RSM28_YEAST
ID RSM28_YEAST Reviewed; 361 AA.
AC Q03430; D6VTB6; Q8X184; Q8X185;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=37S ribosomal protein RSM28, mitochondrial;
DE AltName: Full=Mitochondrial small ribosomal subunit protein mS46 {ECO:0000303|PubMed:28154081};
DE Flags: Precursor;
GN Name=RSM28; OrderedLocusNames=YDR494W;
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], MUTAGENESIS OF 121-PRO--GLN-187,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=15701796; DOI=10.1128/ec.4.2.337-345.2005;
RA Williams E.H., Bsat N., Bonnefoy N., Butler C.A., Fox T.D.;
RT "Alteration of a novel dispensable mitochondrial ribosomal small-subunit
RT protein, Rsm28p, allows translation of defective COX2 mRNAs.";
RL Eukaryot. Cell 4:337-345(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
RP SEQUENCE REVISION.
RA Sethuraman A., Dolinski K.J.;
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
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 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 [6]
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 [7]
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:15701796, ECO:0000269|PubMed:28154081}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:15701796,
CC ECO:0000269|PubMed:16823961}. 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 -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC mS46 family. {ECO:0000305}.
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DR EMBL; AF459095; AAL69895.1; -; Genomic_DNA.
DR EMBL; AF459096; AAL69896.1; -; Genomic_DNA.
DR EMBL; U33050; AAB64915.2; -; Genomic_DNA.
DR EMBL; BK006938; DAA12326.1; -; Genomic_DNA.
DR PIR; S69661; S69661.
DR RefSeq; NP_010782.4; NM_001180802.3.
DR PDB; 5MRC; EM; 3.25 A; 77=197-361.
DR PDB; 5MRE; EM; 3.75 A; 77=197-361.
DR PDB; 5MRF; EM; 4.97 A; 77=197-361.
DR PDBsum; 5MRC; -.
DR PDBsum; 5MRE; -.
DR PDBsum; 5MRF; -.
DR AlphaFoldDB; Q03430; -.
DR SMR; Q03430; -.
DR BioGRID; 32545; 227.
DR ComplexPortal; CPX-1603; 37S mitochondrial small ribosomal subunit.
DR DIP; DIP-3923N; -.
DR IntAct; Q03430; 1.
DR MINT; Q03430; -.
DR STRING; 4932.YDR494W; -.
DR iPTMnet; Q03430; -.
DR MaxQB; Q03430; -.
DR PaxDb; Q03430; -.
DR PRIDE; Q03430; -.
DR EnsemblFungi; YDR494W_mRNA; YDR494W; YDR494W.
DR GeneID; 852105; -.
DR KEGG; sce:YDR494W; -.
DR SGD; S000002902; RSM28.
DR VEuPathDB; FungiDB:YDR494W; -.
DR eggNOG; ENOG502S2AE; Eukaryota.
DR HOGENOM; CLU_071897_0_0_1; -.
DR InParanoid; Q03430; -.
DR OMA; PRIANSF; -.
DR BioCyc; YEAST:G3O-30017-MON; -.
DR PRO; PR:Q03430; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03430; 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 GO; GO:0070124; P:mitochondrial translational initiation; IGI:SGD.
PE 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..361
FT /note="37S ribosomal protein RSM28, mitochondrial"
FT /id="PRO_0000269654"
FT REGION 37..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 121..187
FT /note="Missing: In RSM28-1; allows translation of defective
FT COX2 mRNAs."
FT /evidence="ECO:0000269|PubMed:15701796"
SQ SEQUENCE 361 AA; 41216 MW; BBDEDCF34F65218B CRC64;
MRSSMFRCVS RAHYSTSVTE DFINSILARA QEATAKASSN ALKLDKMKEG RMQNKRRNGN
QNRNSMNNKE SRGREGNQGE RNMRLKNRSS DSVRANKQQW NKGANTSFVK NPTGNTVVMQ
PQFKKMQNGK NNLKGDARVE DDLLDVFNSS MEQKPVNFNG TPKSKARFQK KSHILTASKR
RKAPQQQLQK VIKRPVSSEY VLEEPTPLSL LEYTPQVFPT KESRLVNFTL DSLKKSNYPI
YRSPNLGILK VHDFTLNTPN FGKYTPGSSL IFAKEPQLQN LLIEEDPEDF HRQVTGEYQL
LKPYVKKDFE KLTKSKDTVS KLVQNSQVVR LSLQSVVMGS EEKKLVYDVC SGMKPISELQ
Q
