ID   RS21_DROME              Reviewed;          83 AA.
AC   O76927; A4V027;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 168.
DE   RecName: Full=40S ribosomal protein S21 {ECO:0000303|PubMed:10022917, ECO:0000312|EMBL:CAA08751.1};
DE   AltName: Full=Overgrown hematopoietic organs at 23B {ECO:0000312|EMBL:AAF51191.1};
GN   Name=RpS21; Synonyms=oho23B; ORFNames=CG2986;
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] {ECO:0000305, ECO:0000312|EMBL:CAA08751.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH STA,
RP   SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=10022917; DOI=10.1128/mcb.19.3.2308;
RA   Toeroek I., Herrmann-Horle D., Kiss I., Tick G., Speer G., Schmitt R.,
RA   Mechler B.M.;
RT   "Down-regulation of RpS21, a putative translation initiation factor
RT   interacting with P40, produces viable minute imagos and larval lethality
RT   with overgrown hematopoietic organs and imaginal discs.";
RL   Mol. Cell. Biol. 19:2308-2321(1999).
RN   [2] {ECO:0000312|EMBL:AAF51191.1}
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   [3] {ECO:0000305, ECO:0000312|EMBL:AAF51191.1}
RP   GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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   [4] {ECO:0000305, ECO:0000312|EMBL:AAT94418.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC   STRAIN=Berkeley {ECO:0000312|EMBL:AAT94418.1}; TISSUE=Head;
RA   Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA   Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF THE 80S RIBOSOME,
RP   SUBCELLULAR LOCATION, AND SUBUNIT.
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: May be an associated component of the ribosome rather than a
CC       core structural subunit. May act as a translation initiation factor.
CC       Has a role in regulation of cell proliferation in the hematopoietic
CC       organs and the imaginal disks of larva. {ECO:0000269|PubMed:10022917}.
CC   -!- SUBUNIT: Component of the 40S small ribosomal subunit
CC       (PubMed:23636399). Interacts with sta (PubMed:10022917).
CC       {ECO:0000269|PubMed:10022917, ECO:0000269|PubMed:23636399}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P63220}. Cytoplasm {ECO:0000269|PubMed:10022917,
CC       ECO:0000305|PubMed:23636399}. Rough endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:P63221}. Note=Detected on cytosolic polysomes
CC       (By similarity). Detected in ribosomes that are associated with the
CC       rough endoplasmic reticulum (By similarity).
CC       {ECO:0000250|UniProtKB:P63220, ECO:0000250|UniProtKB:P63221}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A {ECO:0000269|PubMed:10731132}; Synonyms=B
CC       {ECO:0000269|PubMed:10731132};
CC         IsoId=O76927-1; Sequence=Displayed;
CC       Name=E {ECO:0000269|PubMed:10731132};
CC         IsoId=O76927-2; Sequence=VSP_039463;
CC   -!- DEVELOPMENTAL STAGE: Uniformly expressed at all developmental stages.
CC       {ECO:0000269|PubMed:10022917}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS21 family.
CC       {ECO:0000255}.
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DR   EMBL; AJ009557; CAA08751.1; -; Genomic_DNA.
DR   EMBL; AE014134; AAF51191.1; -; Genomic_DNA.
DR   EMBL; AE014134; AAN10392.1; -; Genomic_DNA.
DR   EMBL; AE014134; AAN10393.2; -; Genomic_DNA.
DR   EMBL; BT015189; AAT94418.1; -; mRNA.
DR   RefSeq; NP_001259970.1; NM_001273041.1. [O76927-1]
DR   RefSeq; NP_523462.2; NM_078738.5. [O76927-2]
DR   RefSeq; NP_722853.1; NM_164506.4. [O76927-1]
DR   RefSeq; NP_722854.1; NM_164507.4. [O76927-1]
DR   RefSeq; NP_722855.1; NM_164508.3. [O76927-1]
DR   PDB; 4V6W; EM; 6.00 A; AV=1-83.
DR   PDB; 6XU6; EM; 3.50 A; AV=1-82.
DR   PDB; 6XU7; EM; 4.90 A; AV=1-82.
DR   PDB; 6XU8; EM; 3.00 A; AV=1-82.
DR   PDBsum; 4V6W; -.
DR   PDBsum; 6XU6; -.
DR   PDBsum; 6XU7; -.
DR   PDBsum; 6XU8; -.
DR   AlphaFoldDB; O76927; -.
DR   SMR; O76927; -.
DR   BioGRID; 59710; 136.
DR   IntAct; O76927; 1.
DR   STRING; 7227.FBpp0077309; -.
DR   PaxDb; O76927; -.
DR   PRIDE; O76927; -.
DR   DNASU; 33487; -.
DR   EnsemblMetazoa; FBtr0077621; FBpp0077307; FBgn0015521. [O76927-1]
DR   EnsemblMetazoa; FBtr0077622; FBpp0077308; FBgn0015521. [O76927-1]
DR   EnsemblMetazoa; FBtr0077623; FBpp0077309; FBgn0015521. [O76927-1]
DR   EnsemblMetazoa; FBtr0273293; FBpp0271801; FBgn0015521. [O76927-2]
DR   EnsemblMetazoa; FBtr0335131; FBpp0307130; FBgn0015521. [O76927-1]
DR   GeneID; 33487; -.
DR   KEGG; dme:Dmel_CG2986; -.
DR   UCSC; CG2986-RA; d. melanogaster. [O76927-1]
DR   CTD; 6227; -.
DR   FlyBase; FBgn0015521; RpS21.
DR   VEuPathDB; VectorBase:FBgn0015521; -.
DR   eggNOG; KOG3486; Eukaryota.
DR   GeneTree; ENSGT00390000017515; -.
DR   InParanoid; O76927; -.
DR   OMA; ALCGYIR; -.
DR   PhylomeDB; O76927; -.
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; O76927; -.
DR   BioGRID-ORCS; 33487; 0 hits in 1 CRISPR screen.
DR   ChiTaRS; RpS21; fly.
DR   GenomeRNAi; 33487; -.
DR   PRO; PR:O76927; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0015521; Expressed in eye disc (Drosophila) and 23 other tissues.
DR   ExpressionAtlas; O76927; baseline and differential.
DR   Genevisible; O76927; 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:0005840; C:ribosome; IDA:UniProtKB.
DR   GO; GO:0005791; C:rough endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0043022; F:ribosome binding; IPI:UniProtKB.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR   GO; GO:0002181; P:cytoplasmic translation; TAS:FlyBase.
DR   GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   GO; GO:0000461; P:endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   GO; GO:0048542; P:lymph gland development; IMP:FlyBase.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IMP:UniProtKB.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1230.20; -; 1.
DR   InterPro; IPR001931; Ribosomal_S21e.
DR   InterPro; IPR018279; Ribosomal_S21e_CS.
DR   InterPro; IPR038579; Ribosomal_S21e_sf.
DR   PANTHER; PTHR10442; PTHR10442; 1.
DR   Pfam; PF01249; Ribosomal_S21e; 1.
DR   PIRSF; PIRSF002148; Ribosomal_S21e; 1.
DR   PROSITE; PS00996; RIBOSOMAL_S21E; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Developmental protein;
KW   Endoplasmic reticulum; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein; rRNA processing; Translation regulation.
FT   CHAIN           1..83
FT                   /note="40S ribosomal protein S21"
FT                   /id="PRO_0000395418"
FT   VAR_SEQ         82..83
FT                   /note="Missing (in isoform E)"
FT                   /evidence="ECO:0000303|PubMed:10731132"
FT                   /id="VSP_039463"
SQ   SEQUENCE   83 AA;  9167 MW;  DDFB9D498B3E1E05 CRC64;
     MENDAGENVD LYVPRKCSAS NRIIHAKDHA SVQLSIVDVD PETGRQTDGS KTYAICGEIR
     RMGESDDCIV RLAKKDGIIT KNF