Q8VHJ7 (PRGC2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peroxisome proliferator-activated receptor gamma coactivator 1-beta
Short name=PGC-1-beta
Short name=PPAR-gamma coactivator 1-beta
Short name=PPARGC-1-beta

Alternative name(s):
ERR ligand 1

Gene names

Name:	Ppargc1b
Synonyms:	Errl1, Pgc1, Pgc1b, Ppargc1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [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 › Mus › Mus

Protein attributes

Sequence length	1014 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays a role of stimulator of transcription factors and nuclear receptors activities. Activates transcritional activity of estrogen receptor alpha, nuclear respiratory factor 1 (NRF1) and glucocorticoid receptor in the presence of glucocorticoids. May play a role in constitutive non-adrenergic-mediated mitochondrial biogenesis as suggested by increased basal oxygen consumption and mitochondrial number when overexpressed. May be part of the pathways regulating the elevation of gluconeogenesis, beta-oxidation of fatty acids and ketogenesis during fasting. Stimulates SREBP-mediated lipogenic gene expression in the liver. Induces energy expenditure and antagonizes obesity when overexpressed. Induces also the expression of mitochondrial genes involved in oxidative metabolism. Ref.1 Ref.2 Ref.5 Ref.6
Subunit structure	Interacts with estrogen receptor alpha/ESR1 By similarity. Interacts with hepatocyte nuclear factor 4-alpha/HNF4A, Sterol regulatory binding transcription factor 1/SREBF1, PPAR-alpha/PPARA, thyroid hormone receptor beta/THRB and host cell factor/HCFC1. Interacts with estrogen-related receptor gamma/ESRRG and alpha/ESRRA. Interacts with PRDM16. Ref.1 Ref.2 Ref.4 Ref.6 Ref.7 Ref.8
Subcellular location	Nucleus By similarity.
Tissue specificity	Ubiquitous with higher expression in heart, brown adipose tissue, brain and skeletal muscle. Ref.1 Ref.5
Induction	Induced by fasting in the liver, but not by cold exposure in brown adipose tissue. Induced also by saturated fatty acids in primary hepatocytes. Ref.1 Ref.6
Domain	Contains 3 Leu-Xaa-Xaa-Leu-Leu (LXXLL) motif, which are usually required for the association with nuclear receptors By similarity.
Miscellaneous	Transgenic mice overexpressing PPARGC1B exhibits increased expression of medium-chain acyl CoA dehydrogenase. They are hyperphagic but lean, with increased energy expenditure and resistance to obesity.
Sequence similarities	Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	RNA-binding
Molecular function	Activator
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin filament organization Inferred from mutant phenotype PubMed 19252502. Source: DFLAT bone trabecula formation Inferred from mutant phenotype PubMed 19252502. Source: DFLAT cellular response to reactive oxygen species Inferred from direct assay PubMed 19252502. Source: DFLAT intracellular estrogen receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from mutant phenotype PubMed 19252502. Source: DFLAT ossification Inferred from mutant phenotype PubMed 19252502. Source: DFLAT positive regulation of alkaline phosphatase activity Inferred from mutant phenotype PubMed 19252502. Source: DFLAT positive regulation of bone resorption Inferred from mutant phenotype PubMed 19252502. Source: DFLAT positive regulation of osteoclast differentiation Inferred from mutant phenotype PubMed 19252502. Source: DFLAT positive regulation of phosphorylation Inferred from mutant phenotype PubMed 19252502. Source: DFLAT positive regulation of transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: UniProtKB response to cAMP Inferred from electronic annotation. Source: Compara response to glucocorticoid stimulus Inferred from electronic annotation. Source: Compara transcription from mitochondrial promoter Inferred from mutant phenotype PubMed 19252502. Source: DFLAT
Cellular_component	mediator complex Inferred from electronic annotation. Source: Compara nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	AF-2 domain binding Inferred from sequence or structural similarity. Source: UniProtKB RNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA polymerase II transcription cofactor activity Inferred from electronic annotation. Source: Compara ligand-dependent nuclear receptor transcription coactivator activity Inferred from sequence or structural similarity. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro receptor activator activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8VHJ7-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q8VHJ7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MAGNDCGALLDEELSSFFLNYLSDTQ → MKSSRPSSSTISLTRRSAEGLEEVDHEALDRDGCGRRRLADM

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1014	1014	Peroxisome proliferator-activated receptor gamma coactivator 1-beta		PRO_0000240159
Regions
	Domain	893 – 967	75	RRM
	Region	1 – 91	91	Abolishes DNA transcriptional activity when missing By similarity
	Motif	140 – 144	5	LXXLL motif 1
	Motif	156 – 160	5	LXXLL motif 2
	Motif	343 – 347	5	LXXLL motif 3
	Motif	683 – 686	4	HCFC1-binding-motif (HBM)
	Compositional bias	246 – 250	5	Poly-Glu
	Compositional bias	429 – 451	23	Glu-rich
	Compositional bias	786 – 856	71	Ser-rich
Amino acid modifications
	Modified residue	519	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	1 – 26	26	MAGND…LSDTQ → MKSSRPSSSTISLTRRSAEG LEEVDHEALDRDGCGRRRLA DM in isoform 2.		VSP_019302
Experimental info
	Sequence conflict	55	1	A → P in BAC25964. Ref.3
	Sequence conflict	579	1	K → R in BAC25964. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 004BCB7797EAFD1F	FASTA	1,014	112,075
	10 20 30 40 50 60 MAGNDCGALL DEELSSFFLN YLSDTQGGDS GEEQLCADLP ELDLSQLDAS DFDSATCFGE 70 80 90 100 110 120 LQWCPETSET EPSQYSPDDS ELFQIDSENE ALLAALTKTL DDIPEDDVGL AAFPELDEGD 130 140 150 160 170 180 TPSCTPASPA PLSAPPSPTL ERLLSPASDV DELSLLQKLL LATSSPTASS DALKDGATWS 190 200 210 220 230 240 QTSLSSRSQR PCVKVDGTQD KKTPTLRAQS RPCTELHKHL TSVLPCPRVK ACSPTPHPSP 250 260 270 280 290 300 RLLSKEEEEE VGEDCPSPWP TPASPQDSLA QDTASPDSAQ PPEEDVRAMV QLIRYMHTYC 310 320 330 340 350 360 LPQRKLPQRA PEPIPQACSS LSRQVQPRSR HPPKAFWTEF SILRELLAQD ILCDVSKPYR 370 380 390 400 410 420 LAIPVYASLT PQSRPRPPKD SQASPAHSAM AEEVRITASP KSTGPRPSLR PLRLEVKRDV 430 440 450 460 470 480 NKPTRQKREE DEEEEEEEEE EEEEKEEEEE EWGRKRPGRG LPWTKLGRKM DSSVCPVRRS 490 500 510 520 530 540 RRLNPELGPW LTFTDEPLGA LPSMCLDTET HNLEEDLGSL TDSSQGRQLP QGSQIPALES 550 560 570 580 590 600 PCESGCGDTD EDPSCPQPTS RDSSRCLMLA LSQSDSLGKK SFEESLTVEL CGTAGLTPPT 610 620 630 640 650 660 TPPYKPMEED PFKPDTKLSP GQDTAPSLPS PEALPLTATP GASHKLPKRH PERSELLSHL 670 680 690 700 710 720 QHATTQPVSQ AGQKRPFSCS FGDHDYCQVL RPEAALQRKV LRSWEPIGVH LEDLAQQGAP 730 740 750 760 770 780 LPTETKAPRR EANQNCDPTH KDSMQLRDHE IRASLTKHFG LLETALEGED LASCKSPEYD 790 800 810 820 830 840 TVFEDSSSSS GESSFLLEEE EEEEEGGEED DEGEDSGVSP PCSDHCPYQS PPSKASRQLC 850 860 870 880 890 900 SRSRSSSGSS SCSSWSPATR KNFRRESRGP CSDGTPSVRH ARKRREKAIG EGRVVYIRNL 910 920 930 940 950 960 SSDMSSRELK KRFEVFGEIV ECQVLTRSKR GQKHGFITFR CSEHAALSVR NGATLRKRNE 970 980 990 1000 1010 PSFHLSYGGL RHFRWPRYTD YDPTSEESLP SSGKSKYEAM DFDSLLKEAQ QSLH
	Isoform 2 [UniParc]. Checksum: 4F2B27E32E91C84C	FASTA	1,030	113,898
	10 20 30 40 50 60 MKSSRPSSST ISLTRRSAEG LEEVDHEALD RDGCGRRRLA DMGGDSGEEQ LCADLPELDL 70 80 90 100 110 120 SQLDASDFDS ATCFGELQWC PETSETEPSQ YSPDDSELFQ IDSENEALLA ALTKTLDDIP 130 140 150 160 170 180 EDDVGLAAFP ELDEGDTPSC TPASPAPLSA PPSPTLERLL SPASDVDELS LLQKLLLATS 190 200 210 220 230 240 SPTASSDALK DGATWSQTSL SSRSQRPCVK VDGTQDKKTP TLRAQSRPCT ELHKHLTSVL 250 260 270 280 290 300 PCPRVKACSP TPHPSPRLLS KEEEEEVGED CPSPWPTPAS PQDSLAQDTA SPDSAQPPEE 310 320 330 340 350 360 DVRAMVQLIR YMHTYCLPQR KLPQRAPEPI PQACSSLSRQ VQPRSRHPPK AFWTEFSILR 370 380 390 400 410 420 ELLAQDILCD VSKPYRLAIP VYASLTPQSR PRPPKDSQAS PAHSAMAEEV RITASPKSTG 430 440 450 460 470 480 PRPSLRPLRL EVKRDVNKPT RQKREEDEEE EEEEEEEEEE KEEEEEEWGR KRPGRGLPWT 490 500 510 520 530 540 KLGRKMDSSV CPVRRSRRLN PELGPWLTFT DEPLGALPSM CLDTETHNLE EDLGSLTDSS 550 560 570 580 590 600 QGRQLPQGSQ IPALESPCES GCGDTDEDPS CPQPTSRDSS RCLMLALSQS DSLGKKSFEE 610 620 630 640 650 660 SLTVELCGTA GLTPPTTPPY KPMEEDPFKP DTKLSPGQDT APSLPSPEAL PLTATPGASH 670 680 690 700 710 720 KLPKRHPERS ELLSHLQHAT TQPVSQAGQK RPFSCSFGDH DYCQVLRPEA ALQRKVLRSW 730 740 750 760 770 780 EPIGVHLEDL AQQGAPLPTE TKAPRREANQ NCDPTHKDSM QLRDHEIRAS LTKHFGLLET 790 800 810 820 830 840 ALEGEDLASC KSPEYDTVFE DSSSSSGESS FLLEEEEEEE EGGEEDDEGE DSGVSPPCSD 850 860 870 880 890 900 HCPYQSPPSK ASRQLCSRSR SSSGSSSCSS WSPATRKNFR RESRGPCSDG TPSVRHARKR 910 920 930 940 950 960 REKAIGEGRV VYIRNLSSDM SSRELKKRFE VFGEIVECQV LTRSKRGQKH GFITFRCSEH 970 980 990 1000 1010 1020 AALSVRNGAT LRKRNEPSFH LSYGGLRHFR WPRYTDYDPT SEESLPSSGK SKYEAMDFDS 1030 LLKEAQQSLH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Peroxisome proliferator-activated receptor gamma coactivator 1beta (PGC-1beta), a novel PGC-1-related transcription coactivator associated with host cell factor." Lin J., Puigserver P., Donovan J., Tarr P., Spiegelman B.M. J. Biol. Chem. 277:1645-1648(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, MOTIFS, FUNCTION, INDUCTION, SUBUNIT. Strain: C57BL/6.
[2]	"PPARgamma coactivator 1beta/ERR ligand 1 is an ERR protein ligand, whose expression induces a high-energy expenditure and antagonizes obesity." Kamei Y., Ohizumi H., Fujitani Y., Nemoto T., Tanaka T., Takahashi N., Kawada T., Miyoshi M., Ezaki O., Kakizuka A. Proc. Natl. Acad. Sci. U.S.A. 100:12378-12383(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH ESRRA AND ESRRG.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: C57BL/6J. Tissue: Skin.
[4]	"PGC-1 and PERC, coactivators of the estrogen receptor-related receptor gamma." Hentschke M., Suesens U., Borgmeyer U. Biochem. Biophys. Res. Commun. 299:872-879(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ESRRG.
[5]	"Characterization of the human, mouse and rat PGC1 beta (peroxisome-proliferator-activated receptor-gamma co-activator 1 beta) gene in vitro and in vivo." Meirhaeghe A., Crowley V., Lenaghan C., Lelliott C., Green K., Stewart A., Hart K., Schinner S., Sethi J.K., Yeo G., Brand M.D., Cortright R.N., O'Rahilly S., Montague C., Vidal-Puig A.J. Biochem. J. 373:155-165(2003) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, FUNCTION.
[6]	"Hyperlipidemic effects of dietary saturated fats mediated through PGC-1beta coactivation of SREBP." Lin J., Yang R., Tarr P.T., Wu P.-H., Handschin C., Li S., Yang W., Pei L., Uldry M., Tontonoz P., Newgard C.B., Spiegelman B.M. Cell 120:261-273(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SREBF1, INDUCTION.
[7]	"Transcriptional control of brown fat determination by PRDM16." Seale P., Kajimura S., Yang W., Chin S., Rohas L.M., Uldry M., Tavernier G., Langin D., Spiegelman B.M. Cell Metab. 6:38-54(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PRDM16.
[8]	"Regulation of the brown and white fat gene programs through a PRDM16/CtBP transcriptional complex." Kajimura S., Seale P., Tomaru T., Erdjument-Bromage H., Cooper M.P., Ruas J.L., Chin S., Tempst P., Lazar M.A., Spiegelman B.M. Genes Dev. 22:1397-1409(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PRDM16.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF453324 mRNA. Translation: AAL47054.1. AK028464 mRNA. Translation: BAC25964.1.
IPI	IPI00128366. IPI00224182.
RefSeq	NP_573512.1. NM_133249.2.
UniGene	Mm.415302.
3D structure databases
ProteinModelPortal	Q8VHJ7.
SMR	Q8VHJ7. Positions 893-956.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8VHJ7. 1 interaction.
PTM databases
PhosphoSite	Q8VHJ7.
Proteomic databases
PRIDE	Q8VHJ7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000063307; ENSMUSP00000069431; ENSMUSG00000033871. ENSMUST00000075299; ENSMUSP00000074771; ENSMUSG00000033871.
GeneID	170826.
KEGG	mmu:170826.
UCSC	uc008fbx.1. mouse. uc012bdq.1. mouse.
Organism-specific databases
CTD	133522.
MGI	MGI:2444934. Ppargc1b.
Phylogenomic databases
eggNOG	NOG87590.
GeneTree	ENSGT00530000063196.
HOGENOM	HOG000236356.
HOVERGEN	HBG080730.
OMA	EDPFKPD.
OrthoDB	EOG4TTGH5.
Gene expression databases
Bgee	Q8VHJ7.
Genevestigator	Q8VHJ7.
GermOnline	ENSMUSG00000033871. Mus musculus.
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
ChiTaRS	PPARGC1B. mouse.
NextBio	370487.
SOURCE	Search...

Entry information

Entry name

PRGC2_MOUSE

Accession

Primary (citable) accession number: Q8VHJ7
Secondary accession number(s): Q8C1C0

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 13, 2006
Last sequence update:	March 1, 2002
Last modified:	May 1, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program