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RM32_YEAST
ID   RM32_YEAST              Reviewed;         183 AA.
AC   P25348; D6VR13;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 171.
DE   RecName: Full=54S ribosomal protein L32, mitochondrial;
DE   AltName: Full=Mitochondrial large ribosomal subunit protein bL32m {ECO:0000303|PubMed:24675956};
DE   AltName: Full=YmL32;
DE   Flags: Precursor;
GN   Name=MRPL32; OrderedLocusNames=YCR003W; ORFNames=YCR041, YCR3W;
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=1872033; DOI=10.1002/yea.320070412;
RA   Steensma H.Y., van der Aart Q.J.M.;
RT   "Sequence of the CDC10 region at chromosome III of Saccharomyces
RT   cerevisiae.";
RL   Yeast 7:425-429(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1580102; DOI=10.1002/yea.320080107;
RA   Biteau N., Fremaux C., Hebrard S., Menara A., Aigle M., Crouzet M.;
RT   "The complete sequence of a 10.8kb fragment to the right of the chromosome
RT   III centromere of Saccharomyces cerevisiae.";
RL   Yeast 8:61-70(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=1574125; DOI=10.1038/357038a0;
RA   Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA   Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA   Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA   Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA   Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA   Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA   Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA   Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA   Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA   Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA   Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA   Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA   Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA   Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA   Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA   Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA   Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA   Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA   Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA   Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA   Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA   Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA   Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA   Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA   Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA   Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA   Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA   Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA   Sgouros J.G.;
RT   "The complete DNA sequence of yeast chromosome III.";
RL   Nature 357:38-46(1992).
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 72-106, 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   [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       bL32m has a zinc binding site. {ECO:0000269|PubMed:2060626,
CC       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 1700 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL32 family.
CC       {ECO:0000305}.
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DR   EMBL; S48552; AAD13857.1; -; Genomic_DNA.
DR   EMBL; Z11113; CAA77444.1; -; Genomic_DNA.
DR   EMBL; X59720; CAA42340.1; -; Genomic_DNA.
DR   EMBL; AY693214; AAT93233.1; -; Genomic_DNA.
DR   EMBL; BK006937; DAA07482.1; -; Genomic_DNA.
DR   PIR; S22265; R5BY32.
DR   RefSeq; NP_009929.1; NM_001178716.1.
DR   PDB; 3J6B; EM; 3.20 A; W=1-183.
DR   PDB; 5MRC; EM; 3.25 A; W=72-183.
DR   PDB; 5MRE; EM; 3.75 A; W=72-183.
DR   PDB; 5MRF; EM; 4.97 A; W=72-183.
DR   PDBsum; 3J6B; -.
DR   PDBsum; 5MRC; -.
DR   PDBsum; 5MRE; -.
DR   PDBsum; 5MRF; -.
DR   AlphaFoldDB; P25348; -.
DR   SMR; P25348; -.
DR   BioGRID; 30981; 184.
DR   ComplexPortal; CPX-1602; 54S mitochondrial large ribosomal subunit.
DR   DIP; DIP-4987N; -.
DR   IntAct; P25348; 4.
DR   MINT; P25348; -.
DR   STRING; 4932.YCR003W; -.
DR   MaxQB; P25348; -.
DR   PaxDb; P25348; -.
DR   PRIDE; P25348; -.
DR   EnsemblFungi; YCR003W_mRNA; YCR003W; YCR003W.
DR   GeneID; 850359; -.
DR   KEGG; sce:YCR003W; -.
DR   SGD; S000000596; MRPL32.
DR   VEuPathDB; FungiDB:YCR003W; -.
DR   eggNOG; KOG4080; Eukaryota.
DR   GeneTree; ENSGT00390000014996; -.
DR   HOGENOM; CLU_095763_1_0_1; -.
DR   InParanoid; P25348; -.
DR   OMA; IRHIWKT; -.
DR   BioCyc; YEAST:G3O-29322-MON; -.
DR   PRO; PR:P25348; -.
DR   Proteomes; UP000002311; Chromosome III.
DR   RNAct; P25348; protein.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
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   InterPro; IPR002677; Ribosomal_L32p.
DR   InterPro; IPR011332; Ribosomal_zn-bd.
DR   Pfam; PF01783; Ribosomal_L32p; 1.
DR   SUPFAM; SSF57829; SSF57829; 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..71
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:2060626"
FT   CHAIN           72..183
FT                   /note="54S ribosomal protein L32, mitochondrial"
FT                   /id="PRO_0000030518"
SQ   SEQUENCE   183 AA;  21437 MW;  C0F0D87C23AA2DEA CRC64;
     MNSLIFGKQL AFHKIVPTTA IGWLVPLGNP SLQIPGQKQL GSIHRWLREK LQQDHKDTED
     KDFFSNNGIL LAVPKKKVSH QKKRQKLYGP GKKQLKMIHH LNKCPSCGHY KRANTLCMYC
     VGQISHIWKT HTAKEEIKPR QEEELSELDQ RVLYPGRRDT KYTKDLKDKD NYLERRVRTL
     KKD
 
 
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