GenomeNet

Database: UniProt
Entry: P0CX86
LinkDB: P0CX86
Original site: P0CX86 
ID   RL41A_YEAST             Reviewed;          25 AA.
AC   P0CX86; D6VRG8; P05746;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   07-APR-2021, entry version 65.
DE   RecName: Full=60S ribosomal protein L41-A {ECO:0000303|PubMed:9559554};
DE   AltName: Full=L47;
DE   AltName: Full=Large ribosomal subunit protein eL41-A {ECO:0000303|PubMed:24524803};
DE   AltName: Full=YL41;
GN   Name=RPL41A {ECO:0000303|PubMed:9559554}; Synonyms=RPL47A, YL41A;
GN   OrderedLocusNames=YDL184C; ORFNames=D1290;
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   PROTEIN SEQUENCE.
RX   PubMed=18782943; DOI=10.1007/bf00341461;
RA   Otaka E., Higo K., Itoh T.;
RT   "Yeast ribosomal proteins. VIII. Isolation of two proteins and sequence
RT   characterization of twenty-four proteins from cytoplasmic ribosomes.";
RL   Mol. Gen. Genet. 195:544-546(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2187623; DOI=10.1007/bf00312608;
RA   Suzuki K., Hashimoto T., Otaka E.;
RT   "Yeast ribosomal proteins: XI. Molecular analysis of two genes encoding
RT   YL41, an extremely small and basic ribosomal protein, from Saccharomyces
RT   cerevisiae.";
RL   Curr. Genet. 17:185-190(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8533471; DOI=10.1002/yea.320111007;
RA   Verhasselt P., Voet M., Volckaert G.;
RT   "New open reading frames, one of which is similar to the nifV gene of
RT   Azotobacter vinelandii, found on a 12.5 kbp fragment of chromosome IV of
RT   Saccharomyces cerevisiae.";
RL   Yeast 11:961-966(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11451953; DOI=10.1074/jbc.m103772200;
RA   Yu X., Warner J.R.;
RT   "Expression of a micro-protein.";
RL   J. Biol. Chem. 276:33821-33825(2001).
RN   [5]
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   [6]
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   [7]
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   [8]
RP   NOMENCLATURE, AND SUBUNIT.
RX   PubMed=9559554;
RX   DOI=10.1002/(sici)1097-0061(19980330)14:5<471::aid-yea241>3.0.co;2-u;
RA   Planta R.J., Mager W.H.;
RT   "The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae.";
RL   Yeast 14:471-477(1998).
RN   [9]
RP   MASS SPECTROMETRY.
RX   PubMed=11983894; DOI=10.1073/pnas.082119899;
RA   Lee S.-W., Berger S.J., Martinovic S., Pasa-Tolic L., Anderson G.A.,
RA   Shen Y., Zhao R., Smith R.D.;
RT   "Direct mass spectrometric analysis of intact proteins of the yeast large
RT   ribosomal subunit using capillary LC/FTICR.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:5942-5947(2002).
RN   [10]
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   [11]
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   [12]
RP   NOMENCLATURE.
RX   PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
RA   Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
RA   Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
RA   Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
RA   Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
RA   Williamson J.R., Wilson D., Yonath A., Yusupov M.;
RT   "A new system for naming ribosomal proteins.";
RL   Curr. Opin. Struct. Biol. 24:165-169(2014).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 80S RIBOSOME.
RX   PubMed=21109664; DOI=10.1126/science.1194294;
RA   Ben-Shem A., Jenner L., Yusupova G., Yusupov M.;
RT   "Crystal structure of the eukaryotic ribosome.";
RL   Science 330:1203-1209(2010).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 80S RIBOSOME, SUBUNIT, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=22096102; DOI=10.1126/science.1212642;
RA   Ben-Shem A., Garreau de Loubresse N., Melnikov S., Jenner L., Yusupova G.,
RA   Yusupov M.;
RT   "The structure of the eukaryotic ribosome at 3.0 A resolution.";
RL   Science 334:1524-1529(2011).
CC   -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein complex
CC       responsible for the synthesis of proteins in the cell. The small
CC       ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the
CC       encoded message by selecting cognate aminoacyl-transfer RNA (tRNA)
CC       molecules. The large subunit (LSU) contains the ribosomal catalytic
CC       site termed the peptidyl transferase center (PTC), which catalyzes the
CC       formation of peptide bonds, thereby polymerizing the amino acids
CC       delivered by tRNAs into a polypeptide chain. The nascent polypeptides
CC       leave the ribosome through a tunnel in the LSU and interact with
CC       protein factors that function in enzymatic processing, targeting, and
CC       the membrane insertion of nascent chains at the exit of the ribosomal
CC       tunnel. {ECO:0000305|PubMed:22096102}.
CC   -!- SUBUNIT: Component of the large ribosomal subunit (LSU). Mature yeast
CC       ribosomes consist of a small (40S) and a large (60S) subunit. The 40S
CC       small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33
CC       different proteins (encoded by 57 genes). The large 60S subunit
CC       contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different
CC       proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102).
CC       {ECO:0000269|PubMed:22096102, ECO:0000305|PubMed:9559554}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:22096102}.
CC   -!- MASS SPECTROMETRY: Mass=3335.103; Method=Electrospray;
CC       Note=Monoisotopic mass.; Evidence={ECO:0000269|PubMed:11983894};
CC   -!- MISCELLANEOUS: Present with 11900 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- MISCELLANEOUS: There are 2 genes for eL41 in yeast. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL41 family.
CC       {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; X16065; CAA34201.1; -; Genomic_DNA.
DR   EMBL; X83276; CAA58262.1; -; Genomic_DNA.
DR   EMBL; Z74232; CAA98759.1; -; Genomic_DNA.
DR   EMBL; AY693059; AAT93078.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11678.1; -; Genomic_DNA.
DR   PIR; S22246; R6BY4B.
DR   RefSeq; NP_010097.1; NM_001180244.1.
DR   RefSeq; NP_010148.1; NM_001180194.1.
DR   PDB; 3J6X; EM; 6.10 A; 81=1-25.
DR   PDB; 3J6Y; EM; 6.10 A; 81=1-25.
DR   PDB; 3J77; EM; 6.20 A; 91=1-25.
DR   PDB; 3J78; EM; 6.30 A; 91=1-25.
DR   PDB; 3J80; EM; 3.75 A; h=1-25.
DR   PDB; 3J81; EM; 4.00 A; h=1-25.
DR   PDB; 3JAM; EM; 3.46 A; h=1-25.
DR   PDB; 3JAP; EM; 4.90 A; h=1-25.
DR   PDB; 3JAQ; EM; 6.00 A; h=1-25.
DR   PDB; 4U3M; X-ray; 3.00 A; Q1/q1=1-25.
DR   PDB; 4U3N; X-ray; 3.20 A; Q1/q1=1-25.
DR   PDB; 4U3U; X-ray; 2.90 A; Q1/q1=1-25.
DR   PDB; 4U4N; X-ray; 3.10 A; Q1/q1=1-25.
DR   PDB; 4U4O; X-ray; 3.60 A; Q1/q1=1-25.
DR   PDB; 4U4Q; X-ray; 3.00 A; Q1/q1=1-25.
DR   PDB; 4U4R; X-ray; 2.80 A; Q1/q1=1-25.
DR   PDB; 4U4U; X-ray; 3.00 A; Q1/q1=1-25.
DR   PDB; 4U4Y; X-ray; 3.20 A; Q1/q1=1-25.
DR   PDB; 4U4Z; X-ray; 3.10 A; Q1/q1=1-25.
DR   PDB; 4U53; X-ray; 3.30 A; Q1/q1=1-25.
DR   PDB; 4U55; X-ray; 3.20 A; Q1/q1=1-25.
DR   PDB; 4U56; X-ray; 3.45 A; Q1/q1=1-25.
DR   PDB; 4V6I; EM; 8.80 A; Bq=1-25.
DR   PDB; 4V88; X-ray; 3.00 A; Bn/Dn=1-25.
DR   PDB; 4V8T; EM; 8.10 A; n=1-25.
DR   PDB; 4V91; EM; 3.70 A; n=1-25.
DR   PDB; 5DAT; X-ray; 3.15 A; Q1/q1=1-25.
DR   PDB; 5DC3; X-ray; 3.25 A; Q1/q1=1-25.
DR   PDB; 5DGE; X-ray; 3.45 A; Q1/q1=1-25.
DR   PDB; 5DGF; X-ray; 3.30 A; Q1/q1=1-25.
DR   PDB; 5DGV; X-ray; 3.10 A; Q1/q1=1-25.
DR   PDB; 5FCI; X-ray; 3.40 A; Q1/q1=1-25.
DR   PDB; 5FCJ; X-ray; 3.10 A; Q1/q1=1-25.
DR   PDB; 5GAK; EM; 3.88 A; p=1-25.
DR   PDB; 5I4L; X-ray; 3.10 A; Q1/q1=1-25.
DR   PDB; 5IT7; EM; 3.60 A; nn=1-25.
DR   PDB; 5JUO; EM; 4.00 A; SA=1-25.
DR   PDB; 5JUP; EM; 3.50 A; SA=1-25.
DR   PDB; 5JUS; EM; 4.20 A; SA=1-25.
DR   PDB; 5JUT; EM; 4.00 A; SA=1-25.
DR   PDB; 5JUU; EM; 4.00 A; SA=1-25.
DR   PDB; 5LYB; X-ray; 3.25 A; Q1/q1=1-25.
DR   PDB; 5MC6; EM; 3.80 A; AS=1-25.
DR   PDB; 5NDG; X-ray; 3.70 A; Q1/q1=1-25.
DR   PDB; 5NDW; X-ray; 3.70 A; Q1/q1=1-25.
DR   PDB; 5OBM; X-ray; 3.40 A; Q1/q1=1-25.
DR   PDB; 5TBW; X-ray; 3.00 A; AO/DP=1-25.
DR   PDB; 5TGA; X-ray; 3.30 A; Q1/q1=1-25.
DR   PDB; 5TGM; X-ray; 3.50 A; Q1/q1=1-25.
DR   PDB; 5XYI; EM; 3.35 A; n=1-25.
DR   PDB; 6FYX; EM; 3.05 A; h=1-25.
DR   PDB; 6FYY; EM; 3.05 A; h=1-25.
DR   PDB; 6GSN; EM; 5.75 A; h=1-25.
DR   PDB; 6Z6K; EM; 3.40 A; Ln=1-25.
DR   PDBsum; 3J6X; -.
DR   PDBsum; 3J6Y; -.
DR   PDBsum; 3J77; -.
DR   PDBsum; 3J78; -.
DR   PDBsum; 3J80; -.
DR   PDBsum; 3J81; -.
DR   PDBsum; 3JAM; -.
DR   PDBsum; 3JAP; -.
DR   PDBsum; 3JAQ; -.
DR   PDBsum; 4U3M; -.
DR   PDBsum; 4U3N; -.
DR   PDBsum; 4U3U; -.
DR   PDBsum; 4U4N; -.
DR   PDBsum; 4U4O; -.
DR   PDBsum; 4U4Q; -.
DR   PDBsum; 4U4R; -.
DR   PDBsum; 4U4U; -.
DR   PDBsum; 4U4Y; -.
DR   PDBsum; 4U4Z; -.
DR   PDBsum; 4U53; -.
DR   PDBsum; 4U55; -.
DR   PDBsum; 4U56; -.
DR   PDBsum; 4V6I; -.
DR   PDBsum; 4V88; -.
DR   PDBsum; 4V8T; -.
DR   PDBsum; 4V91; -.
DR   PDBsum; 5DAT; -.
DR   PDBsum; 5DC3; -.
DR   PDBsum; 5DGE; -.
DR   PDBsum; 5DGF; -.
DR   PDBsum; 5DGV; -.
DR   PDBsum; 5FCI; -.
DR   PDBsum; 5FCJ; -.
DR   PDBsum; 5GAK; -.
DR   PDBsum; 5I4L; -.
DR   PDBsum; 5IT7; -.
DR   PDBsum; 5JUO; -.
DR   PDBsum; 5JUP; -.
DR   PDBsum; 5JUS; -.
DR   PDBsum; 5JUT; -.
DR   PDBsum; 5JUU; -.
DR   PDBsum; 5LYB; -.
DR   PDBsum; 5MC6; -.
DR   PDBsum; 5NDG; -.
DR   PDBsum; 5NDW; -.
DR   PDBsum; 5OBM; -.
DR   PDBsum; 5TBW; -.
DR   PDBsum; 5TGA; -.
DR   PDBsum; 5TGM; -.
DR   PDBsum; 5XYI; -.
DR   PDBsum; 6FYX; -.
DR   PDBsum; 6FYY; -.
DR   PDBsum; 6GSN; -.
DR   PDBsum; 6Z6K; -.
DR   SMR; P0CX86; -.
DR   BioGRID; 31860; 89.
DR   BioGRID; 31928; 53.
DR   STRING; 4932.YDL184C; -.
DR   PaxDb; P0CX86; -.
DR   EnsemblFungi; YDL133C-A_mRNA; YDL133C-A; YDL133C-A.
DR   EnsemblFungi; YDL184C_mRNA; YDL184C; YDL184C.
DR   GeneID; 851344; -.
DR   GeneID; 851422; -.
DR   KEGG; sce:YDL133C-A; -.
DR   KEGG; sce:YDL184C; -.
DR   SGD; S000002343; RPL41A.
DR   HOGENOM; CLU_220499_0_0_1; -.
DR   PRO; PR:P0CX86; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   ExpressionAtlas; P0CX86; differential.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR   GO; GO:0002181; P:cytoplasmic translation; IDA:SGD.
DR   GO; GO:0006415; P:translational termination; TAS:Reactome.
DR   InterPro; IPR007836; Ribosomal_L41.
DR   Pfam; PF05162; Ribosomal_L41; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein.
FT   CHAIN           1..25
FT                   /note="60S ribosomal protein L41-A"
FT                   /id="PRO_0000198074"
FT   COMPBIAS        2..23
FT                   /note="Arg-rich"
FT   HELIX           3..22
FT                   /evidence="ECO:0007744|PDB:5XYI"
SQ   SEQUENCE   25 AA;  3337 MW;  BD2629DD9ED85381 CRC64;
     MRAKWRKKRT RRLKRKRRKV RARSK
//
DBGET integrated database retrieval system