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RM11_YEAST
ID   RM11_YEAST              Reviewed;         249 AA.
AC   P36521; D6VRF2; Q12313;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 165.
DE   RecName: Full=54S ribosomal protein L11, mitochondrial;
DE   AltName: Full=Mitochondrial large ribosomal subunit protein uL10m {ECO:0000303|PubMed:24675956};
DE   AltName: Full=YmL11;
DE   Flags: Precursor;
GN   Name=MRPL11; OrderedLocusNames=YDL202W; ORFNames=D1070;
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=ATCC 96604 / S288c / FY1679;
RX   PubMed=9046097;
RX   DOI=10.1002/(sici)1097-0061(199702)13:2<163::aid-yea54>3.0.co;2-4;
RA   Bahr A., Moeller-Rieker S., Hankeln T., Kraemer C., Protin U.,
RA   Schmidt E.R.;
RT   "The nucleotide sequence of a 39 kb segment of yeast chromosome IV: 12 new
RT   open reading frames, nine known genes and one gene for Gly-tRNA.";
RL   Yeast 13:163-169(1997).
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   PROTEIN SEQUENCE OF 32-61, 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   SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=9162110; DOI=10.1007/s002940050221;
RA   Bui D.M., Jarosch E., Schweyen R.J.;
RT   "The yeast ORF YDL202w codes for the mitochondrial ribosomal protein
RT   YmL11.";
RL   Curr. Genet. 31:396-400(1997).
RN   [6]
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   [7]
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   [8]
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   [9]
RP   NOMENCLATURE.
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).
RN   [10]
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).
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) (PubMed:2060626, PubMed:9162110). Mature yeast 74S mitochondrial
CC       ribosomes consist of a small (37S) and a large (54S) subunit. The 37S
CC       small subunit contains a 15S ribosomal RNA (15S mt-rRNA) and 34
CC       different proteins. The 54S large subunit contains a 21S rRNA (21S mt-
CC       rRNA) and 46 different proteins (PubMed:24675956).
CC       {ECO:0000269|PubMed:2060626, ECO:0000269|PubMed:9162110,
CC       ECO:0000305|PubMed:24675956}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:9162110}.
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 6000 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL10 family.
CC       {ECO:0000305}.
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DR   EMBL; X99000; CAA67467.1; -; Genomic_DNA.
DR   EMBL; Z74250; CAA98780.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11662.1; -; Genomic_DNA.
DR   PIR; S67761; S67761.
DR   RefSeq; NP_010079.1; NM_001180262.1.
DR   AlphaFoldDB; P36521; -.
DR   SMR; P36521; -.
DR   BioGRID; 31844; 102.
DR   ComplexPortal; CPX-1602; 54S mitochondrial large ribosomal subunit.
DR   DIP; DIP-5294N; -.
DR   MINT; P36521; -.
DR   STRING; 4932.YDL202W; -.
DR   CarbonylDB; P36521; -.
DR   iPTMnet; P36521; -.
DR   MaxQB; P36521; -.
DR   PaxDb; P36521; -.
DR   PRIDE; P36521; -.
DR   EnsemblFungi; YDL202W_mRNA; YDL202W; YDL202W.
DR   GeneID; 851325; -.
DR   KEGG; sce:YDL202W; -.
DR   SGD; S000002361; MRPL11.
DR   VEuPathDB; FungiDB:YDL202W; -.
DR   eggNOG; ENOG502QRUI; Eukaryota.
DR   GeneTree; ENSGT00390000000603; -.
DR   HOGENOM; CLU_078018_1_0_1; -.
DR   InParanoid; P36521; -.
DR   OMA; PLFKGPT; -.
DR   BioCyc; YEAST:G3O-29585-MON; -.
DR   PRO; PR:P36521; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P36521; protein.
DR   GO; GO:0015934; C:large ribosomal subunit; IBA:GO_Central.
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   GO; GO:0006412; P:translation; IBA:GO_Central.
DR   CDD; cd05797; Ribosomal_L10; 1.
DR   Gene3D; 3.30.70.1730; -; 1.
DR   InterPro; IPR043141; Ribosomal_L10-like_sf.
DR   InterPro; IPR001790; Ribosomal_L10P.
DR   PANTHER; PTHR11560; PTHR11560; 1.
DR   Pfam; PF00466; Ribosomal_L10; 1.
DR   SUPFAM; SSF160369; SSF160369; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Mitochondrion; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT   TRANSIT         1..31
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:2060626"
FT   CHAIN           32..249
FT                   /note="54S ribosomal protein L11, mitochondrial"
FT                   /id="PRO_0000030440"
FT   REGION          226..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..249
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        35
FT                   /note="S -> H (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        42
FT                   /note="T -> P (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        48
FT                   /note="S -> K (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        51
FT                   /note="T -> V (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        56
FT                   /note="T -> L (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        60
FT                   /note="L -> N (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   249 AA;  28515 MW;  C245C62F1378796B CRC64;
     MLQLRFMPGW VPRNGFFGLK ETIGTVHKRF YALASEQPSR KTVKPLDSRK TFLIDTYKHL
     MENSSMIFFV HYNNLSKTED HHFRFKIKQT GGKLTKVRNN LFEVYLRNSH LPDPCGFVKR
     KEQNWKHPLL PLLKGPTATI TYEDTNPQQV AKLLKVLQSA QDKLMVIGAK VENEVLNVEK
     INTFKTLPTK PEMQSQLVSV LQMLSGLGLV RTLENSSNAL YLTLKSHNDN QKPKEDVEST
     TDAESKGSK
 
 
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