ID   RM50_YEAST              Reviewed;         139 AA.
AC   P53724; D6W1J7;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   04-NOV-2026, entry version 155.
DE   RecName: Full=Large ribosomal subunit protein bL9m {ECO:0000303|PubMed:24675956};
DE   AltName: Full=54S ribosomal protein L50, mitochondrial;
GN   Name=MRPL50; OrderedLocusNames=YNR022C; ORFNames=N3220;
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; DOI=10.1038/387s093;
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   IDENTIFICATION IN THE MITOCHONDRIAL RIBOSOMAL LARGE 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   [4]
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   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=16823961; DOI=10.1021/pr050477f;
RA   Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT   "Toward the complete yeast mitochondrial proteome: multidimensional
RT   separation techniques for mitochondrial proteomics.";
RL   J. Proteome Res. 5:1543-1554(2006).
RN   [6]
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   [7]
RP   STRUCTURE BY ELECTRON MICROSCOPY, AND SUBUNIT.
RX   PubMed=24675956; DOI=10.1126/science.1249410;
RA   Amunts A., Brown A., Bai X.C., Llacer J.L., Hussain T., Emsley P., Long F.,
RA   Murshudov G., Scheres S.H., Ramakrishnan V.;
RT   "Structure of the yeast mitochondrial large ribosomal subunit.";
RL   Science 343:1485-1489(2014).
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. {ECO:0000305|PubMed:24675956,
CC       ECO:0000305|PubMed:25609543}.
CC   -!- SUBUNIT: Component of the mitochondrial large ribosomal subunit (mt-
CC       LSU). 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:12392552, ECO:0000269|PubMed:24675956}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:16823961}. Note=Mitoribosomes are tethered to the
CC       mitochondrial inner membrane and spatially aligned with the membrane
CC       insertion machinery through two distinct membrane contact sites, formed
CC       by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein
CC       MBA1. {ECO:0000269|PubMed:25609543}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL9 family.
CC       {ECO:0000305}.
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DR   EMBL; Z71637; CAA96301.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10563.1; -; Genomic_DNA.
DR   PIR; S63353; S63353.
DR   RefSeq; NP_014419.1; NM_001183199.1.
DR   PDB; 3J6B; EM; 3.20 A; G=1-139.
DR   PDB; 5MRC; EM; 3.25 A; G=10-83.
DR   PDB; 5MRE; EM; 3.75 A; G=10-83.
DR   PDB; 5MRF; EM; 4.97 A; G=10-83.
DR   PDB; 8UX4; EM; 3.30 A; G=10-83.
DR   PDB; 8UXA; EM; 3.20 A; G=10-83.
DR   PDB; 9HLZ; EM; 3.20 A; GG=1-139.
DR   PDB; 9HM0; EM; 3.00 A; GG=1-139.
DR   AlphaFoldDB; P53724; -.
DR   EMDB; EMD-3551; -.
DR   EMDB; EMD-3552; -.
DR   EMDB; EMD-3553; -.
DR   EMDB; EMD-42687; -.
DR   EMDB; EMD-42720; -.
DR   EMDB; EMD-52283; -.
DR   MDposit; P53724; -.
DR   SMR; P53724; -.
DR   BioGRID; 35847; 182.
DR   ComplexPortal; CPX-1602; 54S mitochondrial large ribosomal subunit.
DR   DIP; DIP-1265N; -.
DR   FunCoup; P53724; 163.
DR   IntAct; P53724; 67.
DR   STRING; 4932.YNR022C; -.
DR   PaxDb; 4932-YNR022C; -.
DR   PeptideAtlas; P53724; -.
DR   EnsemblFungi; YNR022C_mRNA; YNR022C; YNR022C.
DR   GeneID; 855756; -.
DR   KEGG; sce:YNR022C; -.
DR   AGR; SGD:S000005305; -.
DR   SGD; S000005305; MRPL50.
DR   VEuPathDB; FungiDB:YNR022C; -.
DR   eggNOG; ENOG502S54F; Eukaryota.
DR   HOGENOM; CLU_1846247_0_0_1; -.
DR   InParanoid; P53724; -.
DR   OMA; ARYILHE; -.
DR   OrthoDB; 5555409at2759; -.
DR   BioCyc; YEAST:G3O-33336-MONOMER; -.
DR   BioGRID-ORCS; 855756; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P53724; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P53724; protein.
DR   GO; GO:0005743; C:mitochondrial inner membrane; NAS:ComplexPortal.
DR   GO; GO:0005762; C:mitochondrial large 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; IBA:GO_Central.
DR   Gene3D; 3.40.5.10; Ribosomal protein L9, N-terminal domain; 1.
DR   InterPro; IPR000244; Ribosomal_bL9.
DR   InterPro; IPR036935; Ribosomal_bL9_N_sf.
DR   PANTHER; PTHR21368; 50S RIBOSOMAL PROTEIN L9; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein.
FT   CHAIN           1..139
FT                   /note="Large ribosomal subunit protein bL9m"
FT                   /id="PRO_0000030584"
FT   REGION          83..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..121
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           11..16
FT                   /evidence="ECO:0007829|PDB:9HM0"
FT   STRAND          19..25
FT                   /evidence="ECO:0007829|PDB:9HM0"
FT   HELIX           28..30
FT                   /evidence="ECO:0007829|PDB:9HM0"
FT   STRAND          37..40
FT                   /evidence="ECO:0007829|PDB:9HM0"
FT   HELIX           45..49
FT                   /evidence="ECO:0007829|PDB:9HM0"
FT   HELIX           51..53
FT                   /evidence="ECO:0007829|PDB:9HM0"
FT   STRAND          54..57
FT                   /evidence="ECO:0007829|PDB:9HM0"
FT   HELIX           61..64
FT                   /evidence="ECO:0007829|PDB:9HM0"
FT   HELIX           67..87
FT                   /evidence="ECO:0007829|PDB:9HM0"
SQ   SEQUENCE   139 AA;  16283 MW;  9B03AA8C283063E9 CRC64;
     MLHCTQVCLS ALTKRTHRVK VQVLKDFPRF QLYKGQVANV KPSLMRNYLH NFNGAKYILS
     EEHDINTELL KQYQTLEAKL EEDHQQLSKR HETEVQKNME LRKESVFGHK KEEKPKEEKK
     GLLDSGITIE EVKIPGLDI
//