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RM16_YEAST
ID   RM16_YEAST              Reviewed;         232 AA.
AC   P38064; D6VPW1; Q07216;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 174.
DE   RecName: Full=54S ribosomal protein L16, mitochondrial;
DE   AltName: Full=Mitochondrial large ribosomal subunit protein uL16m {ECO:0000303|PubMed:24675956};
DE   AltName: Full=YmL47;
DE   Flags: Precursor;
GN   Name=MRPL16; Synonyms=RML16; OrderedLocusNames=YBL038W; ORFNames=YBL0411;
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].
RA   Ozier-Kalogeropoulos O.;
RL   Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7871888; DOI=10.1002/yea.320101113;
RA   de Wergifosse P., Jacques B., Jonniaux J.-L., Purnelle B., Skala J.,
RA   Goffeau A.;
RT   "The sequence of a 22.4 kb DNA fragment from the left arm of yeast
RT   chromosome II reveals homologues to bacterial proline synthetase and murine
RT   alpha-adaptin, as well as a new permease and a DNA-binding protein.";
RL   Yeast 10:1489-1496(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
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   PROTEIN SEQUENCE OF 202-209, 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   FUNCTION, AND SUBUNIT.
RX   PubMed=7478995; DOI=10.1093/nar/23.18.3673;
RA   Pan C., Mason T.L.;
RT   "Identification of the yeast nuclear gene for the mitochondrial homologue
RT   of bacterial ribosomal protein L16.";
RL   Nucleic Acids Res. 23:3673-3677(1995).
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:7478995,
CC       ECO:0000269|PubMed:9151978}.
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 2900 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL16 family.
CC       {ECO:0000305}.
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DR   EMBL; X53995; CAA37942.1; -; Genomic_DNA.
DR   EMBL; X78214; CAA55056.1; -; Genomic_DNA.
DR   EMBL; Z35799; CAA84858.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07081.1; -; Genomic_DNA.
DR   PIR; S50292; S50292.
DR   RefSeq; NP_009515.1; NM_001178278.1.
DR   PDB; 3J6B; EM; 3.20 A; K=1-232.
DR   PDB; 5MRC; EM; 3.25 A; K=38-232.
DR   PDB; 5MRE; EM; 3.75 A; K=38-232.
DR   PDB; 5MRF; EM; 4.97 A; K=38-232.
DR   PDBsum; 3J6B; -.
DR   PDBsum; 5MRC; -.
DR   PDBsum; 5MRE; -.
DR   PDBsum; 5MRF; -.
DR   AlphaFoldDB; P38064; -.
DR   SMR; P38064; -.
DR   BioGRID; 32659; 51.
DR   ComplexPortal; CPX-1602; 54S mitochondrial large ribosomal subunit.
DR   DIP; DIP-3939N; -.
DR   IntAct; P38064; 33.
DR   MINT; P38064; -.
DR   STRING; 4932.YBL038W; -.
DR   MaxQB; P38064; -.
DR   PaxDb; P38064; -.
DR   PRIDE; P38064; -.
DR   EnsemblFungi; YBL038W_mRNA; YBL038W; YBL038W.
DR   GeneID; 852242; -.
DR   KEGG; sce:YBL038W; -.
DR   SGD; S000000134; MRPL16.
DR   VEuPathDB; FungiDB:YBL038W; -.
DR   eggNOG; KOG3422; Eukaryota.
DR   GeneTree; ENSGT00390000002038; -.
DR   HOGENOM; CLU_078858_0_1_1; -.
DR   InParanoid; P38064; -.
DR   OMA; MPGQYEF; -.
DR   BioCyc; YEAST:G3O-28940-MON; -.
DR   PRO; PR:P38064; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P38064; 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:0019843; F:rRNA binding; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR   GO; GO:0032543; P:mitochondrial translation; IMP:SGD.
DR   CDD; cd01433; Ribosomal_L16_L10e; 1.
DR   Gene3D; 3.90.1170.10; -; 1.
DR   InterPro; IPR016180; Ribosomal_L10e/L16.
DR   InterPro; IPR036920; Ribosomal_L10e/L16_sf.
DR   InterPro; IPR000114; Ribosomal_L16.
DR   InterPro; IPR020798; Ribosomal_L16_CS.
DR   PANTHER; PTHR12220; PTHR12220; 1.
DR   Pfam; PF00252; Ribosomal_L16; 1.
DR   PRINTS; PR00060; RIBOSOMALL16.
DR   SUPFAM; SSF54686; SSF54686; 1.
DR   TIGRFAMs; TIGR01164; rplP_bact; 1.
DR   PROSITE; PS00586; RIBOSOMAL_L16_1; 1.
DR   PROSITE; PS00701; RIBOSOMAL_L16_2; 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..41
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           42..232
FT                   /note="54S ribosomal protein L16, mitochondrial"
FT                   /id="PRO_0000030469"
FT   CONFLICT        55
FT                   /note="R -> Q (in Ref. 1; CAA37942)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        119
FT                   /note="V -> L (in Ref. 1; CAA37942)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        209
FT                   /note="K -> N (in Ref. 1; CAA37942)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   232 AA;  26518 MW;  6E0C11EADC4C156C CRC64;
     MFPYLTRMNL SIKMGGLTLK ESSPNAFLNN TTIARRFKHE YAPRFKIVQK KQKGRVPVRT
     GGSIKGSTLQ FGKYGLRLKS EGIRISAQQL KEADNAIMRY VRPLNNGHLW RRLCTNVAVC
     IKGNETRMGK GKGGFDHWMV RVPTGKILFE INGDDLHEKV AREAFRKAGT KLPGVYEFVS
     LDSLVRVGLH SFKNPKDDPV KNFYDENAKK PSKKYLNILK SQEPQYKLFR GR
 
 
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