ID RS3_DROME Reviewed; 246 AA.
AC Q06559; Q9VCM9;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 27-MAR-2024, entry version 203.
DE RecName: Full=Small ribosomal subunit protein uS3 {ECO:0000305};
DE AltName: Full=40S ribosomal protein S3;
GN Name=RpS3; Synonyms=M(3)95A; ORFNames=CG6779;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7685082; DOI=10.1093/nar/21.10.2516;
RA Wilson D.M. III, Deutsch W.A., Kelley M.R.;
RT "Cloning of the Drosophila ribosomal protein S3: another multifunctional
RT ribosomal protein with AP endonuclease DNA repair activity.";
RL Nucleic Acids Res. 21:2516-2516(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Shahrinau / Wild-type;
RX PubMed=8070662; DOI=10.1093/genetics/137.2.513;
RA Andersson S., Saeboe-Larssen S., Lambertsson A., Meriam J.,
RA Jacobs-Lorena M.;
RT "A Drosophila third chromosome Minute locus encodes a ribosomal protein.";
RL Genetics 137:513-520(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP DNA REPAIR ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=8641296; DOI=10.1002/j.1460-2075.1996.tb00584.x;
RA Yacoub A., Augeri L., Kelley M.R., Doetsch P.W., Deutsch W.A.;
RT "A Drosophila ribosomal protein contains 8-oxoguanine and abasic site DNA
RT repair activities.";
RL EMBO J. 15:2306-2312(1996).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-223; THR-226 AND SER-241, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [8]
RP INTERACTION WITH LTV1, AND SUBCELLULAR LOCATION.
RX PubMed=25858587; DOI=10.1074/jbc.m114.607036;
RA Kim W., Kim H.D., Jung Y., Kim J., Chung J.;
RT "Drosophila Low Temperature Viability Protein 1 (LTV1) Is Required for
RT Ribosome Biogenesis and Cell Growth Downstream of Drosophila Myc (dMyc).";
RL J. Biol. Chem. 290:13591-13604(2015).
RN [9]
RP STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF THE 80S RIBOSOME.
RX PubMed=23636399; DOI=10.1038/nature12104;
RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA Wilson D.N., Beckmann R.;
RT "Structures of the human and Drosophila 80S ribosome.";
RL Nature 497:80-85(2013).
CC -!- FUNCTION: Has DNA repair activity directed towards the mutagenic
CC lesions 8-oxoguanine and abasic sites in DNA. It can cleave DNA
CC containing 8-oxoguanine residues efficiently. Also acts as an ap lyase,
CC cleaving phosphodiester bonds via a beta,delta elimination reaction.
CC -!- SUBUNIT: Interacts with LTV1; the interaction is RNA-independent.
CC {ECO:0000269|PubMed:25858587}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25858587}. Nucleus
CC {ECO:0000269|PubMed:25858587, ECO:0000269|PubMed:8641296}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS3 family.
CC {ECO:0000305}.
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DR EMBL; L13690; AAA28875.1; -; mRNA.
DR EMBL; X72921; CAA51425.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF56129.1; -; Genomic_DNA.
DR EMBL; AY118971; AAM50831.1; -; mRNA.
DR PIR; S35620; S35620.
DR RefSeq; NP_001287481.1; NM_001300552.1.
DR RefSeq; NP_476632.1; NM_057284.6.
DR PDB; 4V6W; EM; 6.00 A; AD=1-246.
DR PDB; 6XU6; EM; 3.50 A; AD=3-229.
DR PDB; 6XU7; EM; 4.90 A; AD=3-229.
DR PDB; 6XU8; EM; 3.00 A; AD=3-229.
DR PDBsum; 4V6W; -.
DR PDBsum; 6XU6; -.
DR PDBsum; 6XU7; -.
DR PDBsum; 6XU8; -.
DR AlphaFoldDB; Q06559; -.
DR EMDB; EMD-10622; -.
DR EMDB; EMD-10623; -.
DR EMDB; EMD-10624; -.
DR SMR; Q06559; -.
DR BioGRID; 67703; 181.
DR DIP; DIP-17168N; -.
DR IntAct; Q06559; 3.
DR MINT; Q06559; -.
DR STRING; 7227.FBpp0312066; -.
DR MoonProt; Q06559; -.
DR iPTMnet; Q06559; -.
DR PaxDb; 7227-FBpp0083802; -.
DR DNASU; 42761; -.
DR EnsemblMetazoa; FBtr0084410; FBpp0083802; FBgn0002622.
DR EnsemblMetazoa; FBtr0346349; FBpp0312066; FBgn0002622.
DR GeneID; 42761; -.
DR KEGG; dme:Dmel_CG6779; -.
DR AGR; FB:FBgn0002622; -.
DR CTD; 6188; -.
DR FlyBase; FBgn0002622; RpS3.
DR VEuPathDB; VectorBase:FBgn0002622; -.
DR eggNOG; KOG3181; Eukaryota.
DR GeneTree; ENSGT00390000008610; -.
DR HOGENOM; CLU_058591_2_1_1; -.
DR InParanoid; Q06559; -.
DR OMA; NKKKWMI; -.
DR OrthoDB; 5472739at2759; -.
DR PhylomeDB; Q06559; -.
DR Reactome; R-DME-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-DME-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-DME-72649; Translation initiation complex formation.
DR Reactome; R-DME-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-DME-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-DME-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-DME-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-DME-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-DME-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; Q06559; -.
DR BioGRID-ORCS; 42761; 0 hits in 1 CRISPR screen.
DR ChiTaRS; RpS3; fly.
DR GenomeRNAi; 42761; -.
DR PRO; PR:Q06559; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0002622; Expressed in eye disc (Drosophila) and 23 other cell types or tissues.
DR ExpressionAtlas; Q06559; baseline and differential.
DR Genevisible; Q06559; DM.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0016363; C:nuclear matrix; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IDA:FlyBase.
DR GO; GO:0003684; F:damaged DNA binding; IDA:UniProtKB.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0032357; F:oxidized purine DNA binding; IDA:UniProtKB.
DR GO; GO:0008534; F:oxidized purine nucleobase lesion DNA N-glycosylase activity; IDA:FlyBase.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0002181; P:cytoplasmic translation; TAS:FlyBase.
DR GO; GO:0006281; P:DNA repair; IDA:FlyBase.
DR GO; GO:0000278; P:mitotic cell cycle; HMP:FlyBase.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:FlyBase.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IBA:GO_Central.
DR CDD; cd02413; KH-II_40S_S3; 1.
DR Gene3D; 3.30.300.20; -; 1.
DR Gene3D; 3.30.1140.32; Ribosomal protein S3, C-terminal domain; 1.
DR InterPro; IPR015946; KH_dom-like_a/b.
DR InterPro; IPR004044; KH_dom_type_2.
DR InterPro; IPR009019; KH_sf_prok-type.
DR InterPro; IPR036419; Ribosomal_S3_C_sf.
DR InterPro; IPR001351; Ribosomal_uS3_C.
DR InterPro; IPR018280; Ribosomal_uS3_CS.
DR InterPro; IPR005703; Ribosomal_uS3_euk/arc.
DR NCBIfam; TIGR01008; uS3_euk_arch; 1.
DR PANTHER; PTHR11760; 30S/40S RIBOSOMAL PROTEIN S3; 1.
DR PANTHER; PTHR11760:SF32; 40S RIBOSOMAL PROTEIN S3; 1.
DR Pfam; PF07650; KH_2; 1.
DR Pfam; PF00189; Ribosomal_S3_C; 1.
DR SUPFAM; SSF54814; Prokaryotic type KH domain (KH-domain type II); 1.
DR SUPFAM; SSF54821; Ribosomal protein S3 C-terminal domain; 1.
DR PROSITE; PS50823; KH_TYPE_2; 1.
DR PROSITE; PS00548; RIBOSOMAL_S3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA damage; DNA repair; Endonuclease; Hydrolase;
KW Nuclease; Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding.
FT CHAIN 1..246
FT /note="Small ribosomal subunit protein uS3"
FT /id="PRO_0000130328"
FT DOMAIN 23..94
FT /note="KH type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00118"
FT REGION 201..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 223
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 226
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 46..47
FT /note="SR -> FG (in Ref. 2; CAA51425)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="G -> A (in Ref. 2; CAA51425)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="G -> E (in Ref. 2; CAA51425)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 246 AA; 27471 MW; 122A6E775339E673 CRC64;
MNANLPISKK RKFVSDGIFK AELNEFLTRE LAEDGYSGVE VRVTPSRTEI IIMATKTQQV
LGEKGRRIRE LTAMVQKRFN FETGRIELYA EKVAARGLCA IAQAESLRYK LTGGLAVRRA
CYGVLRYIME SGAKGCEVVV SGKLRGQRAK SMKFVDGLMI HSGDPCNDYV ETATRHVLLR
QGVLGIKVKV MLPYDPKNKI GPKKPLPDNV SVVEPKEEKI YETPETEYKI PPPSKPLDDL
SEAKVL
//
