RL3_YEAST
ID RL3_YEAST Reviewed; 387 AA.
AC P14126; D6W2C6; Q08459;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=60S ribosomal protein L3 {ECO:0000303|PubMed:9559554};
DE AltName: Full=Large ribosomal subunit protein uL3 {ECO:0000303|PubMed:24524803};
DE AltName: Full=Maintenance of killer protein 8;
DE AltName: Full=RP1;
DE AltName: Full=Trichodermin resistance protein;
DE AltName: Full=YL1;
GN Name=RPL3 {ECO:0000303|PubMed:9559554}; Synonyms=MAK8, TCM1;
GN OrderedLocusNames=YOR063W; ORFNames=YOR29-14;
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], AND DISRUPTION PHENOTYPE.
RC STRAIN=CLP1;
RX PubMed=6305925; DOI=10.1128/jb.155.1.8-14.1983;
RA Schultz L.D., Friesen J.D.;
RT "Nucleotide sequence of the tcm1 gene (ribosomal protein L3) of
RT Saccharomyces cerevisiae.";
RL J. Bacteriol. 155:8-14(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9133743;
RX DOI=10.1002/(sici)1097-0061(19970330)13:4<379::aid-yea85>3.0.co;2-g;
RA Valens M., Bohn C., Daignan-Fornier B., Dang V.-D., Bolotin-Fukuhara M.;
RT "The sequence of a 54.7 kb fragment of yeast chromosome XV reveals the
RT presence of two tRNAs and 24 new open reading frames.";
RL Yeast 13:379-390(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
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 [5]
RP PROTEIN SEQUENCE OF 2-20.
RX PubMed=6355773; DOI=10.1007/bf00425772;
RA Otaka E., Higo K., Itoh T.;
RT "Yeast ribosomal proteins: VII. Cytoplasmic ribosomal proteins from
RT Schizosaccharomyces pombe.";
RL Mol. Gen. Genet. 191:519-524(1983).
RN [6]
RP PROTEIN SEQUENCE OF 2-10.
RX PubMed=1544921; DOI=10.1016/s0021-9258(18)42785-8;
RA Takakura H., Tsunasawa S., Miyagi M., Warner J.R.;
RT "NH2-terminal acetylation of ribosomal proteins of Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 267:5442-5445(1992).
RN [7]
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 [8]
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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-103, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-156, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [14]
RP METHYLATION AT HIS-243.
RX PubMed=20864530; DOI=10.1074/jbc.m110.170787;
RA Webb K.J., Zurita-Lopez C.I., Al-Hadid Q., Laganowsky A., Young B.D.,
RA Lipson R.S., Souda P., Faull K.F., Whitelegge J.P., Clarke S.G.;
RT "A novel 3-methylhistidine modification of yeast ribosomal protein Rpl3 is
RT dependent upon the YIL110W methyltransferase.";
RL J. Biol. Chem. 285:37598-37606(2010).
RN [15]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-39 AND LYS-136, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [16]
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 [17]
RP FUNCTION, AND METHYLATION AT HIS-243.
RX PubMed=24865971; DOI=10.1128/mcb.01634-13;
RA Al-Hadid Q., Roy K., Munroe W., Dzialo M.C., Chanfreau G.F., Clarke S.G.;
RT "Histidine methylation of yeast ribosomal protein Rpl3p is required for
RT proper 60S subunit assembly.";
RL Mol. Cell. Biol. 34:2903-2916(2014).
RN [18]
RP METHYLATION AT HIS-243, AND MUTAGENESIS OF HIS-243.
RX PubMed=26826131; DOI=10.1261/rna.054569.115;
RA Al-Hadid Q., Roy K., Chanfreau G., Clarke S.G.;
RT "Methylation of yeast ribosomal protein Rpl3 promotes translational
RT elongation fidelity.";
RL RNA 22:489-498(2016).
RN [19]
RP 3D-STRUCTURE MODELING OF 8-366, AND ELECTRON MICROSCOPY.
RX PubMed=11701127; DOI=10.1016/s0092-8674(01)00539-6;
RA Spahn C.M.T., Beckmann R., Eswar N., Penczek P.A., Sali A., Blobel G.,
RA Frank J.;
RT "Structure of the 80S ribosome from Saccharomyces cerevisiae -- tRNA-
RT ribosome and subunit-subunit interactions.";
RL Cell 107:373-386(2001).
RN [20]
RP 3D-STRUCTURE MODELING, AND ELECTRON MICROSCOPY.
RX PubMed=14976550; DOI=10.1038/sj.emboj.7600102;
RA Spahn C.M.T., Gomez-Lorenzo M.G., Grassucci R.A., Joergensen R.,
RA Andersen G.R., Beckmann R., Penczek P.A., Ballesta J.P.G., Frank J.;
RT "Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome
RT facilitate tRNA translocation.";
RL EMBO J. 23:1008-1019(2004).
RN [21]
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 [22]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 80S RIBOSOME, FUNCTION, SUBUNIT,
RP AND 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 (PubMed:24865971,
CC PubMed:22096102). The small ribosomal subunit (SSU) binds messenger
CC RNAs (mRNAs) and translates the encoded message by selecting cognate
CC aminoacyl-transfer RNA (tRNA) molecules (PubMed:22096102). The large
CC subunit (LSU) contains the ribosomal catalytic site termed the peptidyl
CC transferase center (PTC), which catalyzes the formation of peptide
CC bonds, thereby polymerizing the amino acids delivered by tRNAs into a
CC polypeptide chain (PubMed:22096102). The nascent polypeptides leave the
CC ribosome through a tunnel in the LSU and interact with protein factors
CC that function in enzymatic processing, targeting, and the membrane
CC insertion of nascent chains at the exit of the ribosomal tunnel
CC (PubMed:22096102). uL3 plays a role in coordinating processes of
CC accommodating the aminoacyl-tRNA in the PTC (PubMed:22096102).
CC {ECO:0000269|PubMed:22096102, ECO:0000269|PubMed:24865971}.
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). uL3 forms together with ES39L one of
CC the contact sites for the signal recognition particle that targets
CC ribosomes to the endoplasmic reticulum membrane (PubMed:9559554,
CC PubMed:24865971, PubMed:22096102). {ECO:0000269|PubMed:22096102,
CC ECO:0000269|PubMed:24865971, ECO:0000305|PubMed:9559554}.
CC -!- INTERACTION:
CC P14126; P17555: SRV2; NbExp=3; IntAct=EBI-15364, EBI-4024;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:22096102}.
CC -!- PTM: Methylation at His-243 by HPM1 is required for proper 60S subunit
CC assembly and promotes translational elongation fidelity.
CC {ECO:0000269|PubMed:24865971, ECO:0000269|PubMed:26826131}.
CC -!- DISRUPTION PHENOTYPE: A mutant confers resistance to trichodermin, a
CC trichotecene toxin produced by plant-pathogenic fungi.
CC {ECO:0000269|PubMed:6305925}.
CC -!- MISCELLANEOUS: Present with 450 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL3 family.
CC {ECO:0000305}.
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DR EMBL; J01351; AAA88732.1; -; Genomic_DNA.
DR EMBL; Z74971; CAA99256.1; -; Genomic_DNA.
DR EMBL; Z70678; CAA94548.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10842.1; -; Genomic_DNA.
DR PIR; S66946; R5BY4E.
DR RefSeq; NP_014706.1; NM_001183482.1.
DR PDB; 3J6X; EM; 6.10 A; L3=1-387.
DR PDB; 3J6Y; EM; 6.10 A; L3=1-387.
DR PDB; 3J77; EM; 6.20 A; L3=1-387.
DR PDB; 3J78; EM; 6.30 A; L3=1-387.
DR PDB; 3JCT; EM; 3.08 A; B=1-387.
DR PDB; 4U3M; X-ray; 3.00 A; L3/l3=2-387.
DR PDB; 4U3N; X-ray; 3.20 A; L3/l3=2-387.
DR PDB; 4U3U; X-ray; 2.90 A; L3/l3=2-387.
DR PDB; 4U4N; X-ray; 3.10 A; L3/l3=2-387.
DR PDB; 4U4O; X-ray; 3.60 A; L3/l3=2-387.
DR PDB; 4U4Q; X-ray; 3.00 A; L3/l3=2-387.
DR PDB; 4U4R; X-ray; 2.80 A; L3/l3=2-387.
DR PDB; 4U4U; X-ray; 3.00 A; L3/l3=2-387.
DR PDB; 4U4Y; X-ray; 3.20 A; L3/l3=2-387.
DR PDB; 4U4Z; X-ray; 3.10 A; L3/l3=2-387.
DR PDB; 4U50; X-ray; 3.20 A; L3/l3=2-387.
DR PDB; 4U51; X-ray; 3.20 A; L3/l3=2-387.
DR PDB; 4U52; X-ray; 3.00 A; L3/l3=2-387.
DR PDB; 4U53; X-ray; 3.30 A; L3/l3=2-387.
DR PDB; 4U55; X-ray; 3.20 A; L3/l3=2-387.
DR PDB; 4U56; X-ray; 3.45 A; L3/l3=2-387.
DR PDB; 4U6F; X-ray; 3.10 A; L3/l3=2-387.
DR PDB; 4V4B; EM; 11.70 A; BC=2-387.
DR PDB; 4V6I; EM; 8.80 A; BC=1-387.
DR PDB; 4V7F; EM; 8.70 A; C=1-387.
DR PDB; 4V7R; X-ray; 4.00 A; BC/DC=1-387.
DR PDB; 4V88; X-ray; 3.00 A; BB/DB=1-387.
DR PDB; 4V8T; EM; 8.10 A; B=1-387.
DR PDB; 4V8Y; EM; 4.30 A; BB=2-387.
DR PDB; 4V8Z; EM; 6.60 A; BB=2-387.
DR PDB; 4V91; EM; 3.70 A; B=1-387.
DR PDB; 5APN; EM; 3.91 A; B=1-387.
DR PDB; 5APO; EM; 3.41 A; B=1-387.
DR PDB; 5DAT; X-ray; 3.15 A; L3/l3=2-387.
DR PDB; 5DC3; X-ray; 3.25 A; L3/l3=2-387.
DR PDB; 5DGE; X-ray; 3.45 A; L3/l3=2-387.
DR PDB; 5DGF; X-ray; 3.30 A; L3/l3=2-387.
DR PDB; 5DGV; X-ray; 3.10 A; L3/l3=2-387.
DR PDB; 5FCI; X-ray; 3.40 A; L3/l3=2-387.
DR PDB; 5FCJ; X-ray; 3.10 A; L3/l3=2-387.
DR PDB; 5FL8; EM; 9.50 A; B=1-387.
DR PDB; 5GAK; EM; 3.88 A; F=1-387.
DR PDB; 5H4P; EM; 3.07 A; B=1-387.
DR PDB; 5I4L; X-ray; 3.10 A; L3/l3=2-387.
DR PDB; 5JCS; EM; 9.50 A; B=1-387.
DR PDB; 5JUO; EM; 4.00 A; G=1-387.
DR PDB; 5JUP; EM; 3.50 A; G=1-387.
DR PDB; 5JUS; EM; 4.20 A; G=1-387.
DR PDB; 5JUT; EM; 4.00 A; G=1-387.
DR PDB; 5JUU; EM; 4.00 A; G=1-387.
DR PDB; 5LYB; X-ray; 3.25 A; L3/l3=2-387.
DR PDB; 5M1J; EM; 3.30 A; B5=2-387.
DR PDB; 5MC6; EM; 3.80 A; BA=1-387.
DR PDB; 5MEI; X-ray; 3.50 A; CE/k=2-387.
DR PDB; 5NDG; X-ray; 3.70 A; L3/l3=2-387.
DR PDB; 5NDV; X-ray; 3.30 A; L3/l3=2-387.
DR PDB; 5NDW; X-ray; 3.70 A; L3/l3=2-387.
DR PDB; 5OBM; X-ray; 3.40 A; L3/l3=2-387.
DR PDB; 5ON6; X-ray; 3.10 A; CE/k=2-387.
DR PDB; 5T62; EM; 3.30 A; E=1-387.
DR PDB; 5T6R; EM; 4.50 A; E=1-387.
DR PDB; 5TBW; X-ray; 3.00 A; CE/k=2-387.
DR PDB; 5TGA; X-ray; 3.30 A; L3/l3=2-387.
DR PDB; 5TGM; X-ray; 3.50 A; L3/l3=2-387.
DR PDB; 5Z3G; EM; 3.65 A; F=1-387.
DR PDB; 6C0F; EM; 3.70 A; B=1-387.
DR PDB; 6ELZ; EM; 3.30 A; B=1-387.
DR PDB; 6EM1; EM; 3.60 A; B=1-387.
DR PDB; 6EM4; EM; 4.10 A; B=1-387.
DR PDB; 6EM5; EM; 4.30 A; B=1-387.
DR PDB; 6FT6; EM; 3.90 A; B=1-387.
DR PDB; 6GQ1; EM; 4.40 A; B=2-387.
DR PDB; 6GQB; EM; 3.90 A; B=2-387.
DR PDB; 6GQV; EM; 4.00 A; B=2-387.
DR PDB; 6HD7; EM; 3.40 A; F=1-387.
DR PDB; 6HHQ; X-ray; 3.10 A; CE/k=1-387.
DR PDB; 6I7O; EM; 5.30 A; BA/YA=2-387.
DR PDB; 6M62; EM; 3.20 A; B=1-387.
DR PDB; 6N8J; EM; 3.50 A; B=1-387.
DR PDB; 6N8K; EM; 3.60 A; B=1-387.
DR PDB; 6N8L; EM; 3.60 A; B=1-387.
DR PDB; 6N8M; EM; 3.50 A; E=1-387.
DR PDB; 6N8N; EM; 3.80 A; E=1-387.
DR PDB; 6N8O; EM; 3.50 A; E=1-387.
DR PDB; 6OIG; EM; 3.80 A; B=2-387.
DR PDB; 6Q8Y; EM; 3.10 A; BA=2-387.
DR PDB; 6QIK; EM; 3.10 A; C=1-387.
DR PDB; 6QT0; EM; 3.40 A; C=1-387.
DR PDB; 6QTZ; EM; 3.50 A; C=1-387.
DR PDB; 6R84; EM; 3.60 A; F=2-387.
DR PDB; 6R86; EM; 3.40 A; F=2-387.
DR PDB; 6R87; EM; 3.40 A; F=2-387.
DR PDB; 6RI5; EM; 3.30 A; C=1-387.
DR PDB; 6RZZ; EM; 3.20 A; C=1-387.
DR PDB; 6S05; EM; 3.90 A; C=1-387.
DR PDB; 6S47; EM; 3.28 A; AE=2-387.
DR PDB; 6SNT; EM; 2.80 A; i=1-387.
DR PDB; 6SV4; EM; 3.30 A; BA/YA/ZA=1-387.
DR PDB; 6T4Q; EM; 2.60 A; LB=2-387.
DR PDB; 6T7I; EM; 3.20 A; LB=1-387.
DR PDB; 6T7T; EM; 3.10 A; LB=1-387.
DR PDB; 6T83; EM; 4.00 A; By/Ea=1-387.
DR PDB; 6TB3; EM; 2.80 A; BA=2-387.
DR PDB; 6TNU; EM; 3.10 A; BA=2-387.
DR PDB; 6WOO; EM; 2.90 A; B=2-385.
DR PDB; 6YLG; EM; 3.00 A; B=1-387.
DR PDB; 6YLH; EM; 3.10 A; B=1-387.
DR PDB; 6YLX; EM; 3.90 A; B=1-387.
DR PDB; 6YLY; EM; 3.80 A; B=1-387.
DR PDB; 6Z6J; EM; 3.40 A; LB=1-387.
DR PDB; 6Z6K; EM; 3.40 A; LB=1-387.
DR PDB; 7AZY; EM; 2.88 A; l=1-387.
DR PDB; 7B7D; EM; 3.30 A; LE=2-387.
DR PDB; 7BT6; EM; 3.12 A; B=1-387.
DR PDB; 7BTB; EM; 3.22 A; B=1-387.
DR PDB; 7NRC; EM; 3.90 A; LE=2-387.
DR PDB; 7NRD; EM; 4.36 A; LE=2-387.
DR PDB; 7OF1; EM; 3.10 A; B=1-387.
DR PDB; 7OH3; EM; 3.40 A; B=1-387.
DR PDB; 7OHP; EM; 3.90 A; B=1-387.
DR PDB; 7OHQ; EM; 3.10 A; B=1-387.
DR PDB; 7OHR; EM; 4.72 A; B=1-387.
DR PDB; 7OHS; EM; 4.38 A; B=1-387.
DR PDB; 7OHT; EM; 4.70 A; B=1-387.
DR PDB; 7OHU; EM; 3.70 A; B=1-387.
DR PDB; 7OHV; EM; 3.90 A; B=1-387.
DR PDB; 7OHW; EM; 3.50 A; B=1-387.
DR PDB; 7OHX; EM; 3.30 A; B=1-387.
DR PDB; 7OHY; EM; 3.90 A; B=1-387.
DR PDBsum; 3J6X; -.
DR PDBsum; 3J6Y; -.
DR PDBsum; 3J77; -.
DR PDBsum; 3J78; -.
DR PDBsum; 3JCT; -.
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; 4U50; -.
DR PDBsum; 4U51; -.
DR PDBsum; 4U52; -.
DR PDBsum; 4U53; -.
DR PDBsum; 4U55; -.
DR PDBsum; 4U56; -.
DR PDBsum; 4U6F; -.
DR PDBsum; 4V4B; -.
DR PDBsum; 4V6I; -.
DR PDBsum; 4V7F; -.
DR PDBsum; 4V7R; -.
DR PDBsum; 4V88; -.
DR PDBsum; 4V8T; -.
DR PDBsum; 4V8Y; -.
DR PDBsum; 4V8Z; -.
DR PDBsum; 4V91; -.
DR PDBsum; 5APN; -.
DR PDBsum; 5APO; -.
DR PDBsum; 5DAT; -.
DR PDBsum; 5DC3; -.
DR PDBsum; 5DGE; -.
DR PDBsum; 5DGF; -.
DR PDBsum; 5DGV; -.
DR PDBsum; 5FCI; -.
DR PDBsum; 5FCJ; -.
DR PDBsum; 5FL8; -.
DR PDBsum; 5GAK; -.
DR PDBsum; 5H4P; -.
DR PDBsum; 5I4L; -.
DR PDBsum; 5JCS; -.
DR PDBsum; 5JUO; -.
DR PDBsum; 5JUP; -.
DR PDBsum; 5JUS; -.
DR PDBsum; 5JUT; -.
DR PDBsum; 5JUU; -.
DR PDBsum; 5LYB; -.
DR PDBsum; 5M1J; -.
DR PDBsum; 5MC6; -.
DR PDBsum; 5MEI; -.
DR PDBsum; 5NDG; -.
DR PDBsum; 5NDV; -.
DR PDBsum; 5NDW; -.
DR PDBsum; 5OBM; -.
DR PDBsum; 5ON6; -.
DR PDBsum; 5T62; -.
DR PDBsum; 5T6R; -.
DR PDBsum; 5TBW; -.
DR PDBsum; 5TGA; -.
DR PDBsum; 5TGM; -.
DR PDBsum; 5Z3G; -.
DR PDBsum; 6C0F; -.
DR PDBsum; 6ELZ; -.
DR PDBsum; 6EM1; -.
DR PDBsum; 6EM4; -.
DR PDBsum; 6EM5; -.
DR PDBsum; 6FT6; -.
DR PDBsum; 6GQ1; -.
DR PDBsum; 6GQB; -.
DR PDBsum; 6GQV; -.
DR PDBsum; 6HD7; -.
DR PDBsum; 6HHQ; -.
DR PDBsum; 6I7O; -.
DR PDBsum; 6M62; -.
DR PDBsum; 6N8J; -.
DR PDBsum; 6N8K; -.
DR PDBsum; 6N8L; -.
DR PDBsum; 6N8M; -.
DR PDBsum; 6N8N; -.
DR PDBsum; 6N8O; -.
DR PDBsum; 6OIG; -.
DR PDBsum; 6Q8Y; -.
DR PDBsum; 6QIK; -.
DR PDBsum; 6QT0; -.
DR PDBsum; 6QTZ; -.
DR PDBsum; 6R84; -.
DR PDBsum; 6R86; -.
DR PDBsum; 6R87; -.
DR PDBsum; 6RI5; -.
DR PDBsum; 6RZZ; -.
DR PDBsum; 6S05; -.
DR PDBsum; 6S47; -.
DR PDBsum; 6SNT; -.
DR PDBsum; 6SV4; -.
DR PDBsum; 6T4Q; -.
DR PDBsum; 6T7I; -.
DR PDBsum; 6T7T; -.
DR PDBsum; 6T83; -.
DR PDBsum; 6TB3; -.
DR PDBsum; 6TNU; -.
DR PDBsum; 6WOO; -.
DR PDBsum; 6YLG; -.
DR PDBsum; 6YLH; -.
DR PDBsum; 6YLX; -.
DR PDBsum; 6YLY; -.
DR PDBsum; 6Z6J; -.
DR PDBsum; 6Z6K; -.
DR PDBsum; 7AZY; -.
DR PDBsum; 7B7D; -.
DR PDBsum; 7BT6; -.
DR PDBsum; 7BTB; -.
DR PDBsum; 7NRC; -.
DR PDBsum; 7NRD; -.
DR PDBsum; 7OF1; -.
DR PDBsum; 7OH3; -.
DR PDBsum; 7OHP; -.
DR PDBsum; 7OHQ; -.
DR PDBsum; 7OHR; -.
DR PDBsum; 7OHS; -.
DR PDBsum; 7OHT; -.
DR PDBsum; 7OHU; -.
DR PDBsum; 7OHV; -.
DR PDBsum; 7OHW; -.
DR PDBsum; 7OHX; -.
DR PDBsum; 7OHY; -.
DR AlphaFoldDB; P14126; -.
DR SMR; P14126; -.
DR BioGRID; 34462; 347.
DR ComplexPortal; CPX-1601; 60S cytosolic large ribosomal subunit.
DR DIP; DIP-6264N; -.
DR IntAct; P14126; 113.
DR MINT; P14126; -.
DR STRING; 4932.YOR063W; -.
DR CarbonylDB; P14126; -.
DR iPTMnet; P14126; -.
DR MaxQB; P14126; -.
DR PaxDb; P14126; -.
DR PRIDE; P14126; -.
DR EnsemblFungi; YOR063W_mRNA; YOR063W; YOR063W.
DR GeneID; 854229; -.
DR KEGG; sce:YOR063W; -.
DR SGD; S000005589; RPL3.
DR VEuPathDB; FungiDB:YOR063W; -.
DR eggNOG; KOG0746; Eukaryota.
DR GeneTree; ENSGT00390000017606; -.
DR HOGENOM; CLU_033361_2_1_1; -.
DR InParanoid; P14126; -.
DR OMA; HQRTEYN; -.
DR BioCyc; YEAST:G3O-33603-MON; -.
DR Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-SCE-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-SCE-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-SCE-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-SCE-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-SCE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR EvolutionaryTrace; P14126; -.
DR PRO; PR:P14126; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P14126; protein.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:1990145; P:maintenance of translational fidelity; IMP:SGD.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IMP:SGD.
DR GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR Gene3D; 4.10.960.10; -; 1.
DR InterPro; IPR045077; L3_arc_euk.
DR InterPro; IPR000597; Ribosomal_L3.
DR InterPro; IPR019926; Ribosomal_L3_CS.
DR InterPro; IPR044892; Ribosomal_L3_dom_3_arc_sf.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR11363; PTHR11363; 1.
DR Pfam; PF00297; Ribosomal_L3; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR PROSITE; PS00474; RIBOSOMAL_L3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Isopeptide bond;
KW Methylation; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1544921,
FT ECO:0000269|PubMed:6355773"
FT CHAIN 2..387
FT /note="60S ribosomal protein L3"
FT /id="PRO_0000077251"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 103
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 243
FT /note="Pros-methylhistidine"
FT /evidence="ECO:0000269|PubMed:20864530,
FT ECO:0000269|PubMed:24865971, ECO:0000269|PubMed:26826131"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CROSSLNK 39
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 136
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 243
FT /note="H->A: Cells accumulate 35S and 23S pre-rRNA
FT precursors. Cells display defects in translation elongation
FT resulting in decreased translational accuracy."
FT /evidence="ECO:0000269|PubMed:26826131"
FT CONFLICT 255
FT /note="W -> C (in Ref. 1; AAA88732)"
FT /evidence="ECO:0000305"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:4U52"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:4U53"
FT STRAND 44..59
FT /evidence="ECO:0007829|PDB:4U4R"
FT TURN 66..69
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 70..80
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 84..93
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:4U4R"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:4U4R"
FT TURN 129..133
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 142..153
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 156..163
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:4U6F"
FT HELIX 188..197
FT /evidence="ECO:0007829|PDB:4U4R"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:4U3U"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 214..220
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 229..233
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 274..286
FT /evidence="ECO:0007829|PDB:4U4R"
FT TURN 291..294
FT /evidence="ECO:0007829|PDB:4U4R"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:4U4R"
FT TURN 312..314
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 321..326
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 335..340
FT /evidence="ECO:0007829|PDB:4U4R"
FT TURN 349..351
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 356..359
FT /evidence="ECO:0007829|PDB:4U4R"
FT TURN 364..367
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 373..380
FT /evidence="ECO:0007829|PDB:4U4R"
SQ SEQUENCE 387 AA; 43758 MW; 986769A218E9698A CRC64;
MSHRKYEAPR HGHLGFLPRK RAASIRARVK AFPKDDRSKP VALTSFLGYK AGMTTIVRDL
DRPGSKFHKR EVVEAVTVVD TPPVVVVGVV GYVETPRGLR SLTTVWAEHL SDEVKRRFYK
NWYKSKKKAF TKYSAKYAQD GAGIERELAR IKKYASVVRV LVHTQIRKTP LAQKKAHLAE
IQLNGGSISE KVDWAREHFE KTVAVDSVFE QNEMIDAIAV TKGHGFEGVT HRWGTKKLPR
KTHRGLRKVA CIGAWHPAHV MWSVARAGQR GYHSRTSINH KIYRVGKGDD EANGATSFDR
TKKTITPMGG FVHYGEIKND FIMVKGCIPG NRKRIVTLRK SLYTNTSRKA LEEVSLKWID
TASKFGKGRF QTPAEKHAFM GTLKKDL
