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RML2_YEAST
ID   RML2_YEAST              Reviewed;         393 AA.
AC   P32611; D3DLK0;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 167.
DE   RecName: Full=54S ribosomal protein RML2, mitochondrial;
DE            Short=L2;
DE   AltName: Full=Mitochondrial large ribosomal subunit protein uL2m {ECO:0000303|PubMed:24675956};
DE   Flags: Precursor;
GN   Name=RML2; OrderedLocusNames=YEL050C; ORFNames=SYGP-ORF37;
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=9169868;
RA   Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA   Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA   Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA   Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA   Botstein D., Davis R.W.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL   Nature 387:78-81(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   FUNCTION, SUBUNIT, AND MUTAGENESIS OF 336-VAL--ASP-342 AND HIS-343.
RX   PubMed=9079633; DOI=10.1074/jbc.272.13.8165;
RA   Pan C., Mason T.L.;
RT   "Functional analysis of ribosomal protein L2 in yeast mitochondria.";
RL   J. Biol. Chem. 272:8165-8171(1997).
RN   [4]
RP   FUNCTION.
RX   PubMed=10320805; DOI=10.1016/s1388-1981(99)00054-2;
RA   Trotter P.J., Hagerman R.A., Voelker D.R.;
RT   "A yeast strain defective in oleic acid utilization has a mutation in the
RT   RML2 gene.";
RL   Biochim. Biophys. Acta 1438:223-238(1999).
RN   [5]
RP   FUNCTION.
RX   PubMed=11529680; DOI=10.1006/mcbr.2001.0294;
RA   Hagerman R.A., Trotter P.J.;
RT   "A mutation in the yeast mitochondrial ribosomal protein Rml2p is
RT   associated with a defect in catalase gene expression.";
RL   Mol. Cell Biol. Res. Commun. 4:299-306(2001).
RN   [6]
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   [7]
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   [8]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS), SUBUNIT, AND SUBCELLULAR
RP   LOCATION.
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       uL2m has a Na/K ligand binding site. {ECO:0000269|PubMed:24675956,
CC       ECO:0000269|PubMed:9079633}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:24675956}.
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   -!- MISCELLANEOUS: Present with 1600 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL2 family.
CC       {ECO:0000305}.
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DR   EMBL; U18779; AAB64992.1; -; Genomic_DNA.
DR   EMBL; BK006939; DAA07604.1; -; Genomic_DNA.
DR   PIR; S30827; S30827.
DR   RefSeq; NP_010864.3; NM_001178865.3.
DR   PDB; 3J6B; EM; 3.20 A; B=1-393.
DR   PDB; 5MRC; EM; 3.25 A; B=1-393.
DR   PDB; 5MRE; EM; 3.75 A; B=1-393.
DR   PDB; 5MRF; EM; 4.97 A; B=1-393.
DR   PDBsum; 3J6B; -.
DR   PDBsum; 5MRC; -.
DR   PDBsum; 5MRE; -.
DR   PDBsum; 5MRF; -.
DR   AlphaFoldDB; P32611; -.
DR   SMR; P32611; -.
DR   BioGRID; 36679; 512.
DR   ComplexPortal; CPX-1602; 54S mitochondrial large ribosomal subunit.
DR   DIP; DIP-6812N; -.
DR   IntAct; P32611; 5.
DR   MINT; P32611; -.
DR   STRING; 4932.YEL050C; -.
DR   MaxQB; P32611; -.
DR   PaxDb; P32611; -.
DR   PRIDE; P32611; -.
DR   EnsemblFungi; YEL050C_mRNA; YEL050C; YEL050C.
DR   GeneID; 856660; -.
DR   KEGG; sce:YEL050C; -.
DR   SGD; S000000776; RML2.
DR   VEuPathDB; FungiDB:YEL050C; -.
DR   eggNOG; KOG0438; Eukaryota.
DR   GeneTree; ENSGT00940000153244; -.
DR   HOGENOM; CLU_036235_3_1_1; -.
DR   InParanoid; P32611; -.
DR   OMA; LAMNAMD; -.
DR   BioCyc; YEAST:G3O-30168-MON; -.
DR   PRO; PR:P32611; -.
DR   Proteomes; UP000002311; Chromosome V.
DR   RNAct; P32611; 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:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR   GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR   GO; GO:0032543; P:mitochondrial translation; IMP:SGD.
DR   Gene3D; 2.30.30.30; -; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 4.10.950.10; -; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR022666; Rbsml_prot_L2_RNA-bd_dom.
DR   InterPro; IPR014722; Rib_L2_dom2.
DR   InterPro; IPR002171; Ribosomal_L2.
DR   InterPro; IPR005880; Ribosomal_L2_bac/org-type.
DR   InterPro; IPR022669; Ribosomal_L2_C.
DR   InterPro; IPR022671; Ribosomal_L2_CS.
DR   InterPro; IPR014726; Ribosomal_L2_dom3.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   PANTHER; PTHR13691; PTHR13691; 1.
DR   Pfam; PF00181; Ribosomal_L2; 1.
DR   Pfam; PF03947; Ribosomal_L2_C; 1.
DR   SMART; SM01383; Ribosomal_L2; 1.
DR   SMART; SM01382; Ribosomal_L2_C; 1.
DR   SUPFAM; SSF50104; SSF50104; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR01171; rplB_bact; 1.
DR   PROSITE; PS00467; RIBOSOMAL_L2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein; Transit peptide.
FT   TRANSIT         1..43
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           44..393
FT                   /note="54S ribosomal protein RML2, mitochondrial"
FT                   /id="PRO_0000030512"
FT   REGION          337..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         336..342
FT                   /note="Missing: Loss of function."
FT                   /evidence="ECO:0000269|PubMed:9079633"
FT   MUTAGEN         343
FT                   /note="H->Q: Causes a cold-sensitive respiratory growth
FT                   defect. Does not impair assembly of the ribosomal subunit."
FT                   /evidence="ECO:0000269|PubMed:9079633"
SQ   SEQUENCE   393 AA;  43786 MW;  6AD955FF61C24923 CRC64;
     MLVLGSLRSA LSCSSTASLI SKRNPCYPYG ILCRTLSQSV KLWQENTSKD DSSLNITPRL
     LKIIPNDTDI VTLEKQDELI KRRRKLSKEV TQMKRLKPVS PGLRWYRSPI YPYLYKGRPV
     RALTVVRKKH GGRNNSGKIT VRHQGGGHRN RTRLIDFNRW EGGAQTVQRI EYDPGRSSHI
     ALLKHNTTGE LSYIIACDGL RPGDVVESFR RGIPQTLLNE MGGKVDPAIL SVKTTQRGNC
     LPISMIPIGT IIHNVGITPV GPGKFCRSAG TYARVLAKLP EKKKAIVRLQ SGEHRYVSLE
     AVATIGVVSN IDHQNRSLGK AGRSRWLGIR PTVRGVAMNK CDHPHGGGRG KSKSNKLSMS
     PWGQLAKGYK TRRGKNQNRM KVKDRPRGKD ARL
 
 
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