位置:首页 > 蛋白库 > RT01_YEAST
RT01_YEAST
ID   RT01_YEAST              Reviewed;         321 AA.
AC   P10662; D6VSX7;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 184.
DE   RecName: Full=37S ribosomal protein MRP1, mitochondrial;
DE   AltName: Full=Mitochondrial small ribosomal subunit protein mS43 {ECO:0000303|PubMed:28154081};
DE   Flags: Precursor;
GN   Name=MRP1; OrderedLocusNames=YDR347W; ORFNames=D9651.1;
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].
RX   PubMed=3029111; DOI=10.1016/s0021-9258(18)61515-7;
RA   Myers A.M., Crivellone M.D., Tzagoloff A.;
RT   "Assembly of the mitochondrial membrane system. MRP1 and MRP2, two yeast
RT   nuclear genes coding for mitochondrial ribosomal proteins.";
RL   J. Biol. Chem. 262:3388-3397(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [3]
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   [4]
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   [5]
RP   PROTEIN SEQUENCE OF 30-39 AND 264-278.
RX   PubMed=12426313; DOI=10.1074/jbc.m208287200;
RA   Dziembowski A., Piwowarski J., Hoser R., Minczuk M., Dmochowska A.,
RA   Siep M., van der Spek H., Grivell L.A., Stepien P.P.;
RT   "The yeast mitochondrial degradosome. Its composition, interplay between
RT   RNA helicase and RNase activities and the role in mitochondrial RNA
RT   metabolism.";
RL   J. Biol. Chem. 278:1603-1611(2003).
RN   [6]
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=2185247; DOI=10.1016/s0021-9258(19)39134-3;
RA   Dang H., Franklin G., Darlak K., Spatola A.F., Ellis S.R.;
RT   "Discoordinate expression of the yeast mitochondrial ribosomal protein
RT   MRP1.";
RL   J. Biol. Chem. 265:7449-7454(1990).
RN   [7]
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   [8]
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   [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. {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       mS43 forms a dimer with mS42, building a large protuberance adjacent to
CC       the mRNA channel exit in the mt-SSU body. {ECO:0000269|PubMed:11278769,
CC       ECO:0000269|PubMed:12392552, ECO:0000269|PubMed:2185247,
CC       ECO:0000269|PubMed:28154081}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:2185247}.
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 2840 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC       mS43 family. {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; M15160; AAA74727.1; -; Genomic_DNA.
DR   EMBL; U51032; AAB64783.1; -; Genomic_DNA.
DR   EMBL; AY557787; AAS56113.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA12187.1; -; Genomic_DNA.
DR   PIR; S70112; R6BYM1.
DR   RefSeq; NP_010634.3; NM_001180655.3.
DR   PDB; 5MRC; EM; 3.25 A; 44=1-321.
DR   PDB; 5MRE; EM; 3.75 A; 44=1-321.
DR   PDB; 5MRF; EM; 4.97 A; 44=1-321.
DR   PDBsum; 5MRC; -.
DR   PDBsum; 5MRE; -.
DR   PDBsum; 5MRF; -.
DR   AlphaFoldDB; P10662; -.
DR   SMR; P10662; -.
DR   BioGRID; 32403; 133.
DR   ComplexPortal; CPX-1603; 37S mitochondrial small ribosomal subunit.
DR   DIP; DIP-6740N; -.
DR   IntAct; P10662; 26.
DR   MINT; P10662; -.
DR   STRING; 4932.YDR347W; -.
DR   MaxQB; P10662; -.
DR   PaxDb; P10662; -.
DR   PRIDE; P10662; -.
DR   EnsemblFungi; YDR347W_mRNA; YDR347W; YDR347W.
DR   GeneID; 851948; -.
DR   KEGG; sce:YDR347W; -.
DR   SGD; S000002755; MRP1.
DR   VEuPathDB; FungiDB:YDR347W; -.
DR   eggNOG; KOG0876; Eukaryota.
DR   HOGENOM; CLU_057349_0_0_1; -.
DR   InParanoid; P10662; -.
DR   OMA; VFGKQQY; -.
DR   BioCyc; YEAST:G3O-29901-MON; -.
DR   PRO; PR:P10662; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P10662; 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:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:InterPro.
DR   GO; GO:0032543; P:mitochondrial translation; IC:SGD.
DR   Gene3D; 3.55.40.20; -; 1.
DR   InterPro; IPR019832; Mn/Fe_SOD_C.
DR   InterPro; IPR036314; SOD_C_sf.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   SUPFAM; SSF54719; SSF54719; 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..13
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           14..321
FT                   /note="37S ribosomal protein MRP1, mitochondrial"
FT                   /id="PRO_0000087698"
FT   CONFLICT        113
FT                   /note="P -> S (in Ref. 1; AAA74727)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        319
FT                   /note="N -> H (in Ref. 1; AAA74727)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   321 AA;  36729 MW;  66A814C28BA3B0C2 CRC64;
     MLRFTGARAI RKYSTRYALE HLKEGAPLKG LFSIEGLQKA WFDRVKYLDA KLNDCTNEAQ
     QKPLETLIHE NSKSASKKHI VNYASSLYNL KFSMSSLQGC IRTPPEECPR LGPEALLQTP
     DFNRTISNEP LTTGNERLQA ALISSFGSLM EFRTLLINSN LAISGDGFTW LVARRQLDKR
     AMRNDMPNRD IEYDKLFILN TYNAGTPFNF STSGVMNELN NQYTNMEKQR AKEAGNLEDS
     EMTAKQAKTK FIYETQQKGF SGKEVSYIPL LAIDASPKTW LTDYGVFGKR EYLERVWDSI
     EWKIVESRLP QRTKIQAFNT L
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024