ID E9PVA2_MOUSE Unreviewed; 503 AA.
AC E9PVA2;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Ribosomal RNA-processing protein 8 {ECO:0000256|ARBA:ARBA00020203, ECO:0000256|RuleBase:RU365074};
DE EC=2.1.1.- {ECO:0000256|RuleBase:RU365074};
GN Name=Rrp8 {ECO:0000313|Ensembl:ENSMUSP00000095752.5,
GN ECO:0000313|MGI:MGI:1914251};
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 {ECO:0000313|Ensembl:ENSMUSP00000095752.5, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0007829|PubMed:17242355}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [2] {ECO:0000313|Ensembl:ENSMUSP00000095752.5, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000095752.5,
RC ECO:0000313|Proteomes:UP000000589};
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 [3] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [4] {ECO:0000313|Ensembl:ENSMUSP00000095752.5}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000095752.5};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Essential component of the eNoSC (energy-dependent nucleolar
CC silencing) complex, a complex that mediates silencing of rDNA in
CC response to intracellular energy status and acts by recruiting histone-
CC modifying enzymes. The eNoSC complex is able to sense the energy status
CC of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio
CC activates SIRT1, leading to histone H3 deacetylation followed by
CC dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation
CC of silent chromatin in the rDNA locus. In the complex, RRP8 binds to
CC H3K9me2 and probably acts as a methyltransferase.
CC {ECO:0000256|RuleBase:RU365074}.
CC -!- SUBUNIT: Component of the eNoSC complex.
CC {ECO:0000256|RuleBase:RU365074}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000256|ARBA:ARBA00004604, ECO:0000256|RuleBase:RU365074}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RRP8 family.
CC {ECO:0000256|ARBA:ARBA00006301, ECO:0000256|RuleBase:RU365074}.
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DR RefSeq; NP_598712.1; NM_133951.1.
DR AlphaFoldDB; E9PVA2; -.
DR SMR; E9PVA2; -.
DR jPOST; E9PVA2; -.
DR MaxQB; E9PVA2; -.
DR PeptideAtlas; E9PVA2; -.
DR ProteomicsDB; 345335; -.
DR Antibodypedia; 23905; 194 antibodies from 29 providers.
DR DNASU; 101867; -.
DR Ensembl; ENSMUST00000098148.6; ENSMUSP00000095752.5; ENSMUSG00000030888.15.
DR GeneID; 101867; -.
DR UCSC; uc009iza.2; mouse.
DR AGR; MGI:1914251; -.
DR CTD; 23378; -.
DR MGI; MGI:1914251; Rrp8.
DR VEuPathDB; HostDB:ENSMUSG00000030888; -.
DR GeneTree; ENSGT00390000006189; -.
DR OrthoDB; 1694at2759; -.
DR PhylomeDB; E9PVA2; -.
DR BioGRID-ORCS; 101867; 5 hits in 79 CRISPR screens.
DR ChiTaRS; Rrp8; mouse.
DR Proteomes; UP000000589; Chromosome 7.
DR Bgee; ENSMUSG00000030888; Expressed in animal zygote and 219 other cell types or tissues.
DR ExpressionAtlas; E9PVA2; baseline and differential.
DR Genevisible; E9PVA2; MM.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0061773; C:eNoSc complex; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0033553; C:rDNA heterochromatin; IEA:Ensembl.
DR GO; GO:0035064; F:methylated histone binding; IEA:Ensembl.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0042149; P:cellular response to glucose starvation; IEA:Ensembl.
DR GO; GO:0097009; P:energy homeostasis; IEA:Ensembl.
DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IEA:Ensembl.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0045786; P:negative regulation of cell cycle; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:Ensembl.
DR GO; GO:0031065; P:positive regulation of histone deacetylation; IEA:Ensembl.
DR GO; GO:0000183; P:rDNA heterochromatin formation; IEA:Ensembl.
DR GO; GO:1903450; P:regulation of G1 to G0 transition; IEA:Ensembl.
DR GO; GO:0046015; P:regulation of transcription by glucose; IEA:Ensembl.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 1.10.10.2150; Ribosomal RNA-processing protein 8, N-terminal domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR007823; RRP8.
DR InterPro; IPR042036; RRP8_N.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR12787:SF0; RIBOSOMAL RNA-PROCESSING PROTEIN 8; 1.
DR PANTHER; PTHR12787; UNCHARACTERIZED; 1.
DR Pfam; PF05148; Methyltransf_8; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 1: Evidence at protein level;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|RuleBase:RU365074};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365074};
KW Proteomics identification {ECO:0007829|EPD:E9PVA2,
KW ECO:0007829|MaxQB:E9PVA2};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552,
KW ECO:0000256|RuleBase:RU365074};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|RuleBase:RU365074};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365074}.
FT REGION 97..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..249
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 503 AA; 56512 MW; E54C918F70482870 CRC64;
MSTPSSGERT CSRLTRQRFS SPLIEVVLCV VQPQAHRHRV ALPALSENVV HSSVPAQRPR
DWGSLGGLRE NRDKRMTLCG RKRRHLLATL RALEAASLSQ QTPSLPGSDS EEEEEVGRKK
RHLQRPSLAS VSKEVGKKRK GKCQKQAPSI SDSEGKEIRR KCHRQAPPLG GVSAGEEKGK
RKCQEYSSLH LTQPLDSVDQ TVHNSRTSTA TIDPSKPSPE SMSPNSSHTL SRKQWRNRQK
NKRRHKNKFR PLQTPEQAPP KASIEETEVP PVPKSDSQES RAGALRARMT QRLDGARFRY
LNEQLYSGPS SAARRLFQED PEAFLLYHRG FQRQVKKWPL HPVDRIAKDL RQKPASLVVA
DFGCGDCRLA SSVRNPVHCF DLASLDPRVT VCDMAQVPLE DESVDVAVFC LSLMGTNIRD
FLEEANRVLK TGGLLKVAEV SSRFEDIRTF LGAVTKLGFK IIYKDLTNSH FFLFDFEKTG
PPRVGPKAQL SGLKLQPCLY KRR
//
