PERM1_MOUSE
ID PERM1_MOUSE Reviewed; 807 AA.
AC Q149B8; E9QP35; Q8BS19; Q8CB71;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=PGC-1 and ERR-induced regulator in muscle protein 1;
DE AltName: Full=PPARGC1 and ESRR-induced regulator in muscle 1;
DE AltName: Full=Peroxisome proliferator-activated receptor gamma coactivator 1 and estrogen-related receptor-induced regulator in muscle 1;
GN Name=Perm1;
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], FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND
RP TISSUE SPECIFICITY.
RX PubMed=23836911; DOI=10.1074/jbc.m113.489674;
RA Cho Y., Hazen B.C., Russell A.P., Kralli A.;
RT "Peroxisome proliferator-activated receptor gamma coactivator 1 (PGC-
RT 1)- and estrogen-related receptor (ERR)-induced regulator in muscle 1
RT (Perm1) is a tissue-specific regulator of oxidative capacity in skeletal
RT muscle cells.";
RL J. Biol. Chem. 288:25207-25218(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Aorta, and Bone;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198 AND THR-534, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, and Heart;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-548, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Regulates the expression of selective PPARGC1A/B and
CC ESRRA/B/G target genes with roles in glucose and lipid metabolism,
CC energy transfer, contractile function, muscle mitochondrial biogenesis
CC and oxidative capacity. Required for the efficient induction of MT-CO2,
CC MT-CO3, COX4I1, TFB1M, TFB2M, POLRMT and SIRT3 by PPARGC1A. Positively
CC regulates the PPARGC1A/ESRRG-induced expression of CKMT2, TNNI3 and
CC SLC2A4 and negatively regulates the PPARGC1A/ESRRG-induced expression
CC of PDK4. {ECO:0000269|PubMed:23836911}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23836911}. Nucleus
CC {ECO:0000269|PubMed:23836911}. Note=Shows a nuclear localization in the
CC presence of PPARGC1A.
CC -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscles and heart with
CC lower levels in brown adipose tissue (at protein level). Muscle-
CC specific expression is increased by endurance exercise.
CC {ECO:0000269|PubMed:23836911}.
CC -!- INDUCTION: By PPARGC1A, PPARGC1B, ESRRA, ESRRB and ESRRG.
CC {ECO:0000269|PubMed:23836911}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC29522.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC30714.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; KF150176; AGQ48859.1; -; mRNA.
DR EMBL; AK036660; BAC29522.1; ALT_SEQ; mRNA.
DR EMBL; AK040833; BAC30714.1; ALT_FRAME; mRNA.
DR EMBL; CAAA01066807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT998563; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC117871; AAI17872.1; -; mRNA.
DR EMBL; BC117872; AAI17873.1; -; mRNA.
DR CCDS; CCDS51406.1; -.
DR RefSeq; NP_766005.2; NM_172417.3.
DR RefSeq; XP_006539275.1; XM_006539212.3.
DR AlphaFoldDB; Q149B8; -.
DR STRING; 10090.ENSMUSP00000101197; -.
DR iPTMnet; Q149B8; -.
DR PhosphoSitePlus; Q149B8; -.
DR MaxQB; Q149B8; -.
DR PaxDb; Q149B8; -.
DR PeptideAtlas; Q149B8; -.
DR PRIDE; Q149B8; -.
DR ProteomicsDB; 288033; -.
DR Antibodypedia; 51128; 25 antibodies from 7 providers.
DR DNASU; 74183; -.
DR Ensembl; ENSMUST00000105572; ENSMUSP00000101197; ENSMUSG00000078486.
DR GeneID; 74183; -.
DR KEGG; mmu:74183; -.
DR UCSC; uc008wgm.1; mouse.
DR CTD; 84808; -.
DR MGI; MGI:1921433; Perm1.
DR VEuPathDB; HostDB:ENSMUSG00000078486; -.
DR eggNOG; ENOG502RYI7; Eukaryota.
DR GeneTree; ENSGT00390000017652; -.
DR HOGENOM; CLU_015049_1_0_1; -.
DR InParanoid; Q149B8; -.
DR OMA; EVQWPDT; -.
DR OrthoDB; 452214at2759; -.
DR PhylomeDB; Q149B8; -.
DR TreeFam; TF338365; -.
DR BioGRID-ORCS; 74183; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Perm1; mouse.
DR PRO; PR:Q149B8; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q149B8; protein.
DR Bgee; ENSMUSG00000078486; Expressed in interventricular septum and 81 other tissues.
DR Genevisible; Q149B8; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0014850; P:response to muscle activity; IDA:UniProtKB.
DR InterPro; IPR043442; Perm1.
DR PANTHER; PTHR47282; PTHR47282; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..807
FT /note="PGC-1 and ERR-induced regulator in muscle protein 1"
FT /id="PRO_0000299541"
FT REGION 29..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 534
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 548
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CONFLICT 270
FT /note="A -> V (in Ref. 4; AAI17872/AAI17873)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="Q -> QSTPASEPDTALSTPASEPDTALSTPASEPDTAL (in Ref. 4;
FT AAI17872/AAI17873)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="M -> T (in Ref. 4; AAI17872/AAI17873)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="T -> M (in Ref. 4; AAI17872/AAI17873)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="T -> M (in Ref. 4; AAI17872/AAI17873)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="T -> P (in Ref. 4; AAI17872/AAI17873)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 807 AA; 85157 MW; 4C1943E985F3B89E CRC64;
MDNFQYSVQL SDREWAEFSA TADECGLLQA DLASGDEPLS SDIDQGDSSG SSPPGPPPLF
TGQLVSQGRG QQSRELEDVA AQQLVSRSQC EPVLALEASH QVAGTSTQSE APLFPSLDSV
CPGQALSFPG PATCRDKMQR LLQGPAPSSP SKAPHSPESP GHSDNPQSSP DSLEASPRNP
GRKKRRAVGA KGTKHSGSLD SAATQMSSPQ LTRPKEALMS GTLMAKAQQD KPQPDSTSPE
QMAREESGLD LSTPILITEQ DQIRKTSRAA LHVVSKPVQE VHPDVPMASP NVSTRASKPQ
PDVALPKPAS KPQSDIASST HPFTPDVSLS TLAFKCQPNT NQSTPASEPD MALSTPASEP
DTALSTPASE PDTALSTPAS EPDTALSTPA SRSQLVKAEF ASACTPGLHV DLSAAGSEIK
PEVSSSMPAA VDVLRTDLPR SVSKTESKES VSIPVKPSLS PISQAEAAMV DTGVSVPPGG
SIEKPAGQFS AGSSGESCLG PVQAPKKKKV RFSMAIPSHE DSGSGEPTGS PFLTPEQPPV
PRTAAGSRGG SAAWDAVAVA PRLPQPRILK HLPPPVSSVS AEAESGNCFA VTLPEAYEFF
FCDTIEEEDE DVEDEEAASQ ALDEVQWPDT CEFFFRDSRA QRSRCQRGHS PVSPPRADTV
APVPPEGLVP ISIPEVYEHF FTEEGFGHRQ PAATPMQTSE LSREGGLEAS TKPVSPTAEH
LSLTVRKAGE LRSPLTSFTF SQNDMCLVFV AFATWAVRTS DLQAPDAWKT VLLANIGTIS
AIRYFRRQVG RGHSGRPRSS SSSNPSC
