RL41A_YEAST
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 03-AUG-2022, entry version 70.
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}.
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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 PDB; 7NRC; EM; 3.90 A; Lp=1-25.
DR PDB; 7OLC; EM; 2.90 A; Ln/Lr=1-25.
DR PDB; 7OLD; EM; 3.00 A; Ln/Lr=1-25.
DR PDB; 7RR5; EM; 3.23 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 PDBsum; 7NRC; -.
DR PDBsum; 7OLC; -.
DR PDBsum; 7OLD; -.
DR PDBsum; 7RR5; -.
DR AlphaFoldDB; P0CX86; -.
DR SMR; P0CX86; -.
DR BioGRID; 31860; 90.
DR BioGRID; 31928; 53.
DR IntAct; P0CX86; 5.
DR STRING; 4932.YDL133C-A; -.
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 VEuPathDB; FungiDB:YDL133C-A; -.
DR VEuPathDB; FungiDB:YDL184C; -.
DR HOGENOM; CLU_220499_0_0_1; -.
DR BioCyc; YEAST:G3O-29570-MON; -.
DR PRO; PR:P0CX86; -.
DR Proteomes; UP000002311; Chromosome IV.
DR ExpressionAtlas; P0CX86; baseline and 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 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 REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 3..22
FT /evidence="ECO:0007829|PDB:5XYI"
SQ SEQUENCE 25 AA; 3337 MW; BD2629DD9ED85381 CRC64;
MRAKWRKKRT RRLKRKRRKV RARSK
