RT25_YEAST
ID RT25_YEAST Reviewed; 264 AA.
AC P40496; D6VVJ4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=37S ribosomal protein S25, mitochondrial;
DE AltName: Full=Mitochondrial small ribosomal subunit protein mS23 {ECO:0000303|PubMed:28154081};
GN Name=RSM25; OrderedLocusNames=YIL093C;
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=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(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 SUBCELLULAR LOCATION, IDENTIFICATION IN THE MITOCHONDRIAL RIBOSOMAL SMALL
RP COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11278769; DOI=10.1074/jbc.m010864200;
RA Saveanu C., Fromont-Racine M., Harington A., Ricard F., Namane A.,
RA Jacquier A.;
RT "Identification of 12 new yeast mitochondrial ribosomal proteins including
RT 6 that have no prokaryotic homologues.";
RL J. Biol. Chem. 276:15861-15867(2001).
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], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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. {ECO:0000305|PubMed:25609543,
CC 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:11278769, ECO:0000269|PubMed:12392552,
CC ECO:0000269|PubMed:28154081}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11278769,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16823961}.
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 1920 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC mS23 family. {ECO:0000305}.
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DR EMBL; Z46728; CAA86701.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08460.1; -; Genomic_DNA.
DR PIR; S49787; S49787.
DR RefSeq; NP_012173.3; NM_001179441.3.
DR PDB; 5MRC; EM; 3.25 A; UU=1-233.
DR PDB; 5MRE; EM; 3.75 A; UU=1-233.
DR PDB; 5MRF; EM; 4.97 A; UU=1-233.
DR PDBsum; 5MRC; -.
DR PDBsum; 5MRE; -.
DR PDBsum; 5MRF; -.
DR AlphaFoldDB; P40496; -.
DR SMR; P40496; -.
DR BioGRID; 34899; 63.
DR ComplexPortal; CPX-1603; 37S mitochondrial small ribosomal subunit.
DR DIP; DIP-6345N; -.
DR IntAct; P40496; 11.
DR MINT; P40496; -.
DR STRING; 4932.YIL093C; -.
DR MaxQB; P40496; -.
DR PaxDb; P40496; -.
DR PRIDE; P40496; -.
DR EnsemblFungi; YIL093C_mRNA; YIL093C; YIL093C.
DR GeneID; 854715; -.
DR KEGG; sce:YIL093C; -.
DR SGD; S000001355; RSM25.
DR VEuPathDB; FungiDB:YIL093C; -.
DR eggNOG; ENOG502RZQQ; Eukaryota.
DR HOGENOM; CLU_081350_0_0_1; -.
DR InParanoid; P40496; -.
DR OMA; ENWKIWA; -.
DR BioCyc; YEAST:G3O-31353-MON; -.
DR PRO; PR:P40496; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40496; 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:0003735; F:structural constituent of ribosome; IDA:SGD.
DR GO; GO:0032543; P:mitochondrial translation; IC:SGD.
DR InterPro; IPR016939; Mt__Rbsml_prot_S25.
DR PANTHER; PTHR37799; PTHR37799; 1.
DR Pfam; PF13741; MRP-S25; 1.
DR PIRSF; PIRSF029764; RSM25; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT CHAIN 1..264
FT /note="37S ribosomal protein S25, mitochondrial"
FT /id="PRO_0000202972"
FT REGION 233..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 264 AA; 30513 MW; D6E5BB8B1A2B6C2E CRC64;
MKIQTNAVNV LQRTSAYLKS GLLKETPAWY NVVASIPPST KFTREPRFKN PSNGHIIGKL
VDVTEQPHAN NKGLYKTRPN SSDKRVGVKR LYRPPKLTYV EDRLRSLFYK QHPWELSRPK
ILVENEIGDE NYDWSHMLQI GRPLDGESVI QRTMYLIKTK QYGDMVEAYD HARYEFYALR
MQEETEQQVA LEEAEMFGSL FGVSAIEHGI QKEQEVLDVW EKKVVEETEL MAARTSNPAG
SWKDDTTLNT AQEEESTTSE NLHF
