RT17_YEAST
ID RT17_YEAST Reviewed; 237 AA.
AC Q03246; D6W012; Q02523;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=37S ribosomal protein S17, mitochondrial;
DE AltName: Full=Mitochondrial small ribosomal subunit protein uS17m {ECO:0000303|PubMed:28154081};
GN Name=MRPS17; OrderedLocusNames=YMR188C; ORFNames=YM8010.18C;
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] OF 1-47.
RX PubMed=7498764; DOI=10.1093/genetics/140.4.1213;
RA Sinclair D.A., Dawes I.W.;
RT "Genetics of the synthesis of serine from glycine and the utilization of
RT glycine as sole nitrogen source by Saccharomyces cerevisiae.";
RL Genetics 140:1213-1222(1995).
RN [4]
RP IDENTIFICATION IN THE MITOCHONDRIAL RIBOSOMAL SMALL 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 [5]
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 [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 [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 [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15543521; DOI=10.1002/yea.1174;
RA Hanlon S.E., Xu Z., Norris D.N., Vershon A.K.;
RT "Analysis of the meiotic role of the mitochondrial ribosomal proteins
RT Mrps17 and Mrpl37 in Saccharomyces cerevisiae.";
RL Yeast 21:1241-1252(2004).
RN [9]
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 [10]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS), AND SUBUNIT.
RX PubMed=28154081; DOI=10.1126/science.aal2415;
RA Desai N., Brown A., Amunts A., Ramakrishnan V.;
RT "The structure of the yeast mitochondrial ribosome.";
RL Science 355:528-531(2017).
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 (PubMed:25609543, PubMed:28154081). uS17m may have a
CC meiosis-specific role as it accumulates during the middle stage of
CC sporulation (PubMed:15543521). {ECO:0000269|PubMed:15543521,
CC ECO:0000305|PubMed:25609543, ECO:0000305|PubMed:28154081}.
CC -!- SUBUNIT: Component of the mitochondrial small ribosomal subunit (mt-
CC SSU). 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:12392552, ECO:0000269|PubMed:28154081}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:15543521}.
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 2810 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS17 family.
CC {ECO:0000305}.
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DR EMBL; Z49808; CAA89921.1; -; Genomic_DNA.
DR EMBL; U20641; AAB18932.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10086.1; -; Genomic_DNA.
DR PIR; S55135; S55135.
DR RefSeq; NP_013913.1; NM_001182694.1.
DR PDB; 5MRC; EM; 3.25 A; QQ=1-237.
DR PDB; 5MRE; EM; 3.75 A; QQ=1-237.
DR PDB; 5MRF; EM; 4.97 A; QQ=1-237.
DR PDBsum; 5MRC; -.
DR PDBsum; 5MRE; -.
DR PDBsum; 5MRF; -.
DR AlphaFoldDB; Q03246; -.
DR SMR; Q03246; -.
DR BioGRID; 35366; 69.
DR ComplexPortal; CPX-1603; 37S mitochondrial small ribosomal subunit.
DR DIP; DIP-6688N; -.
DR IntAct; Q03246; 7.
DR MINT; Q03246; -.
DR STRING; 4932.YMR188C; -.
DR MaxQB; Q03246; -.
DR PaxDb; Q03246; -.
DR PRIDE; Q03246; -.
DR EnsemblFungi; YMR188C_mRNA; YMR188C; YMR188C.
DR GeneID; 855226; -.
DR KEGG; sce:YMR188C; -.
DR SGD; S000004800; MRPS17.
DR VEuPathDB; FungiDB:YMR188C; -.
DR eggNOG; KOG1740; Eukaryota.
DR HOGENOM; CLU_1246209_0_0_1; -.
DR InParanoid; Q03246; -.
DR OMA; IRNKGQQ; -.
DR BioCyc; YEAST:G3O-32876-MON; -.
DR PRO; PR:Q03246; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03246; protein.
DR GO; GO:0005743; C:mitochondrial inner membrane; IC:ComplexPortal.
DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR GO; GO:0032543; P:mitochondrial translation; IC:SGD.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR000266; Ribosomal_S17/S11.
DR PANTHER; PTHR10744; PTHR10744; 1.
DR Pfam; PF00366; Ribosomal_S17; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding; Sporulation.
FT CHAIN 1..237
FT /note="37S ribosomal protein S17, mitochondrial"
FT /id="PRO_0000128525"
SQ SEQUENCE 237 AA; 27635 MW; F9D606434D1310D6 CRC64;
MARQNFLGLV VSQGKMQKTV KVRVETKVFN KKINKELFHR RDYLVHDEGE ISREGDLVRI
EATRPLSKRK FFAIAEIIRN KGQQFALYES EAQLSVAKEE AQKAKEFLDK RSVRENKLNE
KTTLLRDIRT IQDALSSGST PKELLEIKQR YGIQDFSQET VRQLLQLDIS GLEVNLEKQR
SLIDRIQTRL SELLSNDLKC DQFLKDHGVE DPLTLKKNIK KNLLRKHVMM DMQQPSQ
