RT19_YEAST
ID RT19_YEAST Reviewed; 91 AA.
AC P53733; D6W1L3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=37S ribosomal protein S19, mitochondrial;
DE AltName: Full=Mitochondrial small ribosomal subunit protein uS19m {ECO:0000303|PubMed:28154081};
GN Name=RSM19; OrderedLocusNames=YNR037C; ORFNames=N3300;
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=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 [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].
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 [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:11278769, ECO:0000269|PubMed:12392552,
CC ECO:0000269|PubMed:28154081}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11278769,
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 -!- SIMILARITY: Belongs to the universal ribosomal protein uS19 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z71652; CAA96317.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10579.1; -; Genomic_DNA.
DR PIR; S63368; S63368.
DR RefSeq; NP_014435.3; NM_001183214.3.
DR PDB; 5MRC; EM; 3.25 A; SS=9-88.
DR PDB; 5MRE; EM; 3.75 A; SS=9-88.
DR PDB; 5MRF; EM; 4.97 A; SS=9-88.
DR PDBsum; 5MRC; -.
DR PDBsum; 5MRE; -.
DR PDBsum; 5MRF; -.
DR AlphaFoldDB; P53733; -.
DR SMR; P53733; -.
DR BioGRID; 35863; 186.
DR ComplexPortal; CPX-1603; 37S mitochondrial small ribosomal subunit.
DR DIP; DIP-4257N; -.
DR IntAct; P53733; 6.
DR MINT; P53733; -.
DR STRING; 4932.YNR037C; -.
DR MaxQB; P53733; -.
DR PaxDb; P53733; -.
DR PRIDE; P53733; -.
DR EnsemblFungi; YNR037C_mRNA; YNR037C; YNR037C.
DR GeneID; 855773; -.
DR KEGG; sce:YNR037C; -.
DR SGD; S000005320; RSM19.
DR VEuPathDB; FungiDB:YNR037C; -.
DR eggNOG; KOG0899; Eukaryota.
DR GeneTree; ENSGT00390000000475; -.
DR HOGENOM; CLU_144911_1_0_1; -.
DR InParanoid; P53733; -.
DR OMA; YVAFEIT; -.
DR BioCyc; YEAST:G3O-33347-MON; -.
DR PRO; PR:P53733; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53733; 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:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR GO; GO:0032543; P:mitochondrial translation; IC:SGD.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
DR Gene3D; 3.30.860.10; -; 1.
DR HAMAP; MF_00531; Ribosomal_S19; 1.
DR InterPro; IPR020934; Ribosomal_S15/S19_CS.
DR InterPro; IPR002222; Ribosomal_S19.
DR InterPro; IPR023575; Ribosomal_S19_S15_SF.
DR PANTHER; PTHR11880; PTHR11880; 1.
DR Pfam; PF00203; Ribosomal_S19; 1.
DR PIRSF; PIRSF002144; Ribosomal_S19; 1.
DR PRINTS; PR00975; RIBOSOMALS19.
DR SUPFAM; SSF54570; SSF54570; 1.
DR PROSITE; PS00323; RIBOSOMAL_S19; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT CHAIN 1..91
FT /note="37S ribosomal protein S19, mitochondrial"
FT /id="PRO_0000130025"
SQ SEQUENCE 91 AA; 10275 MW; B39624808BDD9092 CRC64;
MQPAARLLSR SVWKGPNIVP LPIREAMTKG TPIRTNARAA TILPQFVGLK FQIHNGKEYV
PIEISEDMVG HKLGEFAPTR KRFSYTQTKN K
