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RM24_YEAST
ID   RM24_YEAST              Reviewed;         258 AA.
AC   P36525; D6W017;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 163.
DE   RecName: Full=54S ribosomal protein L24, mitochondrial;
DE   AltName: Full=Mitochondrial large ribosomal subunit protein bL28m {ECO:0000303|PubMed:24675956};
DE   AltName: Full=YmL14/YmL24;
DE   Flags: Precursor;
GN   Name=MRPL24; Synonyms=MRPL14; OrderedLocusNames=YMR193W;
GN   ORFNames=YM9646.05;
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=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(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   PROTEIN SEQUENCE OF 22-49 AND 72-87, AND SUBUNIT.
RC   STRAIN=07173;
RX   PubMed=2060626; DOI=10.1016/0014-5793(91)80759-v;
RA   Grohmann L., Graack H.-R., Kruft V., Choli T., Goldschmidt-Reisin S.,
RA   Kitakawa M.;
RT   "Extended N-terminal sequencing of proteins of the large ribosomal subunit
RT   from yeast mitochondria.";
RL   FEBS Lett. 284:51-56(1991).
RN   [5]
RP   PROTEIN SEQUENCE OF 72-83 AND 129-138, AND SUBUNIT.
RC   STRAIN=07173;
RX   PubMed=9151978; DOI=10.1111/j.1432-1033.1997.t01-2-00449.x;
RA   Kitakawa M., Graack H.-R., Grohmann L., Goldschmidt-Reisin S., Herfurth E.,
RA   Wittmann-Liebold B., Nishimura T., Isono K.;
RT   "Identification and characterization of the genes for mitochondrial
RT   ribosomal proteins of Saccharomyces cerevisiae.";
RL   Eur. J. Biochem. 245:449-456(1997).
RN   [6]
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   [7]
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   [8]
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   [9]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS), AND SUBUNIT.
RX   PubMed=24675956; DOI=10.1126/science.1249410;
RA   Amunts A., Brown A., Bai X.C., Llacer J.L., Hussain T., Emsley P., Long F.,
RA   Murshudov G., Scheres S.H., Ramakrishnan V.;
RT   "Structure of the yeast mitochondrial large ribosomal subunit.";
RL   Science 343:1485-1489(2014).
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:24675956,
CC       ECO:0000305|PubMed:25609543}.
CC   -!- SUBUNIT: Component of the mitochondrial large ribosomal subunit (mt-
CC       LSU). 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:2060626, ECO:0000269|PubMed:24675956,
CC       ECO:0000269|PubMed:9151978}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {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 4000 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL28 family.
CC       {ECO:0000305}.
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DR   EMBL; Z47815; CAA87814.1; -; Genomic_DNA.
DR   EMBL; AY557982; AAS56308.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA10091.1; -; Genomic_DNA.
DR   PIR; S50921; S50921.
DR   RefSeq; NP_013918.1; NM_001182700.1.
DR   PDB; 3J6B; EM; 3.20 A; S=1-258.
DR   PDB; 5MRC; EM; 3.25 A; S=22-237.
DR   PDB; 5MRE; EM; 3.75 A; S=22-237.
DR   PDB; 5MRF; EM; 4.97 A; S=22-237.
DR   PDBsum; 3J6B; -.
DR   PDBsum; 5MRC; -.
DR   PDBsum; 5MRE; -.
DR   PDBsum; 5MRF; -.
DR   AlphaFoldDB; P36525; -.
DR   SMR; P36525; -.
DR   BioGRID; 35371; 223.
DR   ComplexPortal; CPX-1602; 54S mitochondrial large ribosomal subunit.
DR   DIP; DIP-3847N; -.
DR   IntAct; P36525; 6.
DR   MINT; P36525; -.
DR   STRING; 4932.YMR193W; -.
DR   MaxQB; P36525; -.
DR   PaxDb; P36525; -.
DR   PRIDE; P36525; -.
DR   EnsemblFungi; YMR193W_mRNA; YMR193W; YMR193W.
DR   GeneID; 855231; -.
DR   KEGG; sce:YMR193W; -.
DR   SGD; S000004806; MRPL24.
DR   VEuPathDB; FungiDB:YMR193W; -.
DR   eggNOG; KOG3278; Eukaryota.
DR   GeneTree; ENSGT00390000017359; -.
DR   HOGENOM; CLU_090033_0_0_1; -.
DR   InParanoid; P36525; -.
DR   OMA; WKLRYRV; -.
DR   BioCyc; YEAST:G3O-32880-MON; -.
DR   PRO; PR:P36525; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; P36525; protein.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IC:ComplexPortal.
DR   GO; GO:0005762; C:mitochondrial large 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   Gene3D; 2.30.170.40; -; 1.
DR   InterPro; IPR034704; L28p-like.
DR   InterPro; IPR026569; Ribo_L28/L24.
DR   InterPro; IPR037147; Ribo_L28/L24_sf.
DR   PANTHER; PTHR13528; PTHR13528; 1.
DR   Pfam; PF00830; Ribosomal_L28; 1.
DR   SUPFAM; SSF143800; SSF143800; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Mitochondrion; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT   TRANSIT         1..21
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:2060626"
FT   CHAIN           22..258
FT                   /note="54S ribosomal protein L24, mitochondrial"
FT                   /id="PRO_0000030509"
FT   CONFLICT        72
FT                   /note="G -> K (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        76
FT                   /note="G -> D (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        130
FT                   /note="G -> Q (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   258 AA;  30049 MW;  F49DC1D41860E359 CRC64;
     MQKIFRPFQL TRGFTSSVKN FRQWRLIETR KIAKQPNYQV GDAKPLHMPK ERKKFPDYKY
     GESNIFKQSN KGLYGGSFVQ FGNNISESKA KTRKKWLPNV VKKGLWSETL NRKISIKMTA
     KVLKTISKEG GIDNYLTKEK SARIKELGPT GWKLRYRVLK RKDEIENPPH KDAPIIEMAG
     GKKAKIYYDE IVNGSPRKIS VGRRRLMSFL YPLEKLEYRS VGKDLNYKKF VELFADVPVK
     DILARLEDHK FDLSTITV
 
 
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