ID   RM35_YEAST              Reviewed;         367 AA.
AC   Q06678; D6VSV4;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 171.
DE   RecName: Full=Large ribosomal subunit protein mL38 {ECO:0000303|PubMed:24675956};
DE   AltName: Full=54S ribosomal protein L35, mitochondrial;
DE   AltName: Full=YmL35;
DE   Flags: Precursor;
GN   Name=MRPL35; OrderedLocusNames=YDR322W; ORFNames=D9798.5;
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=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(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 64-84; 130-140; 159-175 AND 289-295.
RX   PubMed=12426313; DOI=10.1074/jbc.m208287200;
RA   Dziembowski A., Piwowarski J., Hoser R., Minczuk M., Dmochowska A.,
RA   Siep M., van der Spek H., Grivell L.A., Stepien P.P.;
RT   "The yeast mitochondrial degradosome. Its composition, interplay between
RT   RNA helicase and RNase activities and the role in mitochondrial RNA
RT   metabolism.";
RL   J. Biol. Chem. 278:1603-1611(2003).
RN   [4]
RP   PROTEIN SEQUENCE OF 108-116, 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   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   [6]
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   [7]
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   [8]
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   [9]
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   [10]
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:12392552, 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 7700 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the phosphatidylethanolamine-binding protein
CC       family. Mitochondrion-specific ribosomal protein mL38 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; U32517; AAB64758.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA12164.1; -; Genomic_DNA.
DR   PIR; S59788; S59788.
DR   RefSeq; NP_010608.1; NM_001180630.1.
DR   PDB; 3J6B; EM; 3.20 A; 1=1-367.
DR   PDB; 5MRC; EM; 3.25 A; 1=20-367.
DR   PDB; 5MRE; EM; 3.75 A; 1=20-367.
DR   PDB; 5MRF; EM; 4.97 A; 1=20-367.
DR   PDBsum; 3J6B; -.
DR   PDBsum; 5MRC; -.
DR   PDBsum; 5MRE; -.
DR   PDBsum; 5MRF; -.
DR   AlphaFoldDB; Q06678; -.
DR   EMDB; EMD-3551; -.
DR   EMDB; EMD-3552; -.
DR   EMDB; EMD-3553; -.
DR   SMR; Q06678; -.
DR   BioGRID; 32379; 292.
DR   ComplexPortal; CPX-1602; 54S mitochondrial large ribosomal subunit.
DR   DIP; DIP-6832N; -.
DR   IntAct; Q06678; 14.
DR   MINT; Q06678; -.
DR   STRING; 4932.YDR322W; -.
DR   MaxQB; Q06678; -.
DR   PaxDb; 4932-YDR322W; -.
DR   PeptideAtlas; Q06678; -.
DR   EnsemblFungi; YDR322W_mRNA; YDR322W; YDR322W.
DR   GeneID; 851921; -.
DR   KEGG; sce:YDR322W; -.
DR   AGR; SGD:S000002730; -.
DR   SGD; S000002730; MRPL35.
DR   VEuPathDB; FungiDB:YDR322W; -.
DR   eggNOG; KOG3346; Eukaryota.
DR   HOGENOM; CLU_068504_0_0_1; -.
DR   InParanoid; Q06678; -.
DR   OMA; FRTQWDE; -.
DR   OrthoDB; 2724293at2759; -.
DR   BioCyc; YEAST:G3O-29879-MONOMER; -.
DR   BioGRID-ORCS; 851921; 3 hits in 10 CRISPR screens.
DR   PRO; PR:Q06678; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; Q06678; 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; NAS:ComplexPortal.
DR   CDD; cd00866; PEBP_euk; 1.
DR   Gene3D; 1.20.58.1180; -; 1.
DR   Gene3D; 3.90.280.10; PEBP-like; 1.
DR   InterPro; IPR008914; PEBP.
DR   InterPro; IPR036610; PEBP-like_sf.
DR   InterPro; IPR035810; PEBP_euk.
DR   PANTHER; PTHR11362:SF133; 39S RIBOSOMAL PROTEIN L38, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11362; PHOSPHATIDYLETHANOLAMINE-BINDING PROTEIN; 1.
DR   Pfam; PF01161; PBP; 1.
DR   SUPFAM; SSF49777; PEBP-like; 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..29
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..367
FT                   /note="Large ribosomal subunit protein mL38"
FT                   /id="PRO_0000023284"
FT   CONFLICT        113
FT                   /note="P -> D (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   367 AA;  42825 MW;  C6A2C973121FF555 CRC64;
     MLRRSIHTTK ILQKPNATSH IWSDFTTRPS SLSIQSSKVK NYLFQKKASL DPPSISRRSN
     RIKYSPPEHI DEIFRMSYDF LEQRSSKFYE LANKTKNPLK KDALLIKAEI NNPEVQYNFQ
     FNNKLNNVKD IIDYDVPVYR HLGKQHWESY GQMLLMQRLE TLAAIPDTLP TLVPRAEVNI
     KFPFSTGVNK WIEPGEFLSS NVTSMRPIFK IQEYELVNVE KQLYTVLIVN PDVPDLSNDS
     FKTALCYGLV NINLTYNDNL IDPRKFHSSN IIADYLPPVP EKNAGKQRFV VWVFRQPLIE
     DKQGPNMLEI DRKELSRDDF DIRQFTKKYN LTAIGAHIWR SEWDAKVAAV REKYGLPPGR
     VFSRVRR
//