RM10_YEAST
ID RM10_YEAST Reviewed; 322 AA.
AC P36520; D6W0R0; P36524;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=54S ribosomal protein L10, mitochondrial;
DE AltName: Full=Mitochondrial large ribosomal subunit protein uL15m {ECO:0000303|PubMed:24675956};
DE AltName: Full=YmL10/YmL18;
DE Flags: Precursor;
GN Name=MRPL10; Synonyms=MRPL18; OrderedLocusNames=YNL284C; ORFNames=N0580;
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 PROTEIN SEQUENCE OF 58-71, AND SUBUNIT.
RC STRAIN=07173;
RX PubMed=2060626; DOI=10.1016/0014-5793(91)80759-v;
RA Grohmann L., Graack H.-R., Kruft V., Choli T., Goldschmidt-Reisin S.,
RA Kitakawa M.;
RT "Extended N-terminal sequencing of proteins of the large ribosomal subunit
RT from yeast mitochondria.";
RL FEBS Lett. 284:51-56(1991).
RN [4]
RP PROTEIN SEQUENCE OF 182-195 AND 247-253, AND SUBUNIT.
RC STRAIN=07173;
RX PubMed=9151978; DOI=10.1111/j.1432-1033.1997.t01-2-00449.x;
RA Kitakawa M., Graack H.-R., Grohmann L., Goldschmidt-Reisin S., Herfurth E.,
RA Wittmann-Liebold B., Nishimura T., Isono K.;
RT "Identification and characterization of the genes for mitochondrial
RT ribosomal proteins of Saccharomyces cerevisiae.";
RL Eur. J. Biochem. 245:449-456(1997).
RN [5]
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 [6]
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 [7]
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 [8]
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 [9]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS), 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:2060626, ECO:0000269|PubMed:24675956,
CC ECO:0000269|PubMed:9151978}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14576278}. 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 -!- MISCELLANEOUS: Present with 5350 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL15 family.
CC {ECO:0000305}.
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DR EMBL; Z71560; CAA96198.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10276.1; -; Genomic_DNA.
DR PIR; S63258; S63258.
DR RefSeq; NP_014115.1; NM_001183122.1.
DR PDB; 3J6B; EM; 3.20 A; J=1-322.
DR PDB; 5MRC; EM; 3.25 A; J=58-277.
DR PDB; 5MRE; EM; 3.75 A; J=58-277.
DR PDB; 5MRF; EM; 4.97 A; J=58-277.
DR PDBsum; 3J6B; -.
DR PDBsum; 5MRC; -.
DR PDBsum; 5MRE; -.
DR PDBsum; 5MRF; -.
DR AlphaFoldDB; P36520; -.
DR SMR; P36520; -.
DR BioGRID; 35556; 340.
DR ComplexPortal; CPX-1602; 54S mitochondrial large ribosomal subunit.
DR DIP; DIP-6771N; -.
DR IntAct; P36520; 38.
DR MINT; P36520; -.
DR STRING; 4932.YNL284C; -.
DR MaxQB; P36520; -.
DR PaxDb; P36520; -.
DR PRIDE; P36520; -.
DR EnsemblFungi; YNL284C_mRNA; YNL284C; YNL284C.
DR GeneID; 855436; -.
DR KEGG; sce:YNL284C; -.
DR SGD; S000005228; MRPL10.
DR VEuPathDB; FungiDB:YNL284C; -.
DR eggNOG; KOG0846; Eukaryota.
DR GeneTree; ENSGT00390000009040; -.
DR HOGENOM; CLU_055188_5_1_1; -.
DR InParanoid; P36520; -.
DR OMA; YTRHAIK; -.
DR BioCyc; YEAST:G3O-33275-MON; -.
DR PRO; PR:P36520; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P36520; protein.
DR GO; GO:0005743; C:mitochondrial inner membrane; IC: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; IC:SGD.
DR HAMAP; MF_01341; Ribosomal_L15; 1.
DR InterPro; IPR036227; L18e/L15P_sf.
DR InterPro; IPR030878; Ribosomal_L15.
DR InterPro; IPR005749; Ribosomal_L15_bac-type.
DR InterPro; IPR021131; Ribosomal_L18e/L15P.
DR PANTHER; PTHR12934; PTHR12934; 1.
DR Pfam; PF00828; Ribosomal_L27A; 1.
DR SUPFAM; SSF52080; SSF52080; 1.
DR TIGRFAMs; TIGR01071; rplO_bact; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Mitochondrion; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT TRANSIT 1..57
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:2060626"
FT CHAIN 58..322
FT /note="54S ribosomal protein L10, mitochondrial"
FT /id="PRO_0000030468"
FT REGION 69..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 68
FT /note="D -> K (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="T -> G (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="F -> I (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="I -> K (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 322 AA; 36347 MW; FD56AB98F62B4A07 CRC64;
MKAERQTGLR NSFTTVIGRK LINTFVPSMM LTSVAGNDIF FRGLFKSPVL AFQSYRYVSI
LGQLKPSDGS TKSFKRLGRG PSSGLGKTSG RGQKGQKARG KVKSWFEGGQ TPIYKLFPKI
GFTNVGAKPL KELNLKRIQW FHDKNRLHLQ PGEVLDMNKM RKLGLVTGPI KYGVKILASG
KFHYNLPIAL EASRASAKAI AAIEKAGGKF TARYYTPLGL RAHLNPQWFL EKRGRVPLQA
RPTKRRDIDF YSKEEKRGYL VMEKDKLLQD IKEAQNKGSR HFLKQNVKKS SLEIELEELS
PEKDWVPVVS NSKVMNIKAL DH
