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RM09_YEAST
ID   RM09_YEAST              Reviewed;         269 AA.
AC   P31334; D6VV02;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 3.
DT   03-AUG-2022, entry version 175.
DE   RecName: Full=54S ribosomal protein L9, mitochondrial;
DE   AltName: Full=Mitochondrial large ribosomal subunit protein uL3m {ECO:0000303|PubMed:24675956};
DE   AltName: Full=YmL9;
DE   Flags: Precursor;
GN   Name=MRPL9; OrderedLocusNames=YGR220C; ORFNames=G8520;
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], AND PROTEIN SEQUENCE OF 20-53; 176-182
RP   AND 257-261.
RC   STRAIN=07173;
RX   PubMed=1597181; DOI=10.1111/j.1432-1033.1992.tb16937.x;
RA   Graack H.-R., Grohmann L., Kitakawa M., Schaefer K.L., Kruft V.;
RT   "YmL9, a nucleus-encoded mitochondrial ribosomal protein of yeast, is
RT   homologous to L3 ribosomal proteins from all natural kingdoms and
RT   photosynthetic organelles.";
RL   Eur. J. Biochem. 206:373-380(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8701610;
RX   DOI=10.1002/(sici)1097-0061(19960330)12:4<385::aid-yea910>3.0.co;2-g;
RA   van der Aart Q.J.M., Kleine K., Steensma H.Y.;
RT   "Sequence analysis of the 43 kb CRM1-YLM9-PET54-DIE2-SMI1-PHO81-YHB4-PFK1
RT   region from the right arm of Saccharomyces cerevisiae chromosome VII.";
RL   Yeast 12:385-390(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
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   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   [6]
RP   PROTEIN SEQUENCE OF 20-53, AND SUBUNIT.
RC   STRAIN=07173;
RX   PubMed=3060376; DOI=10.1016/0014-5793(88)80975-x;
RA   Graack H.-R., Grohmann L., Choli T.;
RT   "Mitochondrial ribosomes of yeast: isolation of individual proteins and N-
RT   terminal sequencing.";
RL   FEBS Lett. 242:4-8(1988).
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       {ECO:0000269|PubMed:24675956, ECO:0000269|PubMed:3060376}.
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 uL3 family.
CC       {ECO:0000305}.
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DR   EMBL; X65014; CAA46148.1; -; Genomic_DNA.
DR   EMBL; X87941; CAA61168.1; -; Genomic_DNA.
DR   EMBL; Z73004; CAA97248.1; -; Genomic_DNA.
DR   EMBL; AY558274; AAS56600.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08313.1; -; Genomic_DNA.
DR   PIR; S23455; R5BYL3.
DR   RefSeq; NP_011736.1; NM_001181349.1.
DR   PDB; 3J6B; EM; 3.20 A; C=1-269.
DR   PDB; 5MRC; EM; 3.25 A; C=21-269.
DR   PDB; 5MRE; EM; 3.75 A; C=21-269.
DR   PDB; 5MRF; EM; 4.97 A; C=21-269.
DR   PDBsum; 3J6B; -.
DR   PDBsum; 5MRC; -.
DR   PDBsum; 5MRE; -.
DR   PDBsum; 5MRF; -.
DR   AlphaFoldDB; P31334; -.
DR   SMR; P31334; -.
DR   BioGRID; 33473; 149.
DR   ComplexPortal; CPX-1602; 54S mitochondrial large ribosomal subunit.
DR   DIP; DIP-6806N; -.
DR   IntAct; P31334; 47.
DR   MINT; P31334; -.
DR   STRING; 4932.YGR220C; -.
DR   MaxQB; P31334; -.
DR   PaxDb; P31334; -.
DR   PRIDE; P31334; -.
DR   EnsemblFungi; YGR220C_mRNA; YGR220C; YGR220C.
DR   GeneID; 853135; -.
DR   KEGG; sce:YGR220C; -.
DR   SGD; S000003452; MRPL9.
DR   VEuPathDB; FungiDB:YGR220C; -.
DR   eggNOG; KOG3141; Eukaryota.
DR   GeneTree; ENSGT00390000011422; -.
DR   HOGENOM; CLU_044142_4_1_1; -.
DR   InParanoid; P31334; -.
DR   OMA; KRMAGRY; -.
DR   BioCyc; YEAST:G3O-30901-MON; -.
DR   PRO; PR:P31334; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P31334; 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   HAMAP; MF_01325_B; Ribosomal_L3_B; 1.
DR   InterPro; IPR000597; Ribosomal_L3.
DR   InterPro; IPR019927; Ribosomal_L3_bac/org-type.
DR   InterPro; IPR019926; Ribosomal_L3_CS.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   PANTHER; PTHR11229; PTHR11229; 1.
DR   Pfam; PF00297; Ribosomal_L3; 1.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   TIGRFAMs; TIGR03625; L3_bact; 1.
DR   PROSITE; PS00474; RIBOSOMAL_L3; 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..19
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:1597181,
FT                   ECO:0000269|PubMed:3060376"
FT   CHAIN           20..269
FT                   /note="54S ribosomal protein L9, mitochondrial"
FT                   /id="PRO_0000030536"
FT   CONFLICT        21
FT                   /note="S -> V (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        139
FT                   /note="E -> Q (in Ref. 1; CAA46148)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   269 AA;  29790 MW;  A09A4DA5CE9337E5 CRC64;
     MSKFLQGSIF SISKLHVRYS STRPFLVAPS IANSITTEAP AINHSPELAN ARKWLPKRCG
     LITRKKGMMP YFDKSTGERS AATILEVNNV EVIMHRTSEV NGYFACQVGY GSRHLSKVSR
     QMLGHFASKV VNPKEHVAEF RVKDEKGLIP PGTLLKPSFF KEGQYVDVRS VSKGKGFTGV
     MKRYGFKGLR ASHGTSIMHR HGGSYGQNQD PGRVLPGRKM PGHMGNEHVT IQNVKVLKVD
     DENNVIWVKG SVAGPKNSFV KIQDAIKKT
 
 
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