901863; P:positive regulation of muscle tissue development; IMP:UniProtKB.
DR GO; GO:1904635; P:positive regulation of podocyte apoptotic process; ISO:MGI.
DR GO; GO:2000184; P:positive regulation of progesterone biosynthetic process; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0042752; P:regulation of circadian rhythm; IDA:UniProtKB.
DR GO; GO:2000310; P:regulation of NMDA receptor activity; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0022904; P:respiratory electron transport chain; IDA:MGI.
DR GO; GO:0014823; P:response to activity; ISO:MGI.
DR GO; GO:0002021; P:response to dietary excess; IDA:MGI.
DR GO; GO:0014850; P:response to muscle activity; IDA:MGI.
DR CDD; cd12623; RRM_PPARGC1A; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR IDEAL; IID50038; -.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR034605; PGC-1.
DR InterPro; IPR034625; PGC-1alpha.
DR InterPro; IPR034833; PPARGC1A_RRM.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR15528; PTHR15528; 1.
DR PANTHER; PTHR15528:SF10; PTHR15528:SF10; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative promoter usage;
KW Alternative splicing; Biological rhythms; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..797
FT /note="Peroxisome proliferator-activated receptor gamma
FT coactivator 1-alpha"
FT /id="PRO_0000081733"
FT DOMAIN 676..752
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 101..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..338
FT /note="Interaction with PPARG"
FT /evidence="ECO:0000250|UniProtKB:Q9UBK2"
FT REGION 349..797
FT /note="Mediates interaction with RNF34"
FT /evidence="ECO:0000250|UniProtKB:Q9UBK2"
FT REGION 543..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 142..146
FT /note="LXXLL motif"
FT /evidence="ECO:0000269|PubMed:17476214"
FT COMPBIAS 221..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:15744310"
FT MOD_RES 144
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:15744310"
FT MOD_RES 177
FT /note="Phosphothreonine; by AMPK"
FT /evidence="ECO:0000269|PubMed:17609368"
FT MOD_RES 183
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:15744310"
FT MOD_RES 253
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:15744310"
FT MOD_RES 270
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:15744310"
FT MOD_RES 277
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:15744310"
FT MOD_RES 320
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:15744310"
FT MOD_RES 346
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:15744310"
FT MOD_RES 412
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:15744310"
FT MOD_RES 441
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:15744310"
FT MOD_RES 450
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:15744310"
FT MOD_RES 538
FT /note="Phosphoserine; by AMPK"
FT /evidence="ECO:0000269|PubMed:17609368"
FT MOD_RES 757
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:15744310"
FT MOD_RES 778
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:15744310"
FT VAR_SEQ 2..16
FT /note="AWDMCSQDSVWSDIE -> LGLSSMDSILK (in isoform 2 and
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:23217713"
FT /id="VSP_053275"
FT VAR_SEQ 2..16
FT /note="AWDMCSQDSVWSDIE -> LL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:23217713"
FT /id="VSP_053276"
FT VAR_SEQ 108..274
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:23217713"
FT /id="VSP_053277"
FT VAR_SEQ 268..500
FT /note="DPKGSPFENKTIERTLSVELSGTAGLTPPTTPPHKANQDNPFKASPKLKPSC
FT KTVVPPPTKRARYSECSGTQGSHSTKKGPEQSELYAQLSKSSGLSRGHEERKTKRPSLR
FT LFGDHDYCQSLNSKTDILINISQELQDSRQLDFKDASCDWQGHICSSTDSGQCYLRETL
FT EASKQVSPCSTRKQLQDQEIRAELNKHFGHPCQAVFDDKSDKTSELRDGDFSNEQFSKL
FT PVFI -> LFL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:23217713"
FT /id="VSP_053279"
FT VAR_SEQ 501..797
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:23217713"
FT /id="VSP_053281"
FT VAR_SEQ 545..680
FT /note="PCRDSVSPPKSLFSQRPQRMRSRSRSFSRHRSCSRSPYSRSRSRSPGSRSSS
FT RSCYYYESSHYRHRTHRNSPLYVRSRSRSPYSRRPRYDSYEAYEHERLKRDEYRKEHEK
FT RESERAKQRERQKQKAIEERRVIYV -> LNVIIT (in isoform 2 and
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:23217713"
FT /id="VSP_053278"
FT VAR_SEQ 681..797
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:23217713"
FT /id="VSP_053280"
FT MUTAGEN 142..146
FT /note="LKKLL->AKKAA: Strongly reduces coactivation of RORA
FT activity."
FT /evidence="ECO:0000269|PubMed:17476214"
FT MUTAGEN 177
FT /note="T->A: Abolishes AMPK-mediated phosphorylation; when
FT associated with A-538."
FT /evidence="ECO:0000269|PubMed:17609368"
FT MUTAGEN 538
FT /note="S->A: Abolishes AMPK-mediated phosphorylation; when
FT associated with A-177."
FT /evidence="ECO:0000269|PubMed:17609368"
FT CONFLICT 587
FT /note="S -> L (in Ref. 5; AAH66868)"
FT /evidence="ECO:0000305"
FT CONFLICT 629
FT /note="R -> C (in Ref. 5; AAH66868)"
FT /evidence="ECO:0000305"
FT HELIX 141..147
FT /evidence="ECO:0007829|PDB:3F7D"
SQ SEQUENCE 797 AA; 90588 MW; AE73EE2B3A622B05 CRC64;
MAWDMCSQDS VWSDIECAAL VGEDQPLCPD LPELDLSELD VNDLDTDSFL GGLKWCSDQS
EIISNQYNNE PANIFEKIDE ENEANLLAVL TETLDSLPVD EDGLPSFDAL TDGAVTTDNE
ASPSSMPDGT PPPQEAEEPS LLKKLLLAPA NTQLSYNECS GLSTQNHAAN HTHRIRTNPA
IVKTENSWSN KAKSICQQQK PQRRPCSELL KYLTTNDDPP HTKPTENRNS SRDKCASKKK
SHTQPQSQHA QAKPTTLSLP LTPESPNDPK GSPFENKTIE RTLSVELSGT AGLTPPTTPP
HKANQDNPFK ASPKLKPSCK TVVPPPTKRA RYSECSGTQG SHSTKKGPEQ SELYAQLSKS
SGLSRGHEER KTKRPSLRLF GDHDYCQSLN SKTDILINIS QELQDSRQLD FKDASCDWQG
HICSSTDSGQ CYLRETLEAS KQVSPCSTRK QLQDQEIRAE LNKHFGHPCQ AVFDDKSDKT
SELRDGDFSN EQFSKLPVFI NSGLAMDGLF DDSEDESDKL SYPWDGTQPY SLFDVSPSCS
SFNSPCRDSV SPPKSLFSQR PQRMRSRSRS FSRHRSCSRS PYSRSRSRSP GSRSSSRSCY
YYESSHYRHR THRNSPLYVR SRSRSPYSRR PRYDSYEAYE HERLKRDEYR KEHEKRESER
AKQRERQKQK AIEERRVIYV GKIRPDTTRT ELRDRFEVFG EIEECTVNLR DDGDSYGFIT
YRYTCDAFAA LENGYTLRRS NETDFELYFC GRKQFFKSNY ADLDTNSDDF DPASTKSKYD
SLDFDSLLKE AQRSLRR
