RM13_YEAST
ID RM13_YEAST Reviewed; 264 AA.
AC Q02204; D6VX72;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=54S ribosomal protein L13, mitochondrial;
DE AltName: Full=Mitochondrial large ribosomal subunit protein mL50 {ECO:0000303|PubMed:24675956};
DE AltName: Full=YmL13;
DE Flags: Precursor;
GN Name=MRPL13; OrderedLocusNames=YKR006C; ORFNames=YK105;
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].
RC STRAIN=07173;
RX PubMed=7954901; DOI=10.1007/bf00326298;
RA Grohmann L., Kitakawa M., Isono K., Goldschmidt-Reisin S., Graack H.-R.;
RT "The yeast nuclear gene MRP-L13 codes for a protein of the large subunit of
RT the mitochondrial ribosome.";
RL Curr. Genet. 26:8-14(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1441752; DOI=10.1002/yea.320080908;
RA Duesterhoeft A., Philippsen P.;
RT "DNA sequencing and analysis of a 24.7 kb segment encompassing centromere
RT CEN11 of Saccharomyces cerevisiae reveals nine previously unknown open
RT reading frames.";
RL Yeast 8:749-759(1992).
RN [3]
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 [4]
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 [5]
RP PROTEIN SEQUENCE OF 76-109, 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 [6]
RP TRANSPORT INTO MITOCHONDRIA.
RX PubMed=8220240;
RA Matsushita Y., Isono K.;
RT "Transport of mitoribosomal proteins, YmL13 and MRP7, into isolated
RT mitochondria of Saccharomyces cerevisiae.";
RL Biochem. Mol. Biol. Int. 30:911-919(1993).
RN [7]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [8]
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 [9]
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 [10]
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 [11]
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 [12]
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 -!- 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 1350 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC mL50 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA46246.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA52022.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA82076.1; Type=Erroneous initiation; Evidence={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; X73673; CAA52022.1; ALT_INIT; Genomic_DNA.
DR EMBL; X65124; CAA46246.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z28231; CAA82076.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006944; DAA09162.1; -; Genomic_DNA.
DR PIR; S25816; S25816.
DR RefSeq; NP_012931.4; NM_001179796.3.
DR PDB; 3J6B; EM; 3.20 A; 8=1-264.
DR PDB; 5MRC; EM; 3.25 A; 8=1-264.
DR PDB; 5MRE; EM; 3.75 A; 8=1-264.
DR PDB; 5MRF; EM; 4.97 A; 8=1-264.
DR PDBsum; 3J6B; -.
DR PDBsum; 5MRC; -.
DR PDBsum; 5MRE; -.
DR PDBsum; 5MRF; -.
DR AlphaFoldDB; Q02204; -.
DR SMR; Q02204; -.
DR BioGRID; 34138; 92.
DR ComplexPortal; CPX-1602; 54S mitochondrial large ribosomal subunit.
DR DIP; DIP-2092N; -.
DR IntAct; Q02204; 8.
DR MINT; Q02204; -.
DR STRING; 4932.YKR006C; -.
DR MaxQB; Q02204; -.
DR PaxDb; Q02204; -.
DR PRIDE; Q02204; -.
DR EnsemblFungi; YKR006C_mRNA; YKR006C; YKR006C.
DR GeneID; 853875; -.
DR KEGG; sce:YKR006C; -.
DR SGD; S000001714; MRPL13.
DR VEuPathDB; FungiDB:YKR006C; -.
DR eggNOG; ENOG502S1NZ; Eukaryota.
DR HOGENOM; CLU_103468_0_0_1; -.
DR InParanoid; Q02204; -.
DR OMA; FQFTKFL; -.
DR BioCyc; YEAST:G3O-31984-MON; -.
DR PRO; PR:Q02204; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; Q02204; 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 Gene3D; 1.10.1200.10; -; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR018305; Ribosomal_L50_mt.
DR Pfam; PF10501; Ribosomal_L50; 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..75
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:2060626,
FT ECO:0000269|PubMed:7954901"
FT CHAIN 76..264
FT /note="54S ribosomal protein L13, mitochondrial"
FT /id="PRO_0000030571"
FT CONFLICT 108
FT /note="A -> S (in Ref. 2; CAA52022)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 264 AA; 30271 MW; 6418F9BD92910DDA CRC64;
MSSLLKLHCI RPLPQRSVWL SGYKQKARCI HSSAANGDFM SWFKRKKQEE HQEPVKDTKQ
LIKDIEEGTN EASSQSSSNN KNRLELIPEN FIGEGSRRCK RQKELKLAVS SAPFNQWLSR
DKITSDNQLD DMILQATEKT LGKVDQDVQF SDLVAKFQFT KFLQSKSGYL IPDYELTTLS
TPLQFKRYIK EKILPSANDP KLAYKEAEPN AIHPFSDNYA SPNIYVVNDV TSKEQKSKYD
TIMKEIQKLE DDATRKALET ARSA