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RT23_YEAST
ID   RT23_YEAST              Reviewed;         450 AA.
AC   Q01163; D6VU19;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 3.
DT   03-AUG-2022, entry version 158.
DE   RecName: Full=37S ribosomal protein S23, mitochondrial;
DE   AltName: Full=DAP-3;
DE   AltName: Full=Mitochondrial small ribosomal subunit protein mS29 {ECO:0000303|PubMed:28154081};
DE   Flags: Precursor;
GN   Name=RSM23; OrderedLocusNames=YGL129C; ORFNames=G2856;
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].
RC   STRAIN=DBY939;
RX   PubMed=1315757; DOI=10.1016/s0021-9258(19)50122-3;
RA   Shibagaki Y., Itoh N., Yamada H., Nagata S., Mizumoto K.;
RT   "mRNA capping enzyme. Isolation and characterization of the gene encoding
RT   mRNA guanylytransferase subunit from Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 267:9521-9528(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8686378;
RX   DOI=10.1002/(sici)1097-0061(199602)12:2<145::aid-yea888>3.0.co;2-e;
RA   Rodriguez-Belmonte E., Rodriguez Torres A.M., Tizon B., Cadahia J.L.,
RA   Gonzalez-Siso I., Ramil E., Becerra M., Gonzalez-Dominguez M., Cerdan E.;
RT   "Sequence analysis of a 10 kb DNA fragment from yeast chromosome VII
RT   reveals a novel member of the DnaJ family.";
RL   Yeast 12:145-148(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [4]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION.
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   [5]
RP   FUNCTION.
RX   PubMed=11017876; DOI=10.1242/jcs.113.20.3603;
RA   Berger T., Brigl M., Herrmann J.M., Vielhauer V., Luckow B.,
RA   Schloendorff D., Kretzler M.;
RT   "The apoptosis mediator mDAP-3 is a novel member of a conserved family of
RT   mitochondrial proteins.";
RL   J. Cell Sci. 113:3603-3612(2000).
RN   [6]
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   [7]
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   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA   Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA   Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA   Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT   "Assigning function to yeast proteins by integration of technologies.";
RL   Mol. Cell 12:1353-1365(2003).
RN   [9]
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   [10]
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   [11]
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   [12]
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   [13]
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. mS29 binds GTP and is probably an active GTPase. GTP
CC       hydrolysis may be linked to subunit association (PubMed:25609543,
CC       PubMed:28154081). mS29 also has an extraribosomal function, being
CC       required for maintenance of mitochondrial DNA (PubMed:11017876).
CC       {ECO:0000269|PubMed:11017876, 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: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 1300 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC       mS29 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA60702.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAA96838.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; D10263; BAA01104.1; -; Genomic_DNA.
DR   EMBL; X87252; CAA60702.1; ALT_INIT; Genomic_DNA.
DR   EMBL; Z72651; CAA96838.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BK006941; DAA07980.2; -; Genomic_DNA.
DR   PIR; S64140; S64140.
DR   RefSeq; NP_011386.2; NM_001180994.2.
DR   PDB; 5MRC; EM; 3.25 A; WW=50-450.
DR   PDB; 5MRE; EM; 3.75 A; WW=50-450.
DR   PDB; 5MRF; EM; 4.97 A; WW=50-450.
DR   PDBsum; 5MRC; -.
DR   PDBsum; 5MRE; -.
DR   PDBsum; 5MRF; -.
DR   AlphaFoldDB; Q01163; -.
DR   SMR; Q01163; -.
DR   BioGRID; 33122; 63.
DR   ComplexPortal; CPX-1603; 37S mitochondrial small ribosomal subunit.
DR   DIP; DIP-5302N; -.
DR   IntAct; Q01163; 10.
DR   MINT; Q01163; -.
DR   STRING; 4932.YGL129C; -.
DR   MaxQB; Q01163; -.
DR   PaxDb; Q01163; -.
DR   PRIDE; Q01163; -.
DR   EnsemblFungi; YGL129C_mRNA; YGL129C; YGL129C.
DR   GeneID; 852748; -.
DR   KEGG; sce:YGL129C; -.
DR   SGD; S000003097; RSM23.
DR   VEuPathDB; FungiDB:YGL129C; -.
DR   eggNOG; KOG3928; Eukaryota.
DR   GeneTree; ENSGT00390000015248; -.
DR   HOGENOM; CLU_039957_0_0_1; -.
DR   InParanoid; Q01163; -.
DR   OMA; GLAHWMT; -.
DR   BioCyc; YEAST:G3O-30625-MON; -.
DR   PRO; PR:Q01163; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; Q01163; 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:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR   GO; GO:0032543; P:mitochondrial translation; IC:SGD.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR019368; Ribosomal_S23/S29_mit.
DR   InterPro; IPR017082; Ribosomal_S23_mit_fun.
DR   PANTHER; PTHR12810; PTHR12810; 1.
DR   Pfam; PF10236; DAP3; 1.
DR   PIRSF; PIRSF036996; RSM23; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   1: Evidence at protein level;
KW   3D-structure; GTP-binding; Mitochondrion; Nucleotide-binding;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT   TRANSIT         1..14
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           15..450
FT                   /note="37S ribosomal protein S23, mitochondrial"
FT                   /id="PRO_0000202743"
FT   REGION          21..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         150..157
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P51398"
SQ   SEQUENCE   450 AA;  50867 MW;  DCE220C14D020AE2 CRC64;
     MLRMSTSRFI GQRLFTTARS LQAAKPAPKG KTQGFSKKSS SVSSYSSAKR VTPGSLYKNW
     TNTTHTAQLQ QTAVPLALPI FNFDDISKTL NKVVSYSNKQ YKSLHHLGSF KKSQFNELFQ
     KPVCLVREDA TNSFLKKLVS HPVKKFIITG EPGVGKTVLL SQAHAYAVDS KQIIINISYP
     ELFLNGRNDF SYDDDLKLFI QPMYLKKLIR KILKANDPAL LKSIELSKDY KFSNANPKNA
     SVKPFVTLNK TKNTVLDLLS VMTHPHNRGK LMKAIIDELS VQSKVPIMFT VDNFSKVLTT
     AYSAYRNTEN KQIYSLDLQM GKLMMDIISG ETKFANGESS TILAISGVDR TNKTLPVALG
     KIPVDPYVTR YHYEPKFVEL LQKGNVTEFE VPKLNKQEVN ELIDYYKQSN VLLDKDITGK
     KWENLIDEKY FLSGNGNPRE LLKSLVLSHR
 
 
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