MPP6_YEAST
ID MPP6_YEAST Reviewed; 186 AA.
AC P53725; D6W1J9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=M-phase phosphoprotein 6 homolog;
DE AltName: Full=Exosome-associated RNA-binding protein MPP6;
GN Name=MPP6; OrderedLocusNames=YNR024W; ORFNames=N3230;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=16702403; DOI=10.1101/gad.1422006;
RA Fleischer T.C., Weaver C.M., McAfee K.J., Jennings J.L., Link A.J.;
RT "Systematic identification and functional screens of uncharacterized
RT proteins associated with eukaryotic ribosomal complexes.";
RL Genes Dev. 20:1294-1307(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
RP FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18591258; DOI=10.1128/mcb.00463-08;
RA Milligan L., Decourty L., Saveanu C., Rappsilber J., Ceulemans H.,
RA Jacquier A., Tollervey D.;
RT "A yeast exosome cofactor, Mpp6, functions in RNA surveillance and in the
RT degradation of noncoding RNA transcripts.";
RL Mol. Cell. Biol. 28:5446-5457(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 AND SER-150, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [9]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19046973; DOI=10.1016/j.jmb.2008.11.011;
RA Synowsky S.A., van Wijk M., Raijmakers R., Heck A.J.;
RT "Comparative multiplexed mass spectrometric analyses of endogenously
RT expressed yeast nuclear and cytoplasmic exosomes.";
RL J. Mol. Biol. 385:1300-1313(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Involved in surveillance of pre-rRNAs and pre-mRNAs, and the
CC degradation of cryptic non-coding RNAs (ncRNA) derived from intergenic
CC regions and the ribosomal DNA spacer heterochromatin. Binds RNA.
CC {ECO:0000269|PubMed:18591258}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:16702403, ECO:0000269|PubMed:18591258,
CC ECO:0000269|PubMed:19046973}. Note=Colocalizes with the nuclear exosome
CC and ribosomes.
CC -!- DISRUPTION PHENOTYPE: Lethal in combination with the absence of either
CC RRP6 or its cofactor RRP47. Weak but detectable stabilization of
CC unspliced pre-mRNAs, and stronger stabilization is detected for mRNAs
CC with defects in 3' cleavage and polyadenylation.
CC {ECO:0000269|PubMed:18591258}.
CC -!- MISCELLANEOUS: Present with 1350 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z71639; CAA96303.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10565.1; -; Genomic_DNA.
DR PIR; S63355; S63355.
DR RefSeq; NP_014421.3; NM_001183201.3.
DR PDB; 5OKZ; X-ray; 3.20 A; J/T/d/n=1-186.
DR PDB; 5VZJ; X-ray; 3.30 A; L=81-120.
DR PDB; 6FSZ; EM; 4.60 A; NN=90-118.
DR PDB; 6LQS; EM; 3.80 A; M6=1-186.
DR PDB; 7D4I; EM; 4.00 A; M6=1-186.
DR PDBsum; 5OKZ; -.
DR PDBsum; 5VZJ; -.
DR PDBsum; 6FSZ; -.
DR PDBsum; 6LQS; -.
DR PDBsum; 7D4I; -.
DR AlphaFoldDB; P53725; -.
DR SMR; P53725; -.
DR BioGRID; 35849; 97.
DR DIP; DIP-4263N; -.
DR IntAct; P53725; 2.
DR MINT; P53725; -.
DR STRING; 4932.YNR024W; -.
DR iPTMnet; P53725; -.
DR MaxQB; P53725; -.
DR PaxDb; P53725; -.
DR PRIDE; P53725; -.
DR EnsemblFungi; YNR024W_mRNA; YNR024W; YNR024W.
DR GeneID; 855758; -.
DR KEGG; sce:YNR024W; -.
DR SGD; S000005307; MPP6.
DR VEuPathDB; FungiDB:YNR024W; -.
DR eggNOG; ENOG502SFA3; Eukaryota.
DR HOGENOM; CLU_132767_0_0_1; -.
DR InParanoid; P53725; -.
DR OMA; FRDNSEW; -.
DR BioCyc; YEAST:G3O-33338-MON; -.
DR PRO; PR:P53725; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53725; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0008266; F:poly(U) RNA binding; IDA:SGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:SGD.
DR GO; GO:0000467; P:exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0071031; P:nuclear mRNA surveillance of mRNA 3'-end processing; IGI:SGD.
DR GO; GO:0071030; P:nuclear mRNA surveillance of spliceosomal pre-mRNA splicing; IGI:SGD.
DR GO; GO:0071039; P:nuclear polyadenylation-dependent CUT catabolic process; IMP:SGD.
DR GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IGI:SGD.
DR InterPro; IPR019324; MPP6.
DR Pfam; PF10175; MPP6; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; rRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..186
FT /note="M-phase phosphoprotein 6 homolog"
FT /id="PRO_0000203474"
FT REGION 22..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..186
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:5VZJ"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:5OKZ"
SQ SEQUENCE 186 AA; 21142 MW; B1DEE530E6F9379C CRC64;
MSANNGVTGK LSSRVMNMKF MKFGKTDDEE SSNSNTPSNI NSDVEPIEQK GKLFGLDDSA
WDLNSYKDDL KKISGKEKKK VKRVVYKKRP NLIISNVGYS ELRKPEGVIS GRKTFGDNSD
DSGSRKRKFD EGEQNEDEKR DAKDKEFTGS QDDGEDEYDL DKLFKDSIKK KKTNHNGKNK
NRNSKK
