PRGC2_RAT
ID PRGC2_RAT Reviewed; 1010 AA.
AC Q811R2;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Peroxisome proliferator-activated receptor gamma coactivator 1-beta;
DE Short=PGC-1-beta;
DE Short=PPAR-gamma coactivator 1-beta;
DE Short=PPARGC-1-beta;
GN Name=Ppargc1b; Synonyms=Perc, Pgc1, Pgc1b, Ppargc1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=12678921; DOI=10.1042/bj20030200;
RA Meirhaeghe A., Crowley V., Lenaghan C., Lelliott C., Green K., Stewart A.,
RA Hart K., Schinner S., Sethi J.K., Yeo G., Brand M.D., Cortright R.N.,
RA O'Rahilly S., Montague C., Vidal-Puig A.J.;
RT "Characterization of the human, mouse and rat PGC1 beta (peroxisome-
RT proliferator-activated receptor-gamma co-activator 1 beta) gene in vitro
RT and in vivo.";
RL Biochem. J. 373:155-165(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING
RP (ISOFORM 1).
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP FUNCTION.
RX PubMed=12807885; DOI=10.1074/jbc.m303643200;
RA Lin J., Tarr P.T., Yang R., Rhee J., Puigserver P., Newgard C.B.,
RA Spiegelman B.M.;
RT "PGC-1beta in the regulation of hepatic glucose and energy metabolism.";
RL J. Biol. Chem. 278:30843-30848(2003).
CC -!- FUNCTION: Plays a role of stimulator of transcription factors and
CC nuclear receptors activities. Activates transcriptional activity of
CC estrogen receptor alpha, nuclear respiratory factor 1 (NRF1) and
CC glucocorticoid receptor in the presence of glucocorticoids. May play a
CC role in constitutive non-adrenergic-mediated mitochondrial biogenesis
CC as suggested by increased basal oxygen consumption and mitochondrial
CC number when overexpressed. May be part of the pathways regulating the
CC elevation of gluconeogenesis, beta-oxidation of fatty acids and
CC ketogenesis during fasting. Stimulates SREBP-mediated lipogenic gene
CC expression in the liver. Induces energy expenditure and antagonizes
CC obesity when overexpressed. Induces also the expression of
CC mitochondrial genes involved in oxidative metabolism. Induces the
CC expression of PERM1 in the skeletal muscle in an ESRRA-dependent
CC manner. {ECO:0000269|PubMed:12678921, ECO:0000269|PubMed:12807885}.
CC -!- SUBUNIT: Interacts with estrogen receptor alpha/ESR1. Interacts with
CC Sterol regulatory binding transcription factor 1/SREBF1, PPAR-
CC alpha/PPARA, thyroid hormone receptor beta/THRB and host cell
CC factor/HCFC1. Interacts with Estrogen-related receptor gamma/ESRRG and
CC alpha/ESRRA. Interacts with PRDM16 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=PGC1beta-1a;
CC IsoId=Q811R2-1; Sequence=Displayed;
CC Name=2; Synonyms=PGC1beta-2a;
CC IsoId=Q811R2-2; Sequence=VSP_019303;
CC -!- TISSUE SPECIFICITY: Ubiquitous with higher expression in heart, brown
CC adipose tissue. {ECO:0000269|PubMed:12678921}.
CC -!- INDUCTION: Induced by combination of forskolin and dexamethasone in
CC primary hepatocytes.
CC -!- DOMAIN: Contains 3 Leu-Xaa-Xaa-Leu-Leu (LXXLL) motif, which are usually
CC required for the association with nuclear receptors. {ECO:0000250}.
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DR EMBL; AY188951; AAO40026.1; -; mRNA.
DR EMBL; AABR03110123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03000001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_788264.1; NM_176075.2. [Q811R2-1]
DR AlphaFoldDB; Q811R2; -.
DR SMR; Q811R2; -.
DR STRING; 10116.ENSRNOP00000023661; -.
DR PhosphoSitePlus; Q811R2; -.
DR PaxDb; Q811R2; -.
DR PRIDE; Q811R2; -.
DR Ensembl; ENSRNOT00000023661; ENSRNOP00000023661; ENSRNOG00000017503. [Q811R2-1]
DR GeneID; 291567; -.
DR KEGG; rno:291567; -.
DR UCSC; RGD:727948; rat. [Q811R2-1]
DR CTD; 133522; -.
DR RGD; 727948; Ppargc1b.
DR eggNOG; ENOG502QTA7; Eukaryota.
DR GeneTree; ENSGT00950000183137; -.
DR HOGENOM; CLU_014202_0_0_1; -.
DR InParanoid; Q811R2; -.
DR OMA; PTKPCCH; -.
DR OrthoDB; 94418at2759; -.
DR PhylomeDB; Q811R2; -.
DR TreeFam; TF343068; -.
DR PRO; PR:Q811R2; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000017503; Expressed in testis and 18 other tissues.
DR Genevisible; Q811R2; RN.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016592; C:mediator complex; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0050682; F:AF-2 domain binding; ISS:UniProtKB.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISO:RGD.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003712; F:transcription coregulator activity; ISO:RGD.
DR GO; GO:0007015; P:actin filament organization; ISO:RGD.
DR GO; GO:0060346; P:bone trabecula formation; ISO:RGD.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:RGD.
DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006390; P:mitochondrial transcription; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0001503; P:ossification; ISO:RGD.
DR GO; GO:0010694; P:positive regulation of alkaline phosphatase activity; ISO:RGD.
DR GO; GO:0045780; P:positive regulation of bone resorption; ISO:RGD.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; ISO:RGD.
DR GO; GO:0042327; P:positive regulation of phosphorylation; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0051591; P:response to cAMP; IEP:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR CDD; cd12356; RRM_PPARGC1B; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR034605; PGC-1.
DR InterPro; IPR034621; PGC-1beta.
DR InterPro; IPR034177; PPARGC1B_RRM.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR15528; PTHR15528; 1.
DR PANTHER; PTHR15528:SF12; PTHR15528:SF12; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 2: Evidence at transcript level;
KW Activator; Alternative splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Transcription;
KW Transcription regulation.
FT CHAIN 1..1010
FT /note="Peroxisome proliferator-activated receptor gamma
FT coactivator 1-beta"
FT /id="PRO_0000240160"
FT DOMAIN 889..963
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..91
FT /note="Abolishes DNA transcriptional activity when missing"
FT /evidence="ECO:0000250"
FT REGION 115..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 140..144
FT /note="LXXLL motif 1"
FT MOTIF 156..160
FT /note="LXXLL motif 2"
FT MOTIF 342..346
FT /note="LXXLL motif 3"
FT MOTIF 681..684
FT /note="HCFC1-binding-motif (HBM)"
FT COMPBIAS 165..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..446
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..744
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..813
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..857
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VHJ7"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VHJ7"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YN6"
FT MOD_RES 628
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YN6"
FT VAR_SEQ 1..26
FT /note="MAGNDCGALLDEELSSFFLNYLSDTQ -> MQGEGK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12678921"
FT /id="VSP_019303"
SQ SEQUENCE 1010 AA; 111589 MW; E03266060CCA08CC CRC64;
MAGNDCGALL DEELSSFFLN YLSDTQGGES GEEQLCADLP ELDLSQLDAS DFDSATCFGE
LQWCPETSET EPSQYSPDDS EFFQIDSENE ALLAALTKTL DDIPEDDVGL AAFPGLDEGD
TPSCTPASPA PLSVPPSPAL ERLLSPVSEV DELSLLQKLL LATSSPTASS DALKDGATWS
QTSLSSRSQR PCVKVDGTQD KKTPMLRSQS RPCTELHKHL TSVLPCPRGK ACSPPPHPSP
QLLSKEDEEV GEDCPSPWPA PASPQDSLGQ DTANPNSAQV PKDDVRAMVQ LIRYMHTYCL
PQRKLPQRAS EPIPQSCSSP LRKVPPRSRQ TPKAFWTEFS ILRELLAQDI LCDVSKPYRL
ATPVYASLTP QSRTRPPKDS QASPAHSAMA EEVRITASPK STGPRPSLRP LRLEVKRDVN
KPARQKREED EEEEEEEEEE EEKEDEEEEW GRKRPGRGLP WTKLGRKMDS SVCPVRRSRR
LNPELGPWLT FTDEPLGALP SMCLATETHD LEEELGGLTD SSQGQQLPLG SQIPTLESPC
ESGCGDTDED PSCPRPPSRD SPRCLMLALS QSDPLGKKSF EESLTVELCG TAGLTPPTTP
PYKPMEEDPF KQDTKHSPGQ DTAPSLPSPE TLQLTATPGA SHKLPKRHPE RSELLSHLQH
ATTQPVSQAG QKRPFSCSFG DHDYCQVIRP EAALQRKVLR SWEPIKVHLE DLAHQGATLP
VETKTPRREA DQNCDPTPKD SMQLRDHEIR ASLTKHFGLL ETALEEEDLA SCKSPEYDTV
FEDSSSSSGE SSFLLEEEEE EGGEEDDEGE DSGVSPPCSD HCPYQSPPSK ASRQLCSRSR
SSSGSSSCSS WSPATRKNFR LESRGPCSDG TPSARHAKKR REKAIGEGRV VYIRNLSGDM
SSRELKKRFE VFGEIVECQV LRRSKRGQKH GFITFRCSEH AALSVRNGAT LRKRNEPSFH
LSYGGLRHFR WPRYTDYDPT SEESLPSSGK SKYEAMDFDS LLKEAQQSLH
