RM40_YEAST
ID RM40_YEAST Reviewed; 297 AA.
AC P36534; D6W3J5; Q6B277;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=54S ribosomal protein L40, mitochondrial;
DE AltName: Full=Mitochondrial large ribosomal subunit protein uL24m {ECO:0000303|PubMed:24675956};
DE AltName: Full=YmL40;
GN Name=MRPL40; OrderedLocusNames=YPL173W;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP PROTEIN SEQUENCE OF 109-129 AND 146-158, 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 [5]
RP PROTEIN SEQUENCE OF 176-215 AND 287-293.
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 [6]
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 [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 ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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 uL24m forms the wall of the exit tunnel. {ECO:0000269|PubMed:12392552,
CC ECO:0000269|PubMed:2060626, ECO:0000269|PubMed:24675956}.
CC -!- INTERACTION:
CC P36534; P32387: MRP20; NbExp=4; IntAct=EBI-15595, EBI-15599;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14576278}.
CC Note=Mitoribosomes are tethered to the mitochondrial inner membrane and
CC spatially aligned with the membrane insertion machinery through two
CC distinct membrane contact sites, formed by the 21S rRNA expansion
CC segment 96-ES1 and the inner membrane protein MBA1.
CC {ECO:0000269|PubMed:25609543}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL24 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; Z73529; CAA97880.1; -; Genomic_DNA.
DR EMBL; AY692853; AAT92872.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11261.1; -; Genomic_DNA.
DR PIR; S65185; S65185.
DR RefSeq; NP_015152.1; NM_001183987.1.
DR PDB; 3J6B; EM; 3.20 A; Q=1-297.
DR PDB; 5MRC; EM; 3.25 A; Q=2-297.
DR PDB; 5MRE; EM; 3.75 A; Q=2-297.
DR PDB; 5MRF; EM; 4.97 A; Q=2-297.
DR PDBsum; 3J6B; -.
DR PDBsum; 5MRC; -.
DR PDBsum; 5MRE; -.
DR PDBsum; 5MRF; -.
DR AlphaFoldDB; P36534; -.
DR SMR; P36534; -.
DR BioGRID; 36010; 118.
DR ComplexPortal; CPX-1602; 54S mitochondrial large ribosomal subunit.
DR DIP; DIP-7947N; -.
DR IntAct; P36534; 11.
DR MINT; P36534; -.
DR STRING; 4932.YPL173W; -.
DR iPTMnet; P36534; -.
DR MaxQB; P36534; -.
DR PaxDb; P36534; -.
DR PRIDE; P36534; -.
DR TopDownProteomics; P36534; -.
DR EnsemblFungi; YPL173W_mRNA; YPL173W; YPL173W.
DR GeneID; 855930; -.
DR KEGG; sce:YPL173W; -.
DR SGD; S000006094; MRPL40.
DR VEuPathDB; FungiDB:YPL173W; -.
DR eggNOG; ENOG502QUDZ; Eukaryota.
DR HOGENOM; CLU_046293_0_0_1; -.
DR InParanoid; P36534; -.
DR OMA; NPYSKHK; -.
DR BioCyc; YEAST:G3O-34068-MON; -.
DR PRO; PR:P36534; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P36534; 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 GO; GO:0006412; P:translation; IBA:GO_Central.
DR Gene3D; 2.30.30.30; -; 1.
DR InterPro; IPR005824; KOW.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR003256; Ribosomal_L24.
DR InterPro; IPR005825; Ribosomal_L24/26_CS.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR12903; PTHR12903; 1.
DR SMART; SM00739; KOW; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR PROSITE; PS01108; RIBOSOMAL_L24; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Mitochondrion;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..297
FT /note="54S ribosomal protein L40, mitochondrial"
FT /id="PRO_0000030582"
FT DOMAIN 63..96
FT /note="KOW"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CONFLICT 179
FT /note="D -> G (in Ref. 3; AAT92872)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 297 AA; 33751 MW; D5BB2B7AE13ECBF9 CRC64;
MSGSYQHLSN VGSRVMKRLG NRPKNFLPHS EKFIKKSTPE FMKSDLKEVD EKTSFKSEKE
WKFIPGDRVV VMSGASKGNI AVIKSFDKRT NSFILDENGP TKTVPVPKQF WLEGQTSHMI
TIPVSILGKD LRLVADIDDE KTPGKTRTVA VRDVSFNGSY YDADYKKVMP YRCVKGQPDL
IIPWPKPDPI DVQTNLATDP VIAREQTFWV DSVVRNPIPK KAIPSIRNPH SKYKRGTLTA
KDIAKLVAPE MPLTEVRKSH LAEKKELAER EVPKLTEEDM EAIGARVFEF LEKQKRE
