NAM9_YEAST
ID NAM9_YEAST Reviewed; 486 AA.
AC P27929; D6W145;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=37S ribosomal protein NAM9, mitochondrial;
DE AltName: Full=Mitochondrial small ribosomal subunit protein uS4m {ECO:0000303|PubMed:28154081};
DE AltName: Full=Nuclear accommodation of mitochondria protein 9;
GN Name=NAM9; Synonyms=MNA6; OrderedLocusNames=YNL137C; ORFNames=N1211, N1840;
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.
RX PubMed=1729612; DOI=10.1128/mcb.12.1.402-412.1992;
RA Boguta M., Dmochowska A., Borsuk P., Wrobel K., Gargouri A., Lazowska J.,
RA Slonimski P.P., Szczesniak B., Kruszewska A.;
RT "NAM9 nuclear suppressor of mitochondrial ochre mutations in Saccharomyces
RT cerevisiae codes for a protein homologous to S4 ribosomal proteins from
RT chloroplasts, bacteria, and eucaryotes.";
RL Mol. Cell. Biol. 12:402-412(1992).
RN [2]
RP SEQUENCE REVISION.
RA Boguta M.;
RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8619318; DOI=10.1002/yea.320111210;
RA Mallet L., Bussereau F., Jacquet M.;
RT "A 43.5 kb segment of yeast chromosome XIV, which contains MFA2, MEP2,
RT CAP/SRV2, NAM9, FKB1/FPR1/RBP1, MOM22 and CPT1, predicts an adenosine
RT deaminase gene and 14 new open reading frames.";
RL Yeast 11:1195-1209(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [5]
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 [6]
RP FUNCTION, AND MUTAGENESIS OF SER-82.
RX PubMed=7557422; DOI=10.1016/0378-1119(95)00311-s;
RA Dmochowska A., Konopinska A., Krzymowska M., Szczesniak B., Boguta M.;
RT "The NAM9-1 suppressor mutation in a nuclear gene encoding ribosomal
RT mitochondrial protein of Saccharomyces cerevisiae.";
RL Gene 162:81-85(1995).
RN [7]
RP SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-109; ARG-111; PRO-424
RP AND PRO-438.
RX PubMed=10529174; DOI=10.1021/bi990058u;
RA Biswas T.K., Getz G.S.;
RT "The single amino acid changes in the yeast mitochondrial S4 ribosomal
RT protein cause temperature-sensitive defect in the accumulation of
RT mitochondrial 15S rRNA.";
RL Biochemistry 38:13042-13054(1999).
RN [8]
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 [9]
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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
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 uS3m, uS4m and uS5m form the narrow entry site of the mRNA channel.
CC {ECO:0000269|PubMed:10529174, ECO:0000269|PubMed:11278769,
CC ECO:0000269|PubMed:12392552, ECO:0000269|PubMed:28154081}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10529174,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}.
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 3270 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS4 family.
CC {ECO:0000305}.
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DR EMBL; M60730; AAA19439.1; -; Unassigned_DNA.
DR EMBL; Z46843; CAA86888.1; -; Genomic_DNA.
DR EMBL; Z71413; CAA96019.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10411.1; -; Genomic_DNA.
DR PIR; S55146; S55146.
DR RefSeq; NP_014262.3; NM_001182975.3.
DR PDB; 5MRC; EM; 3.25 A; DD=1-486.
DR PDB; 5MRE; EM; 3.75 A; DD=1-486.
DR PDB; 5MRF; EM; 4.97 A; DD=1-486.
DR PDBsum; 5MRC; -.
DR PDBsum; 5MRE; -.
DR PDBsum; 5MRF; -.
DR AlphaFoldDB; P27929; -.
DR SMR; P27929; -.
DR BioGRID; 35689; 71.
DR ComplexPortal; CPX-1603; 37S mitochondrial small ribosomal subunit.
DR DIP; DIP-6702N; -.
DR IntAct; P27929; 34.
DR MINT; P27929; -.
DR STRING; 4932.YNL137C; -.
DR iPTMnet; P27929; -.
DR MaxQB; P27929; -.
DR PaxDb; P27929; -.
DR PRIDE; P27929; -.
DR EnsemblFungi; YNL137C_mRNA; YNL137C; YNL137C.
DR GeneID; 855585; -.
DR KEGG; sce:YNL137C; -.
DR SGD; S000005081; NAM9.
DR VEuPathDB; FungiDB:YNL137C; -.
DR eggNOG; ENOG502QTS9; Eukaryota.
DR HOGENOM; CLU_026386_0_0_1; -.
DR InParanoid; P27929; -.
DR OMA; GDMFQVE; -.
DR BioCyc; YEAST:G3O-33156-MON; -.
DR PRO; PR:P27929; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P27929; 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:0015935; C:small ribosomal subunit; IBA:GO_Central.
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; IC:SGD.
DR GO; GO:0045903; P:positive regulation of translational fidelity; IBA:GO_Central.
DR CDD; cd00165; S4; 1.
DR Gene3D; 3.10.290.10; -; 1.
DR InterPro; IPR022801; Ribosomal_S4/S9.
DR InterPro; IPR005709; Ribosomal_S4_bac-type.
DR InterPro; IPR018079; Ribosomal_S4_CS.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR PANTHER; PTHR11831; PTHR11831; 1.
DR PANTHER; PTHR11831:SF4; PTHR11831:SF4; 1.
DR Pfam; PF01479; S4; 1.
DR SMART; SM00363; S4; 1.
DR PROSITE; PS00632; RIBOSOMAL_S4; 1.
DR PROSITE; PS50889; S4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..486
FT /note="37S ribosomal protein NAM9, mitochondrial"
FT /id="PRO_0000030639"
FT DOMAIN 103..172
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00182"
FT MUTAGEN 82
FT /note="S->L: In NAM9-1; suppressor for ocher mutations in
FT mitochondrial DNA, possibly through decreasing the fidelity
FT of translation."
FT /evidence="ECO:0000269|PubMed:7557422"
FT MUTAGEN 109
FT /note="L->F: In MNA6-3; causes temperature-dependent loss
FT of the 15S rRNA."
FT /evidence="ECO:0000269|PubMed:10529174"
FT MUTAGEN 111
FT /note="R->K: In MNA6-1; causes temperature-dependent loss
FT of the 15S rRNA."
FT /evidence="ECO:0000269|PubMed:10529174"
FT MUTAGEN 424
FT /note="P->L: In MNA6-4; causes temperature-dependent loss
FT of the 15S rRNA."
FT /evidence="ECO:0000269|PubMed:10529174"
FT MUTAGEN 438
FT /note="P->L: In MNA6-2; causes temperature-dependent loss
FT of the 15S rRNA."
FT /evidence="ECO:0000269|PubMed:10529174"
SQ SEQUENCE 486 AA; 56356 MW; 4A5CB85B354955D1 CRC64;
MPRKANLLKS LARGRVRTSF NKYNLFNLYK KGGVDLKSKS LYQQKWTAKQ ETRAYHGEHL
TEKRWQTVFK PKLDSVAQLD ASLRGGEIKE TPFLLQTFAV LEKRLDFALF RAMFASSVRQ
ARQFILHGNV RVNGVKIKHP SYTLKPGDMF SVKPDKVLEA LGAKKPSFQE ALKIDKTQIV
LWNKYVKEAK TEPKEVWEKK LENFEKMSDS NPKKLQFQEF LRQYNKNLES QQYNALKGCT
QEGILRKLLN VEKEIGKSNN EPLSIDELKQ GLPEIQDSQL LESLNNAYQE FFKSGEIRRE
IISKCQPDEL ISLATEMMNP NETTKKELSD GAKSALRSGK RIIAESVKLW TKNITDHFKT
RMSDISDGSL TFDPKWAKNL KYHDPIKLSE LEGDEPKARK LINLPWQKNY VYGRQDPKKP
FFTPWKPRPF LSPFAILPHH LEISFKTCHA VYLRDPVARP GQSEVISPFD VPVHERAYMY
YLRNGK
