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RT12_YEAST
ID   RT12_YEAST              Reviewed;         153 AA.
AC   P53732; D6W1L2;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 164.
DE   RecName: Full=37S ribosomal protein S12, mitochondrial;
DE   AltName: Full=Mitochondrial small ribosomal subunit protein uS12m {ECO:0000303|PubMed:28154081};
DE   Flags: Precursor;
GN   Name=MRPS12; OrderedLocusNames=YNR036C; ORFNames=N3298;
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   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   [4]
RP   FUNCTION.
RX   PubMed=11780787; DOI=10.1038/sj.jim.7000093;
RA   Fujita K., Horie T., Isono K.;
RT   "Cross-genomic analysis of the translational systems of various
RT   organisms.";
RL   J. Ind. Microbiol. Biotechnol. 27:163-169(2001).
RN   [5]
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   [6]
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   [7]
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   [8]
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 (PubMed:25609543, PubMed:28154081). uS12m is required for
CC       respiratory growth (PubMed:11780787). {ECO:0000269|PubMed:11780787,
CC       ECO:0000305|PubMed:25609543, 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       uS12m forms part of the decoding center of the mt-SSU.
CC       {ECO:0000269|PubMed:28154081}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {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 238 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS12 family.
CC       {ECO:0000305}.
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DR   EMBL; Z71651; CAA96316.1; -; Genomic_DNA.
DR   EMBL; AY558003; AAS56329.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10578.1; -; Genomic_DNA.
DR   PIR; S63367; S63367.
DR   RefSeq; NP_014434.1; NM_001183213.1.
DR   PDB; 5MRC; EM; 3.25 A; LL=29-152.
DR   PDB; 5MRE; EM; 3.75 A; LL=29-152.
DR   PDB; 5MRF; EM; 4.97 A; LL=29-152.
DR   PDBsum; 5MRC; -.
DR   PDBsum; 5MRE; -.
DR   PDBsum; 5MRF; -.
DR   AlphaFoldDB; P53732; -.
DR   SMR; P53732; -.
DR   BioGRID; 35862; 80.
DR   ComplexPortal; CPX-1603; 37S mitochondrial small ribosomal subunit.
DR   DIP; DIP-5562N; -.
DR   IntAct; P53732; 31.
DR   MINT; P53732; -.
DR   STRING; 4932.YNR036C; -.
DR   MaxQB; P53732; -.
DR   PaxDb; P53732; -.
DR   PRIDE; P53732; -.
DR   EnsemblFungi; YNR036C_mRNA; YNR036C; YNR036C.
DR   GeneID; 855772; -.
DR   KEGG; sce:YNR036C; -.
DR   SGD; S000005319; MRPS12.
DR   VEuPathDB; FungiDB:YNR036C; -.
DR   eggNOG; KOG1750; Eukaryota.
DR   GeneTree; ENSGT00960000189191; -.
DR   HOGENOM; CLU_104295_0_0_1; -.
DR   InParanoid; P53732; -.
DR   OMA; SPALEKC; -.
DR   BioCyc; YEAST:G3O-33346-MON; -.
DR   PRO; PR:P53732; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P53732; 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:0005840; C:ribosome; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR   GO; GO:0032543; P:mitochondrial translation; ISS:UniProtKB.
DR   GO; GO:0006412; P:translation; IBA:GO_Central.
DR   CDD; cd03368; Ribosomal_S12; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR006032; Ribosomal_S12/S23.
DR   InterPro; IPR005679; Ribosomal_S12_bac.
DR   PANTHER; PTHR11652; PTHR11652; 1.
DR   Pfam; PF00164; Ribosom_S12_S23; 1.
DR   PIRSF; PIRSF002133; Ribosomal_S12/S23; 1.
DR   PRINTS; PR01034; RIBOSOMALS12.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00981; rpsL_bact; 1.
DR   PROSITE; PS00055; RIBOSOMAL_S12; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein; Transit peptide.
FT   TRANSIT         1..20
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..153
FT                   /note="37S ribosomal protein S12, mitochondrial"
FT                   /id="PRO_0000146483"
SQ   SEQUENCE   153 AA;  16917 MW;  B50E2ABEB211580D CRC64;
     MLSRFMSNTW CTPLRQAQRL FSSTTTMQAT LNQIKRGSGP PRRKKISTAP QLDQCPQRKG
     VVLRVMVLKP KKPNSAQRKA CRVRLTNGNV VSAYIPGEGH DAQEHSIVYV RGGRCQDLPG
     VKYHVIRGAG DLSGVVNRIS SRSKYGAKKP SKS
 
 
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