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60S ribosomal protein L43-A (L37a) (Large ribosomal subunit protein eL43-A) (YL35)

 RL43A_YEAST             Reviewed;          92 AA.
P0CX25; D6VWR3; P49631;
28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
28-JUN-2011, sequence version 1.
18-JUL-2018, entry version 69.
RecName: Full=60S ribosomal protein L43-A {ECO:0000303|PubMed:9559554};
AltName: Full=L37a;
AltName: Full=Large ribosomal subunit protein eL43-A {ECO:0000303|PubMed:24524803};
AltName: Full=YL35;
Name=RPL43A {ECO:0000303|PubMed:9559554}; OrderedLocusNames=YPR043W;
ORFNames=YP9499.02;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 46191 / IL125-2B;
PubMed=9730282;
DOI=10.1002/(SICI)1097-0061(199808)14:11<1027::AID-YEA295>3.3.CO;2-J;
Waskiewicz-Staniorowska B., Skala J., Jasinski M., Grenson M.,
Goffeau A., Ulaszewski S.;
"Functional analysis of three adjacent open reading frames from the
right arm of yeast chromosome XVI.";
Yeast 14:1027-1039(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169875;
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V.,
Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M.,
Chung E., Churcher C.M., Coster F., Davis K., Davis R.W.,
Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A.,
Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A.,
Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W.,
Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K.,
Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J.,
Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D.,
Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V.,
Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W.,
Zollner A., Vo D.H., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
Nature 387:103-105(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
NOMENCLATURE, AND SUBUNIT.
PubMed=9559554;
DOI=10.1002/(SICI)1097-0061(19980330)14:5<471::AID-YEA241>3.0.CO;2-U;
Planta R.J., Mager W.H.;
"The list of cytoplasmic ribosomal proteins of Saccharomyces
cerevisiae.";
Yeast 14:471-477(1998).
[5]
MASS SPECTROMETRY, AND CLEAVAGE OF INITIATOR METHIONINE.
PubMed=11983894; DOI=10.1073/pnas.082119899;
Lee S.-W., Berger S.J., Martinovic S., Pasa-Tolic L., Anderson G.A.,
Shen Y., Zhao R., Smith R.D.;
"Direct mass spectrometric analysis of intact proteins of the yeast
large ribosomal subunit using capillary LC/FTICR.";
Proc. Natl. Acad. Sci. U.S.A. 99:5942-5947(2002).
[6]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[7]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=17287358; DOI=10.1073/pnas.0607084104;
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces
cerevisiae by electron transfer dissociation (ETD) mass
spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[9]
NOMENCLATURE.
PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
Williamson J.R., Wilson D., Yonath A., Yusupov M.;
"A new system for naming ribosomal proteins.";
Curr. Opin. Struct. Biol. 24:165-169(2014).
[10]
3D-STRUCTURE MODELING OF 10-82, AND ELECTRON MICROSCOPY.
PubMed=11701127; DOI=10.1016/S0092-8674(01)00539-6;
Spahn C.M.T., Beckmann R., Eswar N., Penczek P.A., Sali A., Blobel G.,
Frank J.;
"Structure of the 80S ribosome from Saccharomyces cerevisiae -- tRNA-
ribosome and subunit-subunit interactions.";
Cell 107:373-386(2001).
[11]
3D-STRUCTURE MODELING, AND ELECTRON MICROSCOPY.
PubMed=14976550; DOI=10.1038/sj.emboj.7600102;
Spahn C.M.T., Gomez-Lorenzo M.G., Grassucci R.A., Joergensen R.,
Andersen G.R., Beckmann R., Penczek P.A., Ballesta J.P.G., Frank J.;
"Domain movements of elongation factor eEF2 and the eukaryotic 80S
ribosome facilitate tRNA translocation.";
EMBO J. 23:1008-1019(2004).
[12]
X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 80S RIBOSOME.
PubMed=21109664; DOI=10.1126/science.1194294;
Ben-Shem A., Jenner L., Yusupova G., Yusupov M.;
"Crystal structure of the eukaryotic ribosome.";
Science 330:1203-1209(2010).
[13]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 80S RIBOSOME, SUBUNIT, AND
SUBCELLULAR LOCATION.
PubMed=22096102; DOI=10.1126/science.1212642;
Ben-Shem A., Garreau de Loubresse N., Melnikov S., Jenner L.,
Yusupova G., Yusupov M.;
"The structure of the eukaryotic ribosome at 3.0 A resolution.";
Science 334:1524-1529(2011).
-!- FUNCTION: Component of the ribosome, a large ribonucleoprotein
complex responsible for the synthesis of proteins in the cell. The
small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and
translates the encoded message by selecting cognate aminoacyl-
transfer RNA (tRNA) molecules. The large subunit (LSU) contains
the ribosomal catalytic site termed the peptidyl transferase
center (PTC), which catalyzes the formation of peptide bonds,
thereby polymerizing the amino acids delivered by tRNAs into a
polypeptide chain. The nascent polypeptides leave the ribosome
through a tunnel in the LSU and interact with protein factors that
function in enzymatic processing, targeting, and the membrane
insertion of nascent chains at the exit of the ribosomal tunnel.
{ECO:0000305|PubMed:22096102}.
-!- SUBUNIT: Component of the large ribosomal subunit (LSU). Mature
yeast ribosomes consist of a small (40S) and a large (60S)
subunit. The 40S small subunit contains 1 molecule of ribosomal
RNA (18S rRNA) and 33 different proteins (encoded by 57 genes).
The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S
rRNA) and 46 different proteins (encoded by 81 genes)
(PubMed:9559554, PubMed:22096102). {ECO:0000269|PubMed:22096102,
ECO:0000305|PubMed:9559554}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
ECO:0000269|PubMed:22096102}.
-!- MASS SPECTROMETRY: Mass=9953.311; Method=Electrospray; Range=2-92;
Note=Monoisotopic mass.; Evidence={ECO:0000269|PubMed:11983894};
-!- MISCELLANEOUS: Present with 44600 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- MISCELLANEOUS: There are 2 genes for eL43 in yeast. {ECO:0000305}.
-!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL43
family. {ECO:0000305}.
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EMBL; Z73616; CAA97993.1; -; Genomic_DNA.
EMBL; Z71255; CAA94991.1; -; Genomic_DNA.
EMBL; Z49219; CAA89164.1; -; Genomic_DNA.
EMBL; BK006949; DAA11468.1; -; Genomic_DNA.
PIR; S54068; S54068.
RefSeq; NP_012628.3; NM_001181752.3.
RefSeq; NP_015368.1; NM_001184140.1.
PDB; 1K5Y; Model; -; 2=10-82.
PDB; 3J6X; EM; 6.10 A; 83=1-92.
PDB; 3J6Y; EM; 6.10 A; 83=1-92.
PDB; 3J77; EM; 6.20 A; 93=1-92.
PDB; 3J78; EM; 6.30 A; 93=1-92.
PDB; 3JCT; EM; 3.08 A; p=1-92.
PDB; 4U3M; X-ray; 3.00 A; Q3/q3=2-92.
PDB; 4U3N; X-ray; 3.20 A; Q3/q3=2-92.
PDB; 4U3U; X-ray; 2.90 A; Q3/q3=2-92.
PDB; 4U4N; X-ray; 3.10 A; Q3/q3=2-92.
PDB; 4U4O; X-ray; 3.60 A; Q3/q3=2-92.
PDB; 4U4Q; X-ray; 3.00 A; Q3/q3=2-92.
PDB; 4U4R; X-ray; 2.80 A; Q3/q3=2-92.
PDB; 4U4U; X-ray; 3.00 A; Q3/q3=2-92.
PDB; 4U4Y; X-ray; 3.20 A; Q3/q3=2-92.
PDB; 4U4Z; X-ray; 3.10 A; Q3/q3=2-92.
PDB; 4U50; X-ray; 3.20 A; Q3/q3=2-92.
PDB; 4U51; X-ray; 3.20 A; Q3/q3=2-92.
PDB; 4U52; X-ray; 3.00 A; Q3/q3=2-92.
PDB; 4U53; X-ray; 3.30 A; Q3/q3=2-92.
PDB; 4U55; X-ray; 3.20 A; Q3/q3=2-92.
PDB; 4U56; X-ray; 3.45 A; Q3/q3=2-92.
PDB; 4U6F; X-ray; 3.10 A; Q3/q3=2-92.
PDB; 4V4B; EM; 11.70 A; B9=2-92.
PDB; 4V6I; EM; 8.80 A; Bm=1-92.
PDB; 4V7F; EM; 8.70 A; k=1-92.
PDB; 4V7R; X-ray; 4.00 A; Bg/Dg=1-92.
PDB; 4V88; X-ray; 3.00 A; Bp/Dp=1-92.
PDB; 4V8T; EM; 8.10 A; p=1-92.
PDB; 4V91; EM; 3.70 A; p=1-92.
PDB; 5APN; EM; 3.91 A; p=1-92.
PDB; 5APO; EM; 3.41 A; p=1-92.
PDB; 5DAT; X-ray; 3.15 A; Q3/q3=2-92.
PDB; 5DC3; X-ray; 3.25 A; Q3/q3=2-92.
PDB; 5DGE; X-ray; 3.45 A; Q3/q3=2-92.
PDB; 5DGF; X-ray; 3.30 A; Q3/q3=2-92.
PDB; 5DGV; X-ray; 3.10 A; Q3/q3=2-92.
PDB; 5FCI; X-ray; 3.40 A; Q3/q3=2-92.
PDB; 5FCJ; X-ray; 3.10 A; Q3/q3=2-92.
PDB; 5FL8; EM; 9.50 A; p=1-92.
PDB; 5GAK; EM; 3.88 A; D=1-92.
PDB; 5H4P; EM; 3.07 A; p=1-92.
PDB; 5I4L; X-ray; 3.10 A; Q3/q3=2-92.
PDB; 5JCS; EM; 9.50 A; p=1-92.
PDB; 5JUO; EM; 4.00 A; UA=1-92.
PDB; 5JUP; EM; 3.50 A; UA=1-92.
PDB; 5JUS; EM; 4.20 A; UA=1-92.
PDB; 5JUT; EM; 4.00 A; UA=1-92.
PDB; 5JUU; EM; 4.00 A; UA=1-92.
PDB; 5LYB; X-ray; 3.25 A; Q3/q3=2-92.
PDB; 5MC6; EM; 3.80 A; AT=1-92.
PDB; 5MEI; X-ray; 3.50 A; AQ/DR=2-92.
PDB; 5NDG; X-ray; 3.70 A; Q3/q3=2-92.
PDB; 5NDV; X-ray; 3.30 A; Q3/q3=2-92.
PDB; 5NDW; X-ray; 3.70 A; Q3/q3=2-92.
PDB; 5OBM; X-ray; 3.40 A; Q3/q3=2-92.
PDB; 5ON6; X-ray; 3.10 A; AQ/DR=2-92.
PDB; 5T62; EM; 3.30 A; R=1-92.
PDB; 5T6R; EM; 4.50 A; R=1-92.
PDB; 5TBW; X-ray; 3.00 A; AQ/DR=2-92.
PDB; 5TGA; X-ray; 3.30 A; Q3/q3=2-92.
PDB; 5TGM; X-ray; 3.50 A; Q3/q3=2-92.
PDB; 6FT6; EM; 3.90 A; p=1-92.
PDBsum; 1K5Y; -.
PDBsum; 3J6X; -.
PDBsum; 3J6Y; -.
PDBsum; 3J77; -.
PDBsum; 3J78; -.
PDBsum; 3JCT; -.
PDBsum; 4U3M; -.
PDBsum; 4U3N; -.
PDBsum; 4U3U; -.
PDBsum; 4U4N; -.
PDBsum; 4U4O; -.
PDBsum; 4U4Q; -.
PDBsum; 4U4R; -.
PDBsum; 4U4U; -.
PDBsum; 4U4Y; -.
PDBsum; 4U4Z; -.
PDBsum; 4U50; -.
PDBsum; 4U51; -.
PDBsum; 4U52; -.
PDBsum; 4U53; -.
PDBsum; 4U55; -.
PDBsum; 4U56; -.
PDBsum; 4U6F; -.
PDBsum; 4V4B; -.
PDBsum; 4V6I; -.
PDBsum; 4V7F; -.
PDBsum; 4V7R; -.
PDBsum; 4V88; -.
PDBsum; 4V8T; -.
PDBsum; 4V91; -.
PDBsum; 5APN; -.
PDBsum; 5APO; -.
PDBsum; 5DAT; -.
PDBsum; 5DC3; -.
PDBsum; 5DGE; -.
PDBsum; 5DGF; -.
PDBsum; 5DGV; -.
PDBsum; 5FCI; -.
PDBsum; 5FCJ; -.
PDBsum; 5FL8; -.
PDBsum; 5GAK; -.
PDBsum; 5H4P; -.
PDBsum; 5I4L; -.
PDBsum; 5JCS; -.
PDBsum; 5JUO; -.
PDBsum; 5JUP; -.
PDBsum; 5JUS; -.
PDBsum; 5JUT; -.
PDBsum; 5JUU; -.
PDBsum; 5LYB; -.
PDBsum; 5MC6; -.
PDBsum; 5MEI; -.
PDBsum; 5NDG; -.
PDBsum; 5NDV; -.
PDBsum; 5NDW; -.
PDBsum; 5OBM; -.
PDBsum; 5ON6; -.
PDBsum; 5T62; -.
PDBsum; 5T6R; -.
PDBsum; 5TBW; -.
PDBsum; 5TGA; -.
PDBsum; 5TGM; -.
PDBsum; 6FT6; -.
ProteinModelPortal; P0CX25; -.
SMR; P0CX25; -.
BioGrid; 33849; 134.
BioGrid; 36220; 322.
STRING; 4932.YPR043W; -.
iPTMnet; P0CX25; -.
MaxQB; P0CX25; -.
PaxDb; P0CX25; -.
PRIDE; P0CX25; -.
EnsemblFungi; YJR094W-A; YJR094W-A; YJR094W-A.
EnsemblFungi; YPR043W; YPR043W; YPR043W.
GeneID; 853557; -.
GeneID; 856156; -.
KEGG; sce:YJR094W-A; -.
KEGG; sce:YPR043W; -.
SGD; S000006247; RPL43A.
InParanoid; P0CX25; -.
KO; K02921; -.
OMA; ISTGIWQ; -.
OrthoDB; EOG092C5X8P; -.
BioCyc; YEAST:G3O-34199-MONOMER; -.
Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
Reactome; R-SCE-1799339; SRP-dependent cotranslational protein targeting to membrane.
Reactome; R-SCE-72689; Formation of a pool of free 40S subunits.
Reactome; R-SCE-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
Reactome; R-SCE-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
Reactome; R-SCE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
EvolutionaryTrace; P0CX25; -.
PRO; PR:P0CX25; -.
Proteomes; UP000002311; Chromosome XVI.
ExpressionAtlas; P0CX25; differential.
GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003735; F:structural constituent of ribosome; IC:SGD.
GO; GO:0002181; P:cytoplasmic translation; IC:SGD.
Gene3D; 2.20.25.30; -; 1.
HAMAP; MF_00327; Ribosomal_L37Ae; 1.
InterPro; IPR002674; Ribosomal_L37ae.
InterPro; IPR011331; Ribosomal_L37ae/L37e.
InterPro; IPR011332; Ribosomal_zn-bd.
PANTHER; PTHR43931; PTHR43931; 1.
Pfam; PF01780; Ribosomal_L37ae; 1.
SUPFAM; SSF57829; SSF57829; 1.
TIGRFAMs; TIGR00280; eL43_euk_arch; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Metal-binding;
Phosphoprotein; Reference proteome; Ribonucleoprotein;
Ribosomal protein; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:11983894}.
CHAIN 2 92 60S ribosomal protein L43-A.
/FTId=PRO_0000139838.
ZN_FING 39 60 C4-type.
MOD_RES 40 40 Phosphoserine.
{ECO:0000244|PubMed:17287358}.
HELIX 9 14 {ECO:0000244|PDB:4U4R}.
TURN 15 18 {ECO:0000244|PDB:4U4R}.
HELIX 20 34 {ECO:0000244|PDB:4U4R}.
TURN 40 42 {ECO:0000244|PDB:4U4R}.
STRAND 44 49 {ECO:0000244|PDB:4U4R}.
STRAND 54 57 {ECO:0000244|PDB:4U4R}.
TURN 58 60 {ECO:0000244|PDB:4U4R}.
STRAND 63 65 {ECO:0000244|PDB:4U4R}.
STRAND 68 72 {ECO:0000244|PDB:4U4R}.
HELIX 74 91 {ECO:0000244|PDB:4U4R}.
SEQUENCE 92 AA; 10091 MW; E2057BF56B131730 CRC64;
MAKRTKKVGI TGKYGVRYGS SLRRQVKKLE IQQHARYDCS FCGKKTVKRG AAGIWTCSCC
KKTVAGGAYT VSTAAAATVR STIRRLREMV EA


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