ID M3Y2B7_MUSPF Unreviewed; 454 AA.
AC M3Y2B7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
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:ENSMPUP00000005468.1,
GN ECO:0000313|RefSeq:XP_004781203.2};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000005468.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000005468.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004781203.2}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004781203.2};
RG RefSeq;
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 EMBL; AEYP01101564; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004781203.2; XM_004781146.3.
DR STRING; 9669.ENSMPUP00000005468; -.
DR Ensembl; ENSMPUT00000005560.1; ENSMPUP00000005468.1; ENSMPUG00000005510.1.
DR eggNOG; KOG3045; Eukaryota.
DR GeneTree; ENSGT00390000006189; -.
DR HOGENOM; CLU_027694_2_3_1; -.
DR OMA; QNQVKKW; -.
DR Proteomes; UP000000715; Unplaced.
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 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|RuleBase:RU365074};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365074};
KW Reference proteome {ECO:0000313|Proteomes:UP000000715};
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 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..203
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 454 AA; 50829 MW; 28974FB8CAE8F213 CRC64;
MFEEPEWTEE APVATDLRPV ASRPLPASAS QIKGSKHRQL LATLRALEAA SLPQQYPSLP
DSDSEEDVVE RKKKRLKKAS SAGASVDVEK KRKKKCQKQG PPGSDYEEKE VKGKKKCLRG
ILNASDPAEE QKRKRKCQKQ APSNPAQHVD KDNKTGSKAW KSTATNNQSK PSPGSTSANP
PQTLSRKQWR NRQKNKRRHK NKFRPPDQAP ATVPTEETEM PPAPSPDNHE DRAGALRARM
AQRLDGARFR YLNEQLYSGP SSAAQRLFQE DPEAFLLYHR GFQSQVKKWP LQPVDRIAKD
LRQRPASLVV ADFGCGDCRL ASSIRNPVHC FDLASLDPRV TVCDMAQVPL EDESVDVAVF
CLSLMGTNIR DFLEEANRVL KQGGLLKVAE VSSRFEDVRT FLGAVTKLGF KVISKDLTNS
HFFLFDFEKT GPPRVGPKAQ LTGLKLQPCL YKRR
//
