ID A0A096MJD6_RAT Unreviewed; 452 AA.
AC A0A096MJD6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 42.
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:ENSRNOP00000068089.2,
GN ECO:0000313|RGD:1308302};
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 {ECO:0000313|Ensembl:ENSRNOP00000068089.2, ECO:0000313|Proteomes:UP000002494};
RN [1] {ECO:0000313|Ensembl:ENSRNOP00000068089.2, ECO:0000313|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000068089.2,
RC ECO:0000313|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RG Rat Genome Sequencing Project Consortium;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000313|Ensembl:ENSRNOP00000068089.2}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000068089.2};
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 AlphaFoldDB; A0A096MJD6; -.
DR Ensembl; ENSRNOT00000076100.2; ENSRNOP00000068089.2; ENSRNOG00000018766.7.
DR RGD; 1308302; Rrp8.
DR VEuPathDB; HostDB:ENSRNOG00000018766; -.
DR GeneTree; ENSGT00390000006189; -.
DR HOGENOM; CLU_027694_1_2_1; -.
DR OMA; QNQVKKW; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000018766; Expressed in thymus and 20 other cell types or tissues.
DR ExpressionAtlas; A0A096MJD6; baseline and differential.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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 InterPro; IPR023576; UbiE/COQ5_MeTrFase_CS.
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.
DR PROSITE; PS01184; UBIE_2; 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|PeptideAtlas:A0A096MJD6};
KW Reference proteome {ECO:0000313|Proteomes:UP000002494};
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..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..197
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 452 AA; 50639 MW; AC289CD140F10C5A CRC64;
QRPGTETPGL GKSRGTAGEQ RQENDSISGR KRRHLLATLR ALEAASLSQQ CPSLPGSDSE
EEEEVGRKKR HFQRSSLANV SKEVGKKRKG KCQKQAPFIS DSEGKEVERT CHRQAPPLGG
ISAGEEKGKR KCQEYSYLHP TQSLNSVDQT VHNSRTSTAT LDPPKSSRES ASPNSSHTLS
RKQWRNRQKN KRRHKNKFRP LETQDQVPLK ASIEETEVPP APKSDSQETR AGALRARMTQ
RLDGARFRYL NEQLYSGPSS AAQCLFQEDP EAFLLYHRGF QRQVKKWPLH PVDRIAKDLR
QKPASLVVAD FGCGDCRLAS SVRNPVHCFD LAALDPRVTV CDMAQVPLED ESVDVAVFCL
SLMGTNIRDF LEEANRVLKP GGLLKVAEVS SRFEDIRTFL GAVTKLGFKV IYKDLTNSHF
FLFDFEKTGP PRVGPKAQLS GLKLQPCLYK HR
//
