RRP8_RAT
ID RRP8_RAT Reviewed; 457 AA.
AC Q5U4F0;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Ribosomal RNA-processing protein 8;
DE EC=2.1.1.-;
DE AltName: Full=Cerebral protein 1 homolog;
GN Name=Rrp8;
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 [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND SER-64, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. Its substrates are
CC however unknown (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the eNoSC complex, composed of SIRT1, SUV39H1 and
CC RRP8. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Note=Localizes
CC at rDNA locus. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RRP8 family.
CC {ECO:0000305}.
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DR EMBL; BC085119; AAH85119.1; -; mRNA.
DR RefSeq; NP_001008347.1; NM_001008346.1.
DR AlphaFoldDB; Q5U4F0; -.
DR SMR; Q5U4F0; -.
DR STRING; 10116.ENSRNOP00000025651; -.
DR iPTMnet; Q5U4F0; -.
DR PhosphoSitePlus; Q5U4F0; -.
DR PaxDb; Q5U4F0; -.
DR PRIDE; Q5U4F0; -.
DR GeneID; 308911; -.
DR KEGG; rno:308911; -.
DR UCSC; RGD:1308302; rat.
DR CTD; 23378; -.
DR RGD; 1308302; Rrp8.
DR VEuPathDB; HostDB:ENSRNOG00000018766; -.
DR eggNOG; KOG3045; Eukaryota.
DR HOGENOM; CLU_027694_2_3_1; -.
DR InParanoid; Q5U4F0; -.
DR OMA; QNQVKKW; -.
DR OrthoDB; 945819at2759; -.
DR PhylomeDB; Q5U4F0; -.
DR TreeFam; TF313749; -.
DR Reactome; R-RNO-427359; SIRT1 negatively regulates rRNA expression.
DR PRO; PR:Q5U4F0; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000018766; Expressed in thymus and 20 other tissues.
DR ExpressionAtlas; Q5U4F0; baseline and differential.
DR Genevisible; Q5U4F0; RN.
DR GO; GO:0005677; C:chromatin silencing complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0061773; C:eNoSc complex; ISO:RGD.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0033553; C:rDNA heterochromatin; ISS:UniProtKB.
DR GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0042149; P:cellular response to glucose starvation; ISO:RGD.
DR GO; GO:0097009; P:energy homeostasis; ISO:RGD.
DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; ISO:RGD.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0045786; P:negative regulation of cell cycle; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0031065; P:positive regulation of histone deacetylation; ISO:RGD.
DR GO; GO:0031062; P:positive regulation of histone methylation; ISO:RGD.
DR GO; GO:0000183; P:rDNA heterochromatin assembly; ISS:UniProtKB.
DR GO; GO:1903450; P:regulation of G1 to G0 transition; ISO:RGD.
DR GO; GO:0046015; P:regulation of transcription by glucose; ISO:RGD.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.2150; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR007823; RRP8.
DR InterPro; IPR042036; RRP8_N.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR023576; UbiE/COQ5_MeTrFase_CS.
DR PANTHER; PTHR12787; PTHR12787; 1.
DR Pfam; PF05148; Methyltransf_8; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Methyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; rRNA processing; S-adenosyl-L-methionine;
KW Transcription; Transcription regulation; Transferase.
FT CHAIN 1..457
FT /note="Ribosomal RNA-processing protein 8"
FT /id="PRO_0000084092"
FT REGION 52..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..202
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 282
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43159"
FT BINDING 317
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43159"
FT BINDING 335
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43159"
FT BINDING 347
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43159"
FT BINDING 348
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43159"
FT BINDING 364
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43159"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43159"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43159"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43159"
SQ SEQUENCE 457 AA; 51216 MW; 37B2AF0216D48F6F CRC64;
MFEEPEWVEA APAIVGLRPV TTQVQAATAP PVKGRKRRHL LATLRALEAA SLSQQCPSLP
GSDSEEEEEV GRKKRHFQRS SLANVSKEVG KKRKGKCQKQ APFISDSEGK EVERTCHRQA
PPLGGISAGE EKGKRKCQEY SYLHPTQSLN SVDQTVHNSR TSTATLDPPK SSRESASPNS
SHTLSRKQWR NRQKNKRRHK NKFRPLETQD QVPLKASIEE TEVPPAPKSD SQETRAGALR
ARMTQRLDGA RFRYLNEQLY SGPSSAAQCL FQEDPEAFLL YHRGFQRQVK KWPLHPVDRI
AKDLRQKPAS LVVADFGCGD CRLASSVRNP VHCFDLAALD PRVTVCDMAQ VPLEDESVDV
AVFCLSLMGT NIRDFLEEAN RVLKPGGLLK VAEVSSRFED IRTFLGAVTK LGFKVIYKDL
TNSHFFLFDF EKTGPPRVGP KAQLSGLKLQ PCLYKHR
