RSSA_DROME
ID RSSA_DROME Reviewed; 270 AA.
AC P38979; Q058X4; Q7KW10; Q9W583; X2JC80;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2018, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=40S ribosomal protein SA {ECO:0000255|HAMAP-Rule:MF_03015};
DE AltName: Full=K14;
DE AltName: Full=Laminin receptor homolog;
DE AltName: Full=Protein stubarista {ECO:0000255|HAMAP-Rule:MF_03015};
GN Name=sta {ECO:0000255|HAMAP-Rule:MF_03015}; ORFNames=CG14792;
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], FUNCTION, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Embryo;
RX PubMed=7916731; DOI=10.1093/genetics/135.2.553;
RA Melnick M.B., Noll E., Perrimon N.;
RT "The Drosophila stubarista phenotype is associated with a dosage effect of
RT the putative ribosome-associated protein D-p40 on spineless.";
RL Genetics 135:553-564(1993).
RN [2]
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]
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oregon-R;
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C.,
RA Celniker S.E.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-270.
RC STRAIN=Canton-S;
RA Kim Y.J., Baker B.S.;
RT "A mammalian laminin receptor homolog from Drosophila.";
RL Submitted (OCT-1991) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP INTERACTION WITH RPS21.
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 [9]
RP SUBCELLULAR LOCATION.
RX PubMed=12150910; DOI=10.1016/s1097-2765(02)00565-8;
RA Brogna S., Sato T., Rosbash M.;
RT "Ribosome components are associated with sites of transcription.";
RL Mol. Cell 10:93-104(2002).
RN [10]
RP ERRATUM OF PUBMED:12150910.
RX PubMed=12455503;
RA Brogna S., Sato T., Rosbash M.;
RL Mol. Cell 10:959-959(2002).
RN [11]
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: Required for the assembly and/or stability of the 40S
CC ribosomal subunit. Required for the processing of the 20S rRNA-
CC precursor to mature 18S rRNA in a late step of the maturation of 40S
CC ribosomal subunits. Required during oogenesis and imaginal development.
CC {ECO:0000255|HAMAP-Rule:MF_03015, ECO:0000269|PubMed:7916731}.
CC -!- SUBUNIT: Component of the small ribosomal subunit. Mature ribosomes
CC consist of a small (40S) and a large (60S) subunit. The 40S subunit
CC contains about 33 different proteins and 1 molecule of RNA (18S). The
CC 60S subunit contains about 49 different proteins and 3 molecules of RNA
CC (28S, 5.8S and 5S). Interacts with oho23B/rpS21. {ECO:0000255|HAMAP-
CC Rule:MF_03015, ECO:0000269|PubMed:10022917}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03015,
CC ECO:0000269|PubMed:12150910}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03015,
CC ECO:0000269|PubMed:12150910}. Note=May associate with nascent RNP
CC complexes within the nucleus.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically in
CC embryos. {ECO:0000269|PubMed:7916731}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS2 family.
CC {ECO:0000255|HAMAP-Rule:MF_03015}.
CC -!- CAUTION: Was originally thought to be a laminin receptor.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA28667.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M90422; AAA28741.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF45638.2; -; Genomic_DNA.
DR EMBL; AE014298; AAN09049.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09050.3; -; Genomic_DNA.
DR EMBL; AL031027; CAA19839.1; -; Genomic_DNA.
DR EMBL; AE014298; AHN59256.1; -; Genomic_DNA.
DR EMBL; AY118899; AAM50759.1; -; mRNA.
DR EMBL; BT029094; ABJ17027.1; -; mRNA.
DR EMBL; M77133; AAA28667.1; ALT_INIT; mRNA.
DR PIR; T13602; T13602.
DR RefSeq; NP_001284785.1; NM_001297856.1.
DR RefSeq; NP_476750.1; NM_057402.5.
DR RefSeq; NP_726744.1; NM_166889.2.
DR RefSeq; NP_726745.3; NM_166890.3.
DR PDB; 4V6W; EM; 6.00 A; AA=1-270.
DR PDB; 6XU6; EM; 3.50 A; AA=6-223.
DR PDB; 6XU7; EM; 4.90 A; AA=6-223.
DR PDB; 6XU8; EM; 3.00 A; AA=6-223.
DR PDBsum; 4V6W; -.
DR PDBsum; 6XU6; -.
DR PDBsum; 6XU7; -.
DR PDBsum; 6XU8; -.
DR AlphaFoldDB; P38979; -.
DR SMR; P38979; -.
DR BioGRID; 57663; 106.
DR DIP; DIP-17178N; -.
DR IntAct; P38979; 3.
DR MINT; P38979; -.
DR STRING; 7227.FBpp0070279; -.
DR PaxDb; P38979; -.
DR PRIDE; P38979; -.
DR DNASU; 31106; -.
DR EnsemblMetazoa; FBtr0070289; FBpp0070277; FBgn0003517.
DR EnsemblMetazoa; FBtr0070290; FBpp0070278; FBgn0003517.
DR EnsemblMetazoa; FBtr0339593; FBpp0308665; FBgn0003517.
DR EnsemblMetazoa; FBtr0339594; FBpp0308666; FBgn0003517.
DR GeneID; 31106; -.
DR KEGG; dme:Dmel_CG14792; -.
DR CTD; 104044; -.
DR FlyBase; FBgn0003517; sta.
DR VEuPathDB; VectorBase:FBgn0003517; -.
DR eggNOG; KOG0830; Eukaryota.
DR GeneTree; ENSGT00950000183099; -.
DR HOGENOM; CLU_058171_1_0_1; -.
DR InParanoid; P38979; -.
DR OMA; QCHLGAK; -.
DR OrthoDB; 1129610at2759; -.
DR PhylomeDB; P38979; -.
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; P38979; -.
DR BioGRID-ORCS; 31106; 1 hit in 1 CRISPR screen.
DR ChiTaRS; sta; fly.
DR GenomeRNAi; 31106; -.
DR PRO; PR:P38979; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0003517; Expressed in seminal fluid secreting gland and 13 other tissues.
DR ExpressionAtlas; P38979; baseline and differential.
DR Genevisible; P38979; 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:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005840; C:ribosome; IDA:FlyBase.
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; IBA:GO_Central.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR CDD; cd01425; RPS2; 1.
DR HAMAP; MF_03015; Ribosomal_S2_euk; 1.
DR InterPro; IPR032281; 40S_SA_C.
DR InterPro; IPR001865; Ribosomal_S2.
DR InterPro; IPR018130; Ribosomal_S2_CS.
DR InterPro; IPR027498; Ribosomal_S2_euk.
DR InterPro; IPR005707; Ribosomal_S2_euk/arc.
DR InterPro; IPR023591; Ribosomal_S2_flav_dom_sf.
DR PANTHER; PTHR11489; PTHR11489; 1.
DR Pfam; PF16122; 40S_SA_C; 1.
DR Pfam; PF00318; Ribosomal_S2; 2.
DR PRINTS; PR00395; RIBOSOMALS2.
DR SUPFAM; SSF52313; SSF52313; 1.
DR TIGRFAMs; TIGR01012; uS2_euk_arch; 1.
DR PROSITE; PS00962; RIBOSOMAL_S2_1; 1.
DR PROSITE; PS00963; RIBOSOMAL_S2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Developmental protein; Nucleus;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..270
FT /note="40S ribosomal protein SA"
FT /id="PRO_0000134353"
FT REGION 214..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 270 AA; 30228 MW; FEC452C3F1712C82 CRC64;
MSGGLDILSL KEDDITKMLV ATTHLGSENV NFQMEQYVYK RRADGVNILN LGKTWEKLQL
AARAIVAIDN PSDIFVISSR PIGQRAVLKF AKYTDTTPIA GRFTPGAFTN QIQPAFREPR
LLVVTDPNTD HQPIMEASYV NIPVIAFTNT DSPLRYIDIA IPCNNKSAHS IGLMWWLLAR
EVLRLRGTIS RSVEWPVVVD LFFYRDPEEA EKEEAAAKEL LPPPKIEEAV DHPVEETTNW
ADEVAAETVG GVEDWNEDTV KTSWGSDGQF
