RT51_YEAST
ID RT51_YEAST Reviewed; 344 AA.
AC Q02950; D6W3Q0;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=37S ribosomal protein MRP51, mitochondrial;
DE AltName: Full=Mitochondrial small ribosomal subunit protein bS1m {ECO:0000303|PubMed:28154081};
GN Name=MRP51; OrderedLocusNames=YPL118W;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF VAL-235; ASN-241;
RP PRO-260; PRO-261 AND GLU-279.
RX PubMed=9528754; DOI=10.1128/mcb.18.4.1826;
RA Green-Willms N.S., Fox T.D., Costanzo M.C.;
RT "Functional interactions between yeast mitochondrial ribosomes and mRNA 5'
RT untranslated leaders.";
RL Mol. Cell. Biol. 18:1826-1834(1998).
RN [5]
RP IDENTIFICATION IN THE MITOCHONDRIAL RIBOSOMAL SMALL COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11278769; DOI=10.1074/jbc.m010864200;
RA Saveanu C., Fromont-Racine M., Harington A., Ricard F., Namane A.,
RA Jacquier A.;
RT "Identification of 12 new yeast mitochondrial ribosomal proteins including
RT 6 that have no prokaryotic homologues.";
RL J. Biol. Chem. 276:15861-15867(2001).
RN [6]
RP IDENTIFICATION IN THE MITOCHONDRIAL RIBOSOMAL SMALL COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12392552; DOI=10.1046/j.1432-1033.2002.03226.x;
RA Gan X., Kitakawa M., Yoshino K., Oshiro N., Yonezawa K., Isono K.;
RT "Tag-mediated isolation of yeast mitochondrial ribosome and mass
RT spectrometric identification of its new components.";
RL Eur. J. Biochem. 269:5203-5214(2002).
RN [7]
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 [8]
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 [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327, AND IDENTIFICATION BY
RP 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 IDENTIFICATION BY MASS SPECTROMETRY [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).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=25609543; DOI=10.1038/ncomms7019;
RA Pfeffer S., Woellhaf M.W., Herrmann J.M., Forster F.;
RT "Organization of the mitochondrial translation machinery studied in situ by
RT cryoelectron tomography.";
RL Nat. Commun. 6:6019-6019(2015).
RN [13]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS), AND SUBUNIT.
RX PubMed=28154081; DOI=10.1126/science.aal2415;
RA Desai N., Brown A., Amunts A., Ramakrishnan V.;
RT "The structure of the yeast mitochondrial ribosome.";
RL Science 355:528-531(2017).
CC -!- FUNCTION: Component of the mitochondrial ribosome (mitoribosome), a
CC dedicated translation machinery responsible for the synthesis of
CC mitochondrial genome-encoded proteins, including at least some of the
CC essential transmembrane subunits of the mitochondrial respiratory
CC chain. The mitoribosomes are attached to the mitochondrial inner
CC membrane and translation products are cotranslationally integrated into
CC the membrane. bS1m functionally interacts with the 5'-UTR of
CC mitochondrial mRNAs. {ECO:0000269|PubMed:9528754,
CC ECO:0000305|PubMed:25609543, ECO:0000305|PubMed:28154081}.
CC -!- SUBUNIT: Component of the mitochondrial small ribosomal subunit (mt-
CC SSU). Mature yeast 74S mitochondrial ribosomes consist of a small (37S)
CC and a large (54S) subunit. The 37S small subunit contains a 15S
CC ribosomal RNA (15S mt-rRNA) and 34 different proteins. The 54S large
CC subunit contains a 21S rRNA (21S mt-rRNA) and 46 different proteins.
CC {ECO:0000269|PubMed:11278769, ECO:0000269|PubMed:12392552,
CC ECO:0000269|PubMed:28154081}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:9528754}.
CC Note=Mitoribosomes are tethered to the mitochondrial inner membrane and
CC spatially aligned with the membrane insertion machinery through two
CC distinct membrane contact sites, formed by the 21S rRNA expansion
CC segment 96-ES1 and the inner membrane protein MBA1.
CC {ECO:0000269|PubMed:25609543}.
CC -!- MISCELLANEOUS: Present with 656 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family.
CC {ECO:0000305}.
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DR EMBL; U43503; AAB68244.1; -; Genomic_DNA.
DR EMBL; AY692937; AAT92956.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11316.1; -; Genomic_DNA.
DR PIR; S62004; S62004.
DR RefSeq; NP_015207.1; NM_001183932.1.
DR PDB; 5MRC; EM; 3.25 A; AA=1-344.
DR PDB; 5MRE; EM; 3.75 A; AA=1-344.
DR PDB; 5MRF; EM; 4.97 A; AA=1-344.
DR PDBsum; 5MRC; -.
DR PDBsum; 5MRE; -.
DR PDBsum; 5MRF; -.
DR AlphaFoldDB; Q02950; -.
DR SMR; Q02950; -.
DR BioGRID; 36063; 80.
DR ComplexPortal; CPX-1603; 37S mitochondrial small ribosomal subunit.
DR DIP; DIP-4002N; -.
DR IntAct; Q02950; 9.
DR MINT; Q02950; -.
DR STRING; 4932.YPL118W; -.
DR iPTMnet; Q02950; -.
DR MaxQB; Q02950; -.
DR PaxDb; Q02950; -.
DR PRIDE; Q02950; -.
DR EnsemblFungi; YPL118W_mRNA; YPL118W; YPL118W.
DR GeneID; 855985; -.
DR KEGG; sce:YPL118W; -.
DR SGD; S000006039; MRP51.
DR VEuPathDB; FungiDB:YPL118W; -.
DR eggNOG; ENOG502R4KN; Eukaryota.
DR HOGENOM; CLU_063080_0_0_1; -.
DR InParanoid; Q02950; -.
DR OMA; THQIIET; -.
DR BioCyc; YEAST:G3O-34017-MON; -.
DR PRO; PR:Q02950; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q02950; protein.
DR GO; GO:0005743; C:mitochondrial inner membrane; IC:ComplexPortal.
DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR GO; GO:0032543; P:mitochondrial translation; IMP:SGD.
DR GO; GO:0070124; P:mitochondrial translational initiation; IGI:SGD.
DR InterPro; IPR016712; Mt_Rbsml_MRP51_fun.
DR PANTHER; PTHR28058; PTHR28058; 1.
DR Pfam; PF11709; Mit_ribos_Mrp51; 1.
DR PIRSF; PIRSF018156; MRPL51_fungal; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..344
FT /note="37S ribosomal protein MRP51, mitochondrial"
FT /id="PRO_0000087701"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 235
FT /note="V->A: Suppresses defects in the 5'UTLs of COX2 and
FT COX3 mitochondrial mRNAs."
FT /evidence="ECO:0000269|PubMed:9528754"
FT MUTAGEN 241
FT /note="N->H: Suppresses defects in the 5'UTLs of COX2 and
FT COX3 mitochondrial mRNAs."
FT /evidence="ECO:0000269|PubMed:9528754"
FT MUTAGEN 260
FT /note="P->L: Suppresses defects in the 5'UTLs of COX2 and
FT COX3 mitochondrial mRNAs."
FT /evidence="ECO:0000269|PubMed:9528754"
FT MUTAGEN 261
FT /note="P->R: Suppresses defects in the 5'UTLs of COX2 and
FT COX3 mitochondrial mRNAs."
FT /evidence="ECO:0000269|PubMed:9528754"
FT MUTAGEN 279
FT /note="E->R: Suppresses defects in the 5'UTLs of COX2 and
FT COX3 mitochondrial mRNAs."
FT /evidence="ECO:0000269|PubMed:9528754"
SQ SEQUENCE 344 AA; 39445 MW; E036C2D92F4FE8AA CRC64;
MTLAELLGRS RIAQVANNHK PLTYTGKKFH PTHQIIETKP STLYRQEWGL KSAIPSKIKS
RYLVYNDLDT LERITTFEPR GGTQWNRLRF QEMGVPIVSN IGRQNPFFKY ISRPEDESHA
KLSLFKEMKG DTDISPAAMK KRLKKITALI RSFQDEFKEW LVENHPDELK LNSNKLEDYV
VKFLNKKLET KTNKKFNTEI IGTGGLSYSL PGKLKNSPNG VIQRTVVPGR ILNVVKENND
NKWLAAIGGF VADVVFFQSP PSSFNSMGDF IRMKTFLFEI LEASMEKNGS VSMHARLLEP
QNDKTREFFN KRPIYKPLTS RRARRPSVGN IQEANNLLNI IKGN
