RM03_YEAST
ID RM03_YEAST Reviewed; 390 AA.
AC P36516; D6VZJ8;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=54S ribosomal protein L3, mitochondrial;
DE AltName: Full=Mitochondrial large ribosomal subunit protein mL44 {ECO:0000303|PubMed:24675956};
DE AltName: Full=YmL3;
DE Flags: Precursor;
GN Name=MRPL3; OrderedLocusNames=YMR024W; ORFNames=YM9711.14;
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=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 60-87, 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 [5]
RP PROTEIN SEQUENCE OF 64-72; 82-94; 105-118; 219-228; 231-239; 262-274 AND
RP 333-356.
RC STRAIN=ATCC 200060 / W303;
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].
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 mL44 forms a heterodimer with mL57 and stabilizes rRNA expansion
CC segments 1/2 at a membrane-facing protuberance close to the point of
CC attachment of the ribosome to the translocon in the membrane.
CC {ECO:0000269|PubMed:12392552, ECO:0000269|PubMed:24675956,
CC 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 300 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ribonuclease III family. Mitochondrion-
CC specific ribosomal protein mL44 subfamily. {ECO:0000305}.
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DR EMBL; Z49211; CAA89127.1; -; Genomic_DNA.
DR EMBL; AY693061; AAT93080.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09922.1; -; Genomic_DNA.
DR PIR; S54026; S54026.
DR RefSeq; NP_013737.1; NM_001182520.1.
DR PDB; 3J6B; EM; 3.20 A; 5=1-390.
DR PDB; 5MRC; EM; 3.25 A; 5=67-390.
DR PDB; 5MRE; EM; 3.75 A; 5=67-390.
DR PDB; 5MRF; EM; 4.97 A; 5=67-390.
DR PDBsum; 3J6B; -.
DR PDBsum; 5MRC; -.
DR PDBsum; 5MRE; -.
DR PDBsum; 5MRF; -.
DR AlphaFoldDB; P36516; -.
DR SMR; P36516; -.
DR BioGRID; 35196; 74.
DR ComplexPortal; CPX-1602; 54S mitochondrial large ribosomal subunit.
DR DIP; DIP-6798N; -.
DR IntAct; P36516; 16.
DR MINT; P36516; -.
DR STRING; 4932.YMR024W; -.
DR MaxQB; P36516; -.
DR PaxDb; P36516; -.
DR PRIDE; P36516; -.
DR EnsemblFungi; YMR024W_mRNA; YMR024W; YMR024W.
DR GeneID; 855039; -.
DR KEGG; sce:YMR024W; -.
DR SGD; S000004626; MRPL3.
DR VEuPathDB; FungiDB:YMR024W; -.
DR eggNOG; KOG3769; Eukaryota.
DR HOGENOM; CLU_034765_1_0_1; -.
DR InParanoid; P36516; -.
DR OMA; MYAYVGP; -.
DR BioCyc; YEAST:G3O-32729-MON; -.
DR PRO; PR:P36516; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P36516; 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:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR GO; GO:0004525; F:ribonuclease III activity; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR GO; GO:0032543; P:mitochondrial translation; IC:SGD.
DR GO; GO:0070125; P:mitochondrial translational elongation; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR CDD; cd19873; DSRM_MRPL3_like; 1.
DR Gene3D; 1.10.1520.10; -; 1.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR044443; MRPL3-like_DSRM.
DR InterPro; IPR011907; RNase_III.
DR InterPro; IPR000999; RNase_III_dom.
DR InterPro; IPR036389; RNase_III_sf.
DR PANTHER; PTHR11207; PTHR11207; 1.
DR Pfam; PF00035; dsrm; 1.
DR SMART; SM00358; DSRM; 1.
DR SMART; SM00535; RIBOc; 1.
DR SUPFAM; SSF69065; SSF69065; 1.
DR PROSITE; PS50137; DS_RBD; 1.
DR PROSITE; PS50142; RNASE_3_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Mitochondrion; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; Transit peptide.
FT TRANSIT 1..59
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:3060376"
FT CHAIN 60..390
FT /note="54S ribosomal protein L3, mitochondrial"
FT /id="PRO_0000030569"
FT DOMAIN 139..205
FT /note="RNase III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 302..372
FT /note="DRBM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT CONFLICT 60
FT /note="Q -> E (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 390 AA; 44000 MW; 0714E1BD875B0155 CRC64;
MGIVLKRAIA AGMKPFPNST WHWSRTIRPF SQHLSSTCFL QQSSRFTSKR YLHLSTLTQQ
EKRFLPESEL AKYKEYYQGL KSTVNEIPES VASKSPSLRT LHKRLQLPNE LTYSTLSRCL
TCPSAKLPDK INNPTKGAAF VNTVPTNKYL DNHGLNIMGK NLLSYHVTKS IIQKYPRLPT
VVLNAAVNAY ISEAVLAHIA KYWGIEVETT SVLSRYLKME PFEFTLGRLK FFNNSLNSKD
GIELITGKNF SETSALAMSV RSIIAAIWAV TEQKDSQAVY RFIDDHIMSR KLDITKMFQF
EQPTRELAML CRREGLEKPV SKLVAESGRL SKSPVFIVHV FSGEETLGEG YGSSLKEAKA
RAATDALMKW YCYEPLAQQE PVIDPGTVVV
