RM41_YEAST
ID RM41_YEAST Reviewed; 263 AA.
AC P32387; D6VT37;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=54S ribosomal protein L41, mitochondrial;
DE AltName: Full=Mitochondrial large ribosomal subunit protein uL23m {ECO:0000303|PubMed:24675956};
DE AltName: Full=YmL41;
DE Flags: Precursor;
GN Name=MRP20; Synonyms=MRPL41; OrderedLocusNames=YDR405W; ORFNames=D9509.23;
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].
RX PubMed=1544898; DOI=10.1016/s0021-9258(18)42745-7;
RA Fearon K., Mason T.L.;
RT "Structure and function of MRP20 and MRP49, the nuclear genes for two
RT proteins of the 54 S subunit of the yeast mitochondrial ribosome.";
RL J. Biol. Chem. 267:5162-5170(1992).
RN [2]
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 [3]
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 [4]
RP PROTEIN SEQUENCE OF 46-58, 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 142-156 AND 252-263, 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 [6]
RP INTERACTION WITH OXA1.
RX PubMed=14657017; DOI=10.1093/emboj/cdg624;
RA Jia L., Dienhart M., Schramp M., McCauley M., Hell K., Stuart R.A.;
RT "Yeast Oxa1 interacts with mitochondrial ribosomes: the importance of the
RT C-terminal region of Oxa1.";
RL EMBO J. 22:6438-6447(2003).
RN [7]
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 [8]
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 [9]
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 [10]
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 [11]
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 uL23m forms the wall of the exit tunnel (PubMed:2060626,
CC PubMed:9151978, PubMed:24675956). Interacts with the C-terminus of OXA1
CC (PubMed:14657017). {ECO:0000269|PubMed:14657017,
CC ECO:0000269|PubMed:2060626, ECO:0000269|PubMed:24675956,
CC ECO:0000269|PubMed:9151978}.
CC -!- INTERACTION:
CC P32387; P36534: MRPL40; NbExp=4; IntAct=EBI-15599, EBI-15595;
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 2200 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL23 family.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-11 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA34790.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M81696; AAA34789.1; -; Genomic_DNA.
DR EMBL; M81696; AAA34790.1; ALT_INIT; Genomic_DNA.
DR EMBL; U32274; AAB64845.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12247.1; -; Genomic_DNA.
DR PIR; B42105; B42105.
DR RefSeq; NP_010693.3; NM_001180713.3.
DR PDB; 3J6B; EM; 3.20 A; P=1-263.
DR PDB; 5MRC; EM; 3.25 A; P=55-261.
DR PDB; 5MRE; EM; 3.75 A; P=55-261.
DR PDB; 5MRF; EM; 4.97 A; P=55-261.
DR PDBsum; 3J6B; -.
DR PDBsum; 5MRC; -.
DR PDBsum; 5MRE; -.
DR PDBsum; 5MRF; -.
DR AlphaFoldDB; P32387; -.
DR SMR; P32387; -.
DR BioGRID; 32465; 234.
DR ComplexPortal; CPX-1602; 54S mitochondrial large ribosomal subunit.
DR DIP; DIP-6703N; -.
DR IntAct; P32387; 11.
DR MINT; P32387; -.
DR STRING; 4932.YDR405W; -.
DR iPTMnet; P32387; -.
DR MaxQB; P32387; -.
DR PaxDb; P32387; -.
DR PRIDE; P32387; -.
DR EnsemblFungi; YDR405W_mRNA; YDR405W; YDR405W.
DR GeneID; 852014; -.
DR KEGG; sce:YDR405W; -.
DR SGD; S000002813; MRP20.
DR VEuPathDB; FungiDB:YDR405W; -.
DR eggNOG; KOG4089; Eukaryota.
DR GeneTree; ENSGT00390000007739; -.
DR HOGENOM; CLU_084850_0_0_1; -.
DR InParanoid; P32387; -.
DR OMA; LYFPKAR; -.
DR BioCyc; YEAST:G3O-29949-MON; -.
DR PRO; PR:P32387; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P32387; 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; IMP:SGD.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR012678; Ribosomal_L23/L15e_core_dom_sf.
DR InterPro; IPR013025; Ribosomal_L25/23.
DR PANTHER; PTHR12059; PTHR12059; 1.
DR Pfam; PF00276; Ribosomal_L23; 1.
DR SUPFAM; SSF54189; SSF54189; 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..45
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:2060626"
FT CHAIN 46..263
FT /note="54S ribosomal protein L41, mitochondrial"
FT /id="PRO_0000030488"
FT CONFLICT 52
FT /note="R -> Q (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="P -> Y (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="I -> K (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="I -> K (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 263 AA; 30566 MW; B8B1E51BAC60C673 CRC64;
MPRLTVGTKN MLYPLQKTLA VGSCKPEQVP IRSLASVVES SSKILDKSGS DREVDINVSE
KIYKWTKAGI EQGKEHFKVG GNKVYFPKAR IILLRPNAKH TPYQAKFIVP KSFNKLDLRD
YLYHIYGLRA MNITTQLLHG KFNRMNLQTT RFREPQIKKM TIEMEEPFIW PEEPRPDENS
FWDSTTPDNM EKYREERLNC LGSDANKPGT AFDGVVGPYE RVAQPFIPRF LKREIDNKRE
RHAAELQRAD KLIALNRYIE DLH
