RS2_DROME
ID RS2_DROME Reviewed; 267 AA.
AC P31009; Q9VL74;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=40S ribosomal protein S2;
DE AltName: Full=Protein strings of pearls;
GN Name=RpS2; Synonyms=sop; ORFNames=CG5920;
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 [GENOMIC DNA / MRNA].
RC STRAIN=Canton-S;
RX PubMed=8441641; DOI=10.1093/nar/21.2.351;
RA Barrio R., del Arco A., Cabrera H.L., Arribas C.;
RT "Cloning and analysis of the S2 ribosomal protein cDNA from Drosophila.";
RL Nucleic Acids Res. 21:351-351(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=7982558; DOI=10.1093/genetics/137.4.1039;
RA Cramton S.E., Laski F.A.;
RT "String of pearls encodes Drosophila ribosomal protein S2, has Minute-like
RT characteristics, and is required during oogenesis.";
RL Genetics 137:1039-1048(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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY
RP 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 [7]
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: 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. Plays a role in the assembly and function of the 40S ribosomal
CC subunit. Mutations in this protein affects the control of translational
CC fidelity. Involved in nucleolar processing of pre-18S ribosomal RNA and
CC ribosome assembly (By similarity). Has a specific developmental role
CC during oogenesis (PubMed:7982558). {ECO:0000250|UniProtKB:P25443,
CC ECO:0000269|PubMed:7982558}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS5 family.
CC {ECO:0000305}.
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DR EMBL; U01334; AAC34198.1; -; mRNA.
DR EMBL; U01335; AAA87053.1; -; Genomic_DNA.
DR EMBL; X69120; CAA48872.1; -; mRNA.
DR EMBL; AE014134; AAF52822.1; -; Genomic_DNA.
DR EMBL; AY094799; AAM11152.1; -; mRNA.
DR PIR; S30395; S30395.
DR RefSeq; NP_001260303.1; NM_001273374.2.
DR RefSeq; NP_001285785.1; NM_001298856.1.
DR RefSeq; NP_476874.1; NM_057526.5.
DR PDB; 4V6W; EM; 6.00 A; AC=1-267.
DR PDB; 6XU6; EM; 3.50 A; AC=38-264.
DR PDB; 6XU7; EM; 4.90 A; AC=38-264.
DR PDB; 6XU8; EM; 3.00 A; AC=38-264.
DR PDBsum; 4V6W; -.
DR PDBsum; 6XU6; -.
DR PDBsum; 6XU7; -.
DR PDBsum; 6XU8; -.
DR AlphaFoldDB; P31009; -.
DR SMR; P31009; -.
DR BioGRID; 60403; 112.
DR DIP; DIP-18767N; -.
DR IntAct; P31009; 9.
DR MINT; P31009; -.
DR STRING; 7227.FBpp0079500; -.
DR iPTMnet; P31009; -.
DR PaxDb; P31009; -.
DR PRIDE; P31009; -.
DR EnsemblMetazoa; FBtr0079905; FBpp0079500; FBgn0004867.
DR EnsemblMetazoa; FBtr0330682; FBpp0303531; FBgn0004867.
DR EnsemblMetazoa; FBtr0345436; FBpp0311561; FBgn0004867.
DR GeneID; 34309; -.
DR KEGG; dme:Dmel_CG5920; -.
DR CTD; 6187; -.
DR FlyBase; FBgn0004867; RpS2.
DR VEuPathDB; VectorBase:FBgn0004867; -.
DR eggNOG; KOG0877; Eukaryota.
DR GeneTree; ENSGT00940000153095; -.
DR HOGENOM; CLU_065898_0_2_1; -.
DR InParanoid; P31009; -.
DR OMA; DLKNWVP; -.
DR OrthoDB; 1197354at2759; -.
DR PhylomeDB; P31009; -.
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-3214858; RMTs methylate histone arginines.
DR Reactome; R-DME-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
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-8876725; Protein methylation.
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; P31009; -.
DR BioGRID-ORCS; 34309; 1 hit in 1 CRISPR screen.
DR ChiTaRS; RpS2; fly.
DR GenomeRNAi; 34309; -.
DR PRO; PR:P31009; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0004867; Expressed in secondary oocyte and 22 other tissues.
DR ExpressionAtlas; P31009; baseline and differential.
DR Genevisible; P31009; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:FlyBase.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0002181; P:cytoplasmic translation; TAS:FlyBase.
DR GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR000851; Ribosomal_S5.
DR InterPro; IPR005324; Ribosomal_S5_C.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR005711; Ribosomal_S5_euk/arc.
DR InterPro; IPR013810; Ribosomal_S5_N.
DR InterPro; IPR018192; Ribosomal_S5_N_CS.
DR PANTHER; PTHR13718; PTHR13718; 1.
DR Pfam; PF00333; Ribosomal_S5; 1.
DR Pfam; PF03719; Ribosomal_S5_C; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR TIGRFAMs; TIGR01020; uS5_euk_arch; 1.
DR PROSITE; PS00585; RIBOSOMAL_S5; 1.
DR PROSITE; PS50881; S5_DSRBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Developmental protein; Differentiation; Oogenesis;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..267
FT /note="40S ribosomal protein S2"
FT /id="PRO_0000131679"
FT DOMAIN 85..148
FT /note="S5 DRBM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00268"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 19..20
FT /note="GG -> PP (in Ref. 1; CAA48872)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="K -> R (in Ref. 1; CAA48872)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 267 AA; 28900 MW; ADA22CD28F100743 CRC64;
MADEAPARSG FRGGFGSRGG RGGRGRGRGR WARGRGKEDS KEWVPVTKLG RLVREGKIKS
LEEIYLYSLP IKEFEIIDFF LGSSLKDEVL KIMPVQKQTR AGQRTRFKAF VAIGDNNGHI
GLGVKCSKEV ATAIRGAIIL AKLSVVPVRR GYWGNKIGKP HTVPCKVTGK CGSVSVRLIP
APRGTGIVSA PVPKKLLTMA GIEDCYTSAR GSTGTLGNFA KATYAAIAKT YAYLTPDLWK
EMPLGSTPYQ AYSDFLSKPT PRLHADA
