ID   MRT4_YEAST              Reviewed;         236 AA.
AC   P33201; D6VXS7;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   27-MAR-2024, entry version 181.
DE   RecName: Full=Ribosome assembly factor MRT4 {ECO:0000303|PubMed:19346338};
DE   AltName: Full=mRNA turnover protein 4 {ECO:0000303|PubMed:10471698};
GN   Name=MRT4 {ECO:0000303|PubMed:10471698};
GN   OrderedLocusNames=YKL009W {ECO:0000312|SGD:S000001492};
GN   ORFNames=YKL160;
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 [GENOMIC DNA].
RX   PubMed=1481574; DOI=10.1002/yea.320081109;
RA   Pascolo S., Ghazvini M., Boyer J., Colleaux L., Thierry A., Dujon B.;
RT   "The sequence of a 9.3 kb segment located on the left arm of the yeast
RT   chromosome XI reveals five open reading frames including the CCE1 gene and
RT   putative products related to MYO2 and to the ribosomal protein L10.";
RL   Yeast 8:987-995(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 190-236.
RX   PubMed=8488728; DOI=10.1002/yea.320090307;
RA   Boyer J., Pascolo S., Richard G.-F., Dujon B.;
RT   "Sequence of a 7.8 kb segment on the left arm of yeast chromosome XI
RT   reveals four open reading frames, including the CAP1 gene, an intron-
RT   containing gene and a gene encoding a homolog to the mammalian UOG-1
RT   gene.";
RL   Yeast 9:279-287(1993).
RN   [5]
RP   GENE NAME, AND INVOLVEMENT IN MRNA TURNOVER.
RX   PubMed=10471698; DOI=10.1093/genetics/153.1.35;
RA   Zuk D., Belk J.P., Jacobson A.;
RT   "Temperature-sensitive mutations in the Saccharomyces cerevisiae MRT4,
RT   GRC5, SLA2 and THS1 genes result in defects in mRNA turnover.";
RL   Genetics 153:35-47(1999).
RN   [6]
RP   SUBCELLULAR LOCATION, AND INVOLVEMENT IN RIBOSOME BIOGENESIS.
RX   PubMed=11583614; DOI=10.1016/s1097-2765(01)00344-6;
RA   Harnpicharnchai P., Jakovljevic J., Horsey E., Miles T., Roman J., Rout M.,
RA   Meagher D., Imai B., Guo Y., Brame C.J., Shabanowitz J., Hunt D.F.,
RA   Woolford J.L. Jr.;
RT   "Composition and functional characterization of yeast 66S ribosome assembly
RT   intermediates.";
RL   Mol. Cell 8:505-515(2001).
RN   [7]
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   [8]
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   FUNCTION, SUBUNIT, AND MUTAGENESIS OF GLY-68.
RX   PubMed=19797078; DOI=10.1083/jcb.200904110;
RA   Lo K.Y., Li Z., Wang F., Marcotte E.M., Johnson A.W.;
RT   "Ribosome stalk assembly requires the dual-specificity phosphatase Yvh1 for
RT   the exchange of Mrt4 with P0.";
RL   J. Cell Biol. 186:849-862(2009).
RN   [10]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=19346338; DOI=10.1093/nar/gkp209;
RA   Rodriguez-Mateos M., Abia D., Garcia-Gomez J.J., Morreale A.,
RA   de la Cruz J., Santos C., Remacha M., Ballesta J.P.;
RT   "The amino terminal domain from Mrt4 protein can functionally replace the
RT   RNA binding domain of the ribosomal P0 protein.";
RL   Nucleic Acids Res. 37:3514-3521(2009).
RN   [11]
RP   FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=19789271; DOI=10.1093/nar/gkp806;
RA   Rodriguez-Mateos M., Garcia-Gomez J.J., Francisco-Velilla R., Remacha M.,
RA   de la Cruz J., Ballesta J.P.;
RT   "Role and dynamics of the ribosomal protein P0 and its related trans-acting
RT   factor Mrt4 during ribosome assembly in Saccharomyces cerevisiae.";
RL   Nucleic Acids Res. 37:7519-7532(2009).
RN   [12]
RP   STRUCTURE BY ELECTRON MICROSCOPY (8.70 ANGSTROMS).
RX   PubMed=24662372; DOI=10.1038/ncomms4491;
RA   Leidig C., Thoms M., Holdermann I., Bradatsch B., Berninghausen O.,
RA   Bange G., Sinning I., Hurt E., Beckmann R.;
RT   "60S ribosome biogenesis requires rotation of the 5S ribonucleoprotein
RT   particle.";
RL   Nat. Commun. 5:3491-3491(2014).
CC   -!- FUNCTION: Component of the ribosome assembly machinery. Nuclear paralog
CC       of the ribosomal protein P0, it binds pre-60S subunits at an early
CC       stage of assembly in the nucleolus, and is replaced by P0 in
CC       cytoplasmic pre-60S subunits and mature 80S ribosomes.
CC       {ECO:0000269|PubMed:10471698, ECO:0000269|PubMed:19346338,
CC       ECO:0000269|PubMed:19789271, ECO:0000269|PubMed:19797078}.
CC   -!- SUBUNIT: Associates with the pre-60S ribosomal particle.
CC       {ECO:0000269|PubMed:11583614, ECO:0000269|PubMed:19346338,
CC       ECO:0000269|PubMed:19789271, ECO:0000269|PubMed:19797078}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11583614,
CC       ECO:0000269|PubMed:19789271}. Cytoplasm {ECO:0000269|PubMed:19789271}.
CC       Note=Shuttles between the nucleus and the cytoplasm.
CC       {ECO:0000269|PubMed:19789271}.
CC   -!- MISCELLANEOUS: Present with 18200 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL10 family.
CC       {ECO:0000305}.
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DR   EMBL; S53418; AAB24904.1; -; Genomic_DNA.
DR   EMBL; X61398; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z28009; CAA81844.1; -; Genomic_DNA.
DR   EMBL; S59773; AAC60552.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA09147.1; -; Genomic_DNA.
DR   PIR; S30013; S30013.
DR   RefSeq; NP_012916.1; NM_001179575.1.
DR   PDB; 3JCT; EM; 3.08 A; W=1-236.
DR   PDB; 4V7F; EM; 8.70 A; n=1-236.
DR   PDB; 5JCS; EM; 9.50 A; n=1-236.
DR   PDB; 6ELZ; EM; 3.30 A; W=1-236.
DR   PDB; 6EM1; EM; 3.60 A; W=1-236.
DR   PDB; 6EM5; EM; 4.30 A; W=1-236.
DR   PDB; 6FT6; EM; 3.90 A; W=1-236.
DR   PDB; 6M62; EM; 3.20 A; W=1-236.
DR   PDB; 6N8J; EM; 3.50 A; W=1-236.
DR   PDB; 6N8K; EM; 3.60 A; W=1-236.
DR   PDB; 6N8L; EM; 3.60 A; W=1-236.
DR   PDB; 6YLG; EM; 3.00 A; W=1-236.
DR   PDB; 6YLH; EM; 3.10 A; W=1-236.
DR   PDB; 6YLX; EM; 3.90 A; W=1-236.
DR   PDB; 6YLY; EM; 3.80 A; W=1-236.
DR   PDB; 7BT6; EM; 3.12 A; W=1-236.
DR   PDB; 7BTB; EM; 3.22 A; W=1-236.
DR   PDB; 7NAC; EM; 3.04 A; W=1-236.
DR   PDB; 7OF1; EM; 3.10 A; W=1-236.
DR   PDB; 7OH3; EM; 3.40 A; W=1-236.
DR   PDB; 7OHP; EM; 3.90 A; W=1-236.
DR   PDB; 7OHQ; EM; 3.10 A; W=1-236.
DR   PDB; 7OHR; EM; 4.72 A; W=1-236.
DR   PDB; 7OHS; EM; 4.38 A; W=1-236.
DR   PDB; 7OHT; EM; 4.70 A; W=1-236.
DR   PDB; 7OHU; EM; 3.70 A; W=1-236.
DR   PDB; 7OHV; EM; 3.90 A; W=1-236.
DR   PDB; 7OHW; EM; 3.50 A; W=1-236.
DR   PDB; 7OHX; EM; 3.30 A; W=1-236.
DR   PDB; 7OHY; EM; 3.90 A; W=1-236.
DR   PDB; 7R7A; EM; 3.04 A; W=1-236.
DR   PDB; 7U0H; EM; 2.76 A; W=1-236.
DR   PDB; 7UG6; EM; 2.90 A; W=1-236.
DR   PDB; 7UOO; EM; 2.34 A; W=1-236.
DR   PDB; 7UQB; EM; 2.43 A; W=1-236.
DR   PDB; 7UQZ; EM; 2.44 A; W=1-236.
DR   PDB; 7V08; EM; 2.36 A; W=1-236.
DR   PDB; 7Z34; EM; 3.80 A; W=1-236.
DR   PDB; 8HFR; EM; 2.64 A; Wg=1-236.
DR   PDBsum; 3JCT; -.
DR   PDBsum; 4V7F; -.
DR   PDBsum; 5JCS; -.
DR   PDBsum; 6ELZ; -.
DR   PDBsum; 6EM1; -.
DR   PDBsum; 6EM5; -.
DR   PDBsum; 6FT6; -.
DR   PDBsum; 6M62; -.
DR   PDBsum; 6N8J; -.
DR   PDBsum; 6N8K; -.
DR   PDBsum; 6N8L; -.
DR   PDBsum; 6YLG; -.
DR   PDBsum; 6YLH; -.
DR   PDBsum; 6YLX; -.
DR   PDBsum; 6YLY; -.
DR   PDBsum; 7BT6; -.
DR   PDBsum; 7BTB; -.
DR   PDBsum; 7NAC; -.
DR   PDBsum; 7OF1; -.
DR   PDBsum; 7OH3; -.
DR   PDBsum; 7OHP; -.
DR   PDBsum; 7OHQ; -.
DR   PDBsum; 7OHR; -.
DR   PDBsum; 7OHS; -.
DR   PDBsum; 7OHT; -.
DR   PDBsum; 7OHU; -.
DR   PDBsum; 7OHV; -.
DR   PDBsum; 7OHW; -.
DR   PDBsum; 7OHX; -.
DR   PDBsum; 7OHY; -.
DR   PDBsum; 7R7A; -.
DR   PDBsum; 7U0H; -.
DR   PDBsum; 7UG6; -.
DR   PDBsum; 7UOO; -.
DR   PDBsum; 7UQB; -.
DR   PDBsum; 7UQZ; -.
DR   PDBsum; 7V08; -.
DR   PDBsum; 7Z34; -.
DR   PDBsum; 8HFR; -.
DR   AlphaFoldDB; P33201; -.
DR   EMDB; EMD-0369; -.
DR   EMDB; EMD-0370; -.
DR   EMDB; EMD-0371; -.
DR   EMDB; EMD-10838; -.
DR   EMDB; EMD-10839; -.
DR   EMDB; EMD-10841; -.
DR   EMDB; EMD-10842; -.
DR   EMDB; EMD-12866; -.
DR   EMDB; EMD-12892; -.
DR   EMDB; EMD-12904; -.
DR   EMDB; EMD-12905; -.
DR   EMDB; EMD-12906; -.
DR   EMDB; EMD-12907; -.
DR   EMDB; EMD-12908; -.
DR   EMDB; EMD-12909; -.
DR   EMDB; EMD-12910; -.
DR   EMDB; EMD-12911; -.
DR   EMDB; EMD-12912; -.
DR   EMDB; EMD-12913; -.
DR   EMDB; EMD-14471; -.
DR   EMDB; EMD-24269; -.
DR   EMDB; EMD-24296; -.
DR   EMDB; EMD-26485; -.
DR   EMDB; EMD-30108; -.
DR   EMDB; EMD-30170; -.
DR   EMDB; EMD-30174; -.
DR   EMDB; EMD-34725; -.
DR   EMDB; EMD-4302; -.
DR   SMR; P33201; -.
DR   BioGRID; 34123; 535.
DR   DIP; DIP-5283N; -.
DR   IntAct; P33201; 30.
DR   MINT; P33201; -.
DR   STRING; 4932.YKL009W; -.
DR   iPTMnet; P33201; -.
DR   MaxQB; P33201; -.
DR   PaxDb; 4932-YKL009W; -.
DR   PeptideAtlas; P33201; -.
DR   EnsemblFungi; YKL009W_mRNA; YKL009W; YKL009W.
DR   GeneID; 853860; -.
DR   KEGG; sce:YKL009W; -.
DR   AGR; SGD:S000001492; -.
DR   SGD; S000001492; MRT4.
DR   VEuPathDB; FungiDB:YKL009W; -.
DR   eggNOG; KOG0816; Eukaryota.
DR   GeneTree; ENSGT00940000168261; -.
DR   HOGENOM; CLU_071690_0_0_1; -.
DR   InParanoid; P33201; -.
DR   OMA; LEWAENY; -.
DR   OrthoDB; 23333at2759; -.
DR   BioCyc; YEAST:G3O-31818-MONOMER; -.
DR   BioGRID-ORCS; 853860; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P33201; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P33201; Protein.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IDA:SGD.
DR   GO; GO:0005654; C:nucleoplasm; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0030687; C:preribosome, large subunit precursor; IDA:SGD.
DR   GO; GO:0032040; C:small-subunit processome; IPI:ComplexPortal.
DR   GO; GO:0070180; F:large ribosomal subunit rRNA binding; ISA:SGD.
DR   GO; GO:0030490; P:maturation of SSU-rRNA; NAS:ComplexPortal.
DR   GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IMP:SGD.
DR   GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:SGD.
DR   GO; GO:0000055; P:ribosomal large subunit export from nucleus; IMP:SGD.
DR   GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR   CDD; cd05796; Ribosomal_P0_like; 1.
DR   Gene3D; 3.30.70.1730; -; 1.
DR   Gene3D; 3.90.105.20; -; 1.
DR   InterPro; IPR033867; Mrt4.
DR   InterPro; IPR001790; Ribosomal_uL10.
DR   InterPro; IPR040637; Ribosomal_uL10-like_insert.
DR   InterPro; IPR043164; Ribosomal_uL10-like_insert_sf.
DR   InterPro; IPR043141; Ribosomal_uL10-like_sf.
DR   PANTHER; PTHR45841:SF1; MRNA TURNOVER PROTEIN 4 HOMOLOG; 1.
DR   PANTHER; PTHR45841; MRNA TURNOVER PROTEIN 4 MRTO4; 1.
DR   Pfam; PF00466; Ribosomal_L10; 1.
DR   Pfam; PF17777; RL10P_insert; 1.
DR   SUPFAM; SSF160369; Ribosomal protein L10-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Nucleus; Reference proteome; Ribosome biogenesis.
FT   CHAIN           1..236
FT                   /note="Ribosome assembly factor MRT4"
FT                   /id="PRO_0000154815"
FT   MUTAGEN         68
FT                   /note="G->D: Bypasses the requirement for phosphatase YVH1
FT                   for the release of MRT4."
FT                   /evidence="ECO:0000269|PubMed:19797078"
SQ   SEQUENCE   236 AA;  27058 MW;  9FCFDEE9F009F427 CRC64;
     MPRSKRSKLV TLAQTDKKGR ENKERIFDEV REALDTYRYV WVLHLDDVRT PVLQEIRTSW
     AGSKLIMGKR KVLQKALGEK REEEYKENLY QLSKLCSGVT GLLFTDEDVN TVKEYFKSYV
     RSDYSRPNTK APLTFTIPEG IVYSRGGQIP AEEDVPMIHS LEPTMRNKFE IPTKIKAGKI
     TIDSPYLVCT EGEKLDVRQA LILKQFGIAA SEFKVKVSAY YDNDSSTVES TNINME
//