ID RM19_YEAST Reviewed; 158 AA.
AC P53875; D6W102;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 27-MAR-2024, entry version 179.
DE RecName: Full=Large ribosomal subunit protein uL11m {ECO:0000303|PubMed:24675956};
DE AltName: Full=54S ribosomal protein L19, mitochondrial;
DE AltName: Full=YmL19;
DE Flags: Precursor;
GN Name=MRPL19; OrderedLocusNames=YNL185C; ORFNames=N1623;
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 74-83, 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 [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 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 [6]
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 [7]
RP NOMENCLATURE.
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).
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).
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) (PubMed:9151978). Mature yeast 74S mitochondrial ribosomes consist
CC of a small (37S) and a large (54S) subunit. The 37S small subunit
CC contains a 15S ribosomal RNA (15S mt-rRNA) and 34 different proteins.
CC The 54S large subunit contains a 21S rRNA (21S mt-rRNA) and 46
CC different proteins (PubMed:24675956). {ECO:0000269|PubMed:9151978,
CC ECO:0000305|PubMed:24675956}.
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 3200 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL11 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z71461; CAA96078.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10368.1; -; Genomic_DNA.
DR PIR; S63140; S63140.
DR RefSeq; NP_014214.1; NM_001183023.1.
DR AlphaFoldDB; P53875; -.
DR SMR; P53875; -.
DR BioGRID; 35648; 211.
DR ComplexPortal; CPX-1602; 54S mitochondrial large ribosomal subunit.
DR DIP; DIP-6781N; -.
DR IntAct; P53875; 10.
DR MINT; P53875; -.
DR STRING; 4932.YNL185C; -.
DR MaxQB; P53875; -.
DR PaxDb; 4932-YNL185C; -.
DR PeptideAtlas; P53875; -.
DR EnsemblFungi; YNL185C_mRNA; YNL185C; YNL185C.
DR GeneID; 855536; -.
DR KEGG; sce:YNL185C; -.
DR AGR; SGD:S000005129; -.
DR SGD; S000005129; MRPL19.
DR VEuPathDB; FungiDB:YNL185C; -.
DR eggNOG; KOG3257; Eukaryota.
DR GeneTree; ENSGT00390000003153; -.
DR HOGENOM; CLU_074237_1_0_1; -.
DR InParanoid; P53875; -.
DR OMA; CKQFNAK; -.
DR OrthoDB; 166522at2759; -.
DR BioCyc; YEAST:G3O-33196-MONOMER; -.
DR BioGRID-ORCS; 855536; 3 hits in 10 CRISPR screens.
DR PRO; PR:P53875; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53875; 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:0070180; F:large ribosomal subunit rRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR GO; GO:0032543; P:mitochondrial translation; NAS:ComplexPortal.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR CDD; cd00349; Ribosomal_L11; 1.
DR Gene3D; 1.10.10.250; Ribosomal protein L11, C-terminal domain; 1.
DR Gene3D; 3.30.1550.10; Ribosomal protein L11/L12, N-terminal domain; 1.
DR HAMAP; MF_00736; Ribosomal_uL11; 1.
DR InterPro; IPR000911; Ribosomal_uL11.
DR InterPro; IPR006519; Ribosomal_uL11_bac-typ.
DR InterPro; IPR020783; Ribosomal_uL11_C.
DR InterPro; IPR036769; Ribosomal_uL11_C_sf.
DR InterPro; IPR020784; Ribosomal_uL11_N.
DR InterPro; IPR036796; Ribosomal_uL11_N_sf.
DR NCBIfam; TIGR01632; L11_bact; 1.
DR PANTHER; PTHR11661:SF1; 39S RIBOSOMAL PROTEIN L11, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11661; 60S RIBOSOMAL PROTEIN L12; 1.
DR Pfam; PF00298; Ribosomal_L11; 1.
DR Pfam; PF03946; Ribosomal_L11_N; 1.
DR SMART; SM00649; RL11; 1.
DR SUPFAM; SSF54747; Ribosomal L11/L12e N-terminal domain; 1.
DR SUPFAM; SSF46906; Ribosomal protein L11, C-terminal domain; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Mitochondrion; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT TRANSIT 1..73
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:9151978"
FT CHAIN 74..158
FT /note="Large ribosomal subunit protein uL11m"
FT /id="PRO_0000030447"
SQ SEQUENCE 158 AA; 16670 MW; A47715F1FC547685 CRC64;
MSQAAKNVIV KLIVGAGQAA PSPPVGPALG SKGIKAIDFC KEFNARSANY QPGVPVPVLI
TIKPDRTFTF EMKSPPTGYL LLKALKMDKG HGQPNVGTML GSAPAKGPTR ALGELSLKHV
YEIAKIKKSD ERHSLLEMEG IVKSIVGVAK SMGIKVVP
//
