PRGC1_PIG
ID PRGC1_PIG Reviewed; 796 AA.
AC Q865B6;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 119.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chikuni K., Muroya S., Nakajima I.;
RT "Sequences of bovine and swine PGC-1alpha.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS SER-430 AND VAL-790.
RA Milosevic Berlic T., Kokalj-Vokac N., Anderson S.I., Archibald A.L.,
RA Dovc P.;
RT "Porcine peroxisome proliferative activated receptor gamma coactivator-1
RT (ppargc1) gene: cDNA sequence, chromosomal localization and
RT polymorphisms.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcriptional coactivator for steroid receptors and nuclear
CC receptors. Greatly increases the transcriptional activity of PPARG and
CC thyroid hormone receptor on the uncoupling protein promoter. Can
CC regulate key mitochondrial genes that contribute to the program of
CC adaptive thermogenesis. 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. Acts as a key regulator of gluconeogenesis:
CC stimulates hepatic gluconeogenesis by increasing the expression of
CC gluconeogenic enzymes, and acting together with FOXO1 to promote the
CC fasting gluconeogenic program (By similarity). Induces the expression
CC of PERM1 in the skeletal muscle in an ESRRA-dependent manner. Also
CC involved in the integration of the circadian rhythms and energy
CC metabolism. Required for oscillatory expression of clock genes, such as
CC ARNTL/BMAL1 and NR1D1, through the coactivation of RORA and RORC, and
CC metabolic genes, such as PDK4 and PEPCK (By similarity).
CC {ECO:0000250|UniProtKB:O70343, ECO:0000250|UniProtKB:Q9UBK2}.
CC -!- SUBUNIT: Homooligomer (By similarity). Interacts with MYBBP1A; inhibits
CC MYBBP1A transcriptional activation. Interacts with PRDM16, LPIN1 and
CC PML. Interacts (via LXXLL motif) with RORA and RORC (via AF-2 motif);
CC activates RORA and RORC transcriptional activation (By similarity).
CC Interacts with LRPPRC (By similarity). Interacts with FOXO1 (By
CC similarity). {ECO:0000250|UniProtKB:O70343,
CC ECO:0000250|UniProtKB:Q9UBK2}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O70343}. Nucleus,
CC PML body {ECO:0000250|UniProtKB:O70343}.
CC -!- PTM: Phosphorylation by AMPK in skeletal muscle increases activation of
CC its own promoter. Phosphorylated by CLK2.
CC {ECO:0000250|UniProtKB:O70343}.
CC -!- PTM: Heavily acetylated by KAT2A/GCN5 under conditions of high
CC nutrients, leading to inactivation of PPARGC1A. Deacetylated by SIRT1
CC in low nutrients/high NAD conditions, leading to its activation.
CC {ECO:0000250|UniProtKB:Q9UBK2}.
CC -!- PTM: Ubiquitinated. Ubiquitination by RNF34 induces proteasomal
CC degradation. {ECO:0000250|UniProtKB:Q9UBK2}.
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DR EMBL; AB106108; BAC66019.1; -; mRNA.
DR EMBL; AY346131; AAQ54575.1; -; mRNA.
DR RefSeq; NP_999128.2; NM_213963.2.
DR AlphaFoldDB; Q865B6; -.
DR SMR; Q865B6; -.
DR STRING; 9823.ENSSSCP00000026890; -.
DR PaxDb; Q865B6; -.
DR Ensembl; ENSSSCT00000045482; ENSSSCP00000032437; ENSSSCG00000029275.
DR Ensembl; ENSSSCT00005033988; ENSSSCP00005020748; ENSSSCG00005021108.
DR Ensembl; ENSSSCT00030063112; ENSSSCP00030028869; ENSSSCG00030045092.
DR Ensembl; ENSSSCT00040037153; ENSSSCP00040015451; ENSSSCG00040027395.
DR Ensembl; ENSSSCT00055035477; ENSSSCP00055028183; ENSSSCG00055018093.
DR Ensembl; ENSSSCT00060098488; ENSSSCP00060042713; ENSSSCG00060071790.
DR Ensembl; ENSSSCT00065057615; ENSSSCP00065025022; ENSSSCG00065042112.
DR Ensembl; ENSSSCT00070045683; ENSSSCP00070038505; ENSSSCG00070022943.
DR GeneID; 397013; -.
DR KEGG; ssc:397013; -.
DR CTD; 10891; -.
DR VGNC; VGNC:91685; PPARGC1A.
DR eggNOG; ENOG502QSXU; Eukaryota.
DR GeneTree; ENSGT00950000183137; -.
DR InParanoid; Q865B6; -.
DR OMA; KCPSKKK; -.
DR OrthoDB; 94418at2759; -.
DR Proteomes; UP000008227; Chromosome 8.
DR Proteomes; UP000314985; Chromosome 8.
DR Bgee; ENSSSCG00000029275; Expressed in heart left ventricle and 38 other tissues.
DR ExpressionAtlas; Q865B6; baseline and differential.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:AgBase.
DR GO; GO:0016922; F:nuclear receptor binding; IEA:Ensembl.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0060612; P:adipose tissue development; IEA:Ensembl.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0097009; P:energy homeostasis; ISS:UniProtKB.
DR GO; GO:0006094; P:gluconeogenesis; ISS:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; IEA:InterPro.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:1901215; P:negative regulation of neuron death; ISS:UniProtKB.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:2001171; P:positive regulation of ATP biosynthetic process; ISS:UniProtKB.
DR GO; GO:1901857; P:positive regulation of cellular respiration; IEA:Ensembl.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IEA:Ensembl.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:1901860; P:positive regulation of mitochondrial DNA metabolic process; IEA:Ensembl.
DR GO; GO:0010822; P:positive regulation of mitochondrion organization; ISS:UniProtKB.
DR GO; GO:1901863; P:positive regulation of muscle tissue development; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:AgBase.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:AgBase.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0022904; P:respiratory electron transport chain; ISS:UniProtKB.
DR GO; GO:0002021; P:response to dietary excess; IEA:Ensembl.
DR GO; GO:0014850; P:response to muscle activity; ISS:UniProtKB.
DR CDD; cd12623; RRM_PPARGC1A; 1.
DR Gene3D; 3.30.70.330; -; 1.
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 2: Evidence at transcript level;
KW Acetylation; Activator; Biological rhythms; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..796
FT /note="Peroxisome proliferator-activated receptor gamma
FT coactivator 1-alpha"
FT /id="PRO_0000081734"
FT DOMAIN 675..751
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 98..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..337
FT /note="Interaction with PPARG"
FT /evidence="ECO:0000250|UniProtKB:Q9UBK2"
FT REGION 348..796
FT /note="Mediates interaction with RNF34"
FT /evidence="ECO:0000250|UniProtKB:Q9UBK2"
FT REGION 463..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 142..146
FT /note="LXXLL motif"
FT COMPBIAS 220..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O70343"
FT MOD_RES 144
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O70343"
FT MOD_RES 176
FT /note="Phosphothreonine; by AMPK"
FT /evidence="ECO:0000250|UniProtKB:O70343"
FT MOD_RES 182
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O70343"
FT MOD_RES 252
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O70343"
FT MOD_RES 269
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O70343"
FT MOD_RES 276
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O70343"
FT MOD_RES 319
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O70343"
FT MOD_RES 345
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O70343"
FT MOD_RES 411
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O70343"
FT MOD_RES 449
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O70343"
FT MOD_RES 537
FT /note="Phosphoserine; by AMPK"
FT /evidence="ECO:0000250|UniProtKB:O70343"
FT MOD_RES 756
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O70343"
FT MOD_RES 777
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O70343"
FT VARIANT 430
FT /note="C -> S"
FT /evidence="ECO:0000269|Ref.2"
FT VARIANT 790
FT /note="A -> V"
FT /evidence="ECO:0000269|Ref.2"
SQ SEQUENCE 796 AA; 90336 MW; 10C5574559D1BCCF CRC64;
MAWDMCNQDS VWTDIECAAL VGEDQPLCPD LPELDLSELD VNDLDTDSFL GGLKWCSDQS
EIISNQYNNE PSNIFEKIDE ENEANLLAVL TETLDSLPVD EDGLPSFDAL TDGDVTTENE
ASPSSMPDGT PPPQEAEEPS LLKKLLLAPA NTQLSYNECS GLSTQNHANH NHRIRTNPAV
VKTENSWSNK AKSICQQQKP QRRPCSELLK YLTTNDDPPH TKPTETRNSS RDKCTSKKKA
HTQSQSQHLQ AKPTSLSLPL TPESPNDPKG SPFENKTIER TLSVELSGTA GLTPPTTPPH
KANQDNPFRA SPKLKPPCKT VVPPPSKKTR YSESSGTHGN NSTKKGPEQS ELYAQLSKTS
ALGGGHEERK ARRPSLRLFG DHDYCQSINS KAEILINISQ ELHDSRQLDS KDAASDWQRQ
MCSSTDSDQC YLTETSEASR QVSPGSARKQ LQDQEIRAEL NKHFGHPSQA VFDDEADKTS
ELRDSDFSNE QFSKLPMFIN SGLAMDGLFD DSEDESDKLN SPWDGTQSYS LFDVSPSCSS
FNSPCRDSVS PPKSLFSQRP QRMRSRSRSF SQHRSCSRSP YSRSRSRSPG SRSSSRSCYY
SESGHCRHRT HRNSPLCARS RSRSPYSRRP RYDSYEEYQH ERLKREEYRR EYEKRESERA
KQRERQRQKA IEERRVIYVG KIRPDTTRTE LRDRFEVFGE IEECTVNLRD DGDSYGFITY
RYTCDAFAAL ENGYTLRRSN ETDFELYFCG RKQFFKSNYA DLDSNSDDFD PASTKSKYDS
LDFDSLLKEA QRSLRR
