ID   RT04_YEAST              Reviewed;         394 AA.
AC   P32902; D3DKR0;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   02-SEP-2026, entry version 187.
DE   RecName: Full=Small ribosomal subunit protein uS2m {ECO:0000303|PubMed:28154081};
DE   AltName: Full=37S ribosomal protein MRP4, mitochondrial;
DE   Flags: Precursor;
GN   Name=MRP4; Synonyms=MRP4A; OrderedLocusNames=YHL004W;
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].
RX   PubMed=1531984; DOI=10.1016/s0021-9258(18)42796-2;
RA   Davis S.C., Tzagoloff A., Ellis S.R.;
RT   "Characterization of a yeast mitochondrial ribosomal protein structurally
RT   related to the mammalian 68-kDa high affinity laminin receptor.";
RL   J. Biol. Chem. 267:5508-5514(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA   Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA   Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA   Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA   St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA   Waterston R., Wilson R., Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   IDENTIFICATION IN THE MITOCHONDRIAL RIBOSOMAL SMALL COMPLEX, AND
RP   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   [6]
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   [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 (3.25 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: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 6890 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS2 family.
CC       {ECO:0000305}.
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DR   EMBL; M82841; AAA34793.1; -; Genomic_DNA.
DR   EMBL; U10555; AAB68428.1; -; Genomic_DNA.
DR   EMBL; AY558385; AAS56711.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06683.1; -; Genomic_DNA.
DR   PIR; A42115; A42115.
DR   RefSeq; NP_011859.1; NM_001179084.1.
DR   PDB; 5MRC; EM; 3.25 A; BB=128-393.
DR   PDB; 5MRE; EM; 3.75 A; BB=128-393.
DR   PDB; 5MRF; EM; 4.97 A; BB=128-393.
DR   PDB; 8D8K; EM; 3.13 A; B=1-394.
DR   PDB; 8D8L; EM; 2.60 A; B=1-394.
DR   PDB; 8OM2; EM; 2.57 A; B=1-394.
DR   PDB; 8OM3; EM; 2.87 A; B=1-394.
DR   PDB; 8OM4; EM; 2.32 A; B=1-394.
DR   PDB; 8UX4; EM; 3.30 A; h=128-394.
DR   PDB; 8UXA; EM; 3.20 A; h=128-394.
DR   PDB; 9HLZ; EM; 3.20 A; B=1-394.
DR   PDB; 9HM0; EM; 3.00 A; B=1-394.
DR   AlphaFoldDB; P32902; -.
DR   EMDB; EMD-16966; -.
DR   EMDB; EMD-16967; -.
DR   EMDB; EMD-16968; -.
DR   EMDB; EMD-27250; -.
DR   EMDB; EMD-27251; -.
DR   EMDB; EMD-3551; -.
DR   EMDB; EMD-3552; -.
DR   EMDB; EMD-3553; -.
DR   EMDB; EMD-42687; -.
DR   EMDB; EMD-42720; -.
DR   EMDB; EMD-52283; -.
DR   SMR; P32902; -.
DR   BioGRID; 36421; 145.
DR   ComplexPortal; CPX-1603; 37S mitochondrial small ribosomal subunit.
DR   DIP; DIP-5035N; -.
DR   FunCoup; P32902; 992.
DR   IntAct; P32902; 81.
DR   MINT; P32902; -.
DR   STRING; 4932.YHL004W; -.
DR   PaxDb; 4932-YHL004W; -.
DR   PeptideAtlas; P32902; -.
DR   EnsemblFungi; YHL004W_mRNA; YHL004W; YHL004W.
DR   GeneID; 856384; -.
DR   KEGG; sce:YHL004W; -.
DR   AGR; SGD:S000000996; -.
DR   SGD; S000000996; MRP4.
DR   VEuPathDB; FungiDB:YHL004W; -.
DR   eggNOG; KOG0832; Eukaryota.
DR   HOGENOM; CLU_040318_4_3_1; -.
DR   InParanoid; P32902; -.
DR   OMA; RNCINEC; -.
DR   OrthoDB; 2320368at2759; -.
DR   BioCyc; YEAST:G3O-31027-MONOMER; -.
DR   Reactome; R-SCE-9837999; Mitochondrial protein degradation.
DR   BioGRID-ORCS; 856384; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P32902; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; P32902; protein.
DR   GO; GO:0005743; C:mitochondrial inner membrane; NAS: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; NAS:ComplexPortal.
DR   CDD; cd01425; RPS2; 1.
DR   FunFam; 3.40.50.10490:FF:000055; Mitochondrial ribosomal protein; 1.
DR   Gene3D; 3.40.50.10490; Glucose-6-phosphate isomerase like protein, domain 1; 1.
DR   HAMAP; MF_00291_B; Ribosomal_uS2_B; 1.
DR   InterPro; IPR001865; Ribosomal_uS2.
DR   InterPro; IPR005706; Ribosomal_uS2_bac/mit/plastid.
DR   InterPro; IPR018130; Ribosomal_uS2_CS.
DR   InterPro; IPR023591; Ribosomal_uS2_flav_dom_sf.
DR   NCBIfam; TIGR01011; rpsB_bact; 1.
DR   PANTHER; PTHR12534; 30S RIBOSOMAL PROTEIN S2 PROKARYOTIC AND ORGANELLAR; 1.
DR   PANTHER; PTHR12534:SF0; SMALL RIBOSOMAL SUBUNIT PROTEIN US2M; 1.
DR   Pfam; PF00318; Ribosomal_S2; 1.
DR   PRINTS; PR00395; RIBOSOMALS2.
DR   SUPFAM; SSF52313; Ribosomal protein S2; 1.
DR   PROSITE; PS00962; RIBOSOMAL_S2_1; 1.
DR   PROSITE; PS00963; RIBOSOMAL_S2_2; 1.
DR   PDBsum; 5MRC; -.
DR   PDBsum; 5MRE; -.
DR   PDBsum; 5MRF; -.
DR   PDBsum; 8D8K; -.
DR   PDBsum; 8D8L; -.
DR   PDBsum; 8OM2; -.
DR   PDBsum; 8OM3; -.
DR   PDBsum; 8OM4; -.
DR   PDBsum; 8UX4; -.
DR   PDBsum; 8UXA; -.
DR   PDBsum; 9HLZ; -.
DR   PDBsum; 9HM0; -.
PE   1: Evidence at protein level;
KW   3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein; Transit peptide.
FT   TRANSIT         1..25
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..394
FT                   /note="Small ribosomal subunit protein uS2m"
FT                   /id="PRO_0000134345"
FT   HELIX           38..63
FT                   /evidence="ECO:0007829|PDB:8OM4"
FT   HELIX           66..78
FT                   /evidence="ECO:0007829|PDB:8OM4"
FT   HELIX           84..99
FT                   /evidence="ECO:0007829|PDB:8OM4"
FT   STRAND          100..104
FT                   /evidence="ECO:0007829|PDB:8OM4"
FT   HELIX           134..136
FT                   /evidence="ECO:0007829|PDB:8OM4"
FT   STRAND          137..139
FT                   /evidence="ECO:0007829|PDB:8OM4"
FT   HELIX           140..142
FT                   /evidence="ECO:0007829|PDB:8OM4"
FT   HELIX           143..156
FT                   /evidence="ECO:0007829|PDB:8OM4"
FT   TURN            157..159
FT                   /evidence="ECO:0007829|PDB:8OM4"
FT   HELIX           172..175
FT                   /evidence="ECO:0007829|PDB:8OM4"
FT   HELIX           177..179
FT                   /evidence="ECO:0007829|PDB:8OM4"
FT   HELIX           180..182
FT                   /evidence="ECO:0007829|PDB:8OM4"
FT   HELIX           185..190
FT                   /evidence="ECO:0007829|PDB:8OM4"
FT   TURN            191..194
FT                   /evidence="ECO:0007829|PDB:8OM4"
FT   STRAND          195..198
FT                   /evidence="ECO:0007829|PDB:8OM4"
FT   HELIX           199..201
FT                   /evidence="ECO:0007829|PDB:8OM4"
FT   HELIX           204..209
FT                   /evidence="ECO:0007829|PDB:8OM4"
FT   STRAND          210..214
FT                   /evidence="ECO:0007829|PDB:8OM4"
FT   STRAND          217..220
FT                   /evidence="ECO:0007829|PDB:8OM4"
FT   HELIX           222..242
FT                   /evidence="ECO:0007829|PDB:8OM4"
FT   STRAND          246..249
FT                   /evidence="ECO:0007829|PDB:8OM4"
FT   HELIX           256..266
FT                   /evidence="ECO:0007829|PDB:8OM4"
FT   STRAND          269..271
FT                   /evidence="ECO:0007829|PDB:8OM4"
FT   TURN            277..282
FT                   /evidence="ECO:0007829|PDB:8OM4"
FT   HELIX           283..285
FT                   /evidence="ECO:0007829|PDB:8OM4"
FT   STRAND          288..290
FT                   /evidence="ECO:0007829|PDB:8OM4"
FT   STRAND          292..295
FT                   /evidence="ECO:0007829|PDB:8OM4"
FT   STRAND          297..299
FT                   /evidence="ECO:0007829|PDB:5MRC"
FT   HELIX           304..307
FT                   /evidence="ECO:0007829|PDB:8OM4"
FT   HELIX           308..312
FT                   /evidence="ECO:0007829|PDB:8OM4"
FT   STRAND          318..323
FT                   /evidence="ECO:0007829|PDB:8OM4"
FT   HELIX           325..327
FT                   /evidence="ECO:0007829|PDB:8OM4"
FT   HELIX           329..337
FT                   /evidence="ECO:0007829|PDB:8OM4"
FT   STRAND          342..346
FT                   /evidence="ECO:0007829|PDB:8OM4"
FT   HELIX           352..354
FT                   /evidence="ECO:0007829|PDB:8OM4"
FT   STRAND          355..361
FT                   /evidence="ECO:0007829|PDB:8OM4"
FT   STRAND          363..365
FT                   /evidence="ECO:0007829|PDB:8D8K"
FT   HELIX           366..392
FT                   /evidence="ECO:0007829|PDB:8OM4"
SQ   SEQUENCE   394 AA;  44152 MW;  81A1CB33134BC559 CRC64;
     MQRHVFARNF RRLSLLRNPS LTKRFQSSAS GAANTPNNND EVMLLQQKLL YDEIRSELKS
     LSQVPEDEIL PELKKSLEQD KLSDKEQQLE AELSDFFRNY ALLNKLFDSK TLDGQSSTTT
     AAATPTKPYP NLIPSANDKP YSSQELFLRQ LNHSMRTAKL GATISKVYYP HKDIFYPPLP
     ENITVESLMS AGVHLGQSTS LWRSSTQSYI YGEYKGIHII DLNQTLSYLK RAAKVVEGVS
     ESGGIILFLG TRQGQKRGLE EAAKKTHGYY VSTRWIPGTL TNSTEISGIW EKQEIDSNDN
     PTERALSPNE TSKQVKPDLL VVLNPTENRN ALLEAIKSRV PTIAIIDTDS EPSLVTYPIP
     GNDDSLRSVN FLLGVLARAG QRGLQNRLAR NNEK
//