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Protein

40S ribosomal protein SA

Gene

sta

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Required during oogenesis and imaginal development.UniRule annotation1 Publication

GO - Molecular functioni

  • ribosome binding Source: UniProtKB
  • structural constituent of ribosome Source: FlyBase

GO - Biological processi

  • mitotic spindle elongation Source: FlyBase
  • mitotic spindle organization Source: FlyBase
  • multicellular organism development Source: UniProtKB-KW
  • ribosomal small subunit assembly Source: UniProtKB-HAMAP
  • translation Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiR-DME-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-DME-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-DME-6791226. Major pathway of rRNA processing in the nucleolus.
R-DME-72649. Translation initiation complex formation.
R-DME-72689. Formation of a pool of free 40S subunits.
R-DME-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-DME-72702. Ribosomal scanning and start codon recognition.
R-DME-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-DME-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-DME-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein SAUniRule annotation
Alternative name(s):
K14
Laminin receptor homolog
Protein stubaristaUniRule annotation
Gene namesi
Name:staUniRule annotation
ORF Names:CG14792
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0003517. sta.

Subcellular locationi

  • Cytoplasm UniRule annotation1 Publication
  • Nucleus UniRule annotation1 Publication

  • Note: May associate with nascent RNP complexes within the nucleus.

GO - Cellular componenti

  • cytosolic small ribosomal subunit Source: FlyBase
  • microtubule associated complex Source: FlyBase
  • nucleus Source: UniProtKB-SubCell
  • ribosome Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 31331340S ribosomal protein SAPRO_0000134353Add
BLAST

Proteomic databases

PaxDbiP38979.
PRIDEiP38979.

Expressioni

Developmental stagei

Expressed both maternally and zygotically in embryos.1 Publication

Gene expression databases

BgeeiP38979.
GenevisibleiP38979. DM.

Interactioni

Subunit structurei

Component of the small ribosomal subunit. Mature ribosomes consist of a small (40S) and a large (60S) subunit. The 40S subunit contains about 33 different proteins and 1 molecule of RNA (18S). The 60S subunit contains about 49 different proteins and 3 molecules of RNA (28S, 5.8S and 5S). Interacts with oho23B/rpS21.UniRule annotation1 Publication

Protein-protein interaction databases

BioGridi57663. 12 interactions.
DIPiDIP-17178N.
IntActiP38979. 3 interactions.
MINTiMINT-1635735.
STRINGi7227.FBpp0070279.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00AA1-313[»]
ProteinModelPortaliP38979.
SMRiP38979. Positions 45-260.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S2P family.UniRule annotation

Phylogenomic databases

eggNOGiKOG0830. Eukaryota.
COG0052. LUCA.
InParanoidiP38979.
KOiK02998.
OMAiHNKPYVY.
OrthoDBiEOG73NG4F.
PhylomeDBiP38979.

Family and domain databases

HAMAPiMF_03015. Ribosomal_S2_euk.
InterProiIPR032281. 40S_SA_C.
IPR001865. Ribosomal_S2.
IPR018130. Ribosomal_S2_CS.
IPR027498. Ribosomal_S2_euk.
IPR005707. Ribosomal_S2_euk/arc.
IPR023591. Ribosomal_S2_flav_dom.
[Graphical view]
PANTHERiPTHR11489. PTHR11489. 1 hit.
PfamiPF16122. 40S_SA_C. 1 hit.
PF00318. Ribosomal_S2. 2 hits.
[Graphical view]
PRINTSiPR00395. RIBOSOMALS2.
SUPFAMiSSF52313. SSF52313. 1 hit.
TIGRFAMsiTIGR01012. uS2_euk_arch. 1 hit.
PROSITEiPS00962. RIBOSOMAL_S2_1. 1 hit.
PS00963. RIBOSOMAL_S2_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform D (identifier: P38979-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MCRRLWRQAR HRRKVARGAP SLRLCPLTIC LSRSQVRNSF HVNMSGGLDI
60 70 80 90 100
LSLKEDDITK MLVATTHLGS ENVNFQMEQY VYKRRADGVN ILNLGKTWEK
110 120 130 140 150
LQLAARAIVA IDNPSDIFVI SSRPIGQRAV LKFAKYTDTT PIAGRFTPGA
160 170 180 190 200
FTNQIQPAFR EPRLLVVTDP NTDHQPIMEA SYVNIPVIAF TNTDSPLRYI
210 220 230 240 250
DIAIPCNNKS AHSIGLMWWL LAREVLRLRG TISRSVEWPV VVDLFFYRDP
260 270 280 290 300
EEAEKEEAAA KELLPPPKIE EAVDHPVEET TNWADEVAAE TVGGVEDWNE
310
DTVKTSWGSD GQF
Note: No experimental confirmation available.
Length:313
Mass (Da):35,341
Last modified:June 26, 2007 - v2
Checksum:i7F473AEB2C86712C
GO
Isoform A (identifier: P38979-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-43: Missing.

Show »
Length:270
Mass (Da):30,228
Checksum:iFEC452C3F1712C82
GO

Sequence cautioni

The sequence AAA28667.1 differs from that shown. Reason: Erroneous initiation. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4343Missing in isoform A. 3 PublicationsVSP_026172Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M90422 Genomic DNA. Translation: AAA28741.1.
AE014298 Genomic DNA. Translation: AAF45638.2.
AE014298 Genomic DNA. Translation: AAN09049.1.
AE014298 Genomic DNA. Translation: AAN09050.3.
AL031027 Genomic DNA. Translation: CAA19839.1.
AY118899 mRNA. Translation: AAM50759.1.
BT029094 mRNA. Translation: ABJ17027.1.
M77133 mRNA. Translation: AAA28667.1. Different initiation.
PIRiT13602.
RefSeqiNP_001284785.1. NM_001297856.1. [P38979-2]
NP_476750.1. NM_057402.5. [P38979-2]
NP_726744.1. NM_166889.2. [P38979-2]
NP_726745.3. NM_166890.3. [P38979-2]
UniGeneiDm.33985.
Dm.4723.

Genome annotation databases

GeneIDi31106.
KEGGidme:Dmel_CG14792.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M90422 Genomic DNA. Translation: AAA28741.1.
AE014298 Genomic DNA. Translation: AAF45638.2.
AE014298 Genomic DNA. Translation: AAN09049.1.
AE014298 Genomic DNA. Translation: AAN09050.3.
AL031027 Genomic DNA. Translation: CAA19839.1.
AY118899 mRNA. Translation: AAM50759.1.
BT029094 mRNA. Translation: ABJ17027.1.
M77133 mRNA. Translation: AAA28667.1. Different initiation.
PIRiT13602.
RefSeqiNP_001284785.1. NM_001297856.1. [P38979-2]
NP_476750.1. NM_057402.5. [P38979-2]
NP_726744.1. NM_166889.2. [P38979-2]
NP_726745.3. NM_166890.3. [P38979-2]
UniGeneiDm.33985.
Dm.4723.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00AA1-313[»]
ProteinModelPortaliP38979.
SMRiP38979. Positions 45-260.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi57663. 12 interactions.
DIPiDIP-17178N.
IntActiP38979. 3 interactions.
MINTiMINT-1635735.
STRINGi7227.FBpp0070279.

Proteomic databases

PaxDbiP38979.
PRIDEiP38979.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi31106.
KEGGidme:Dmel_CG14792.

Organism-specific databases

CTDi104044.
FlyBaseiFBgn0003517. sta.

Phylogenomic databases

eggNOGiKOG0830. Eukaryota.
COG0052. LUCA.
InParanoidiP38979.
KOiK02998.
OMAiHNKPYVY.
OrthoDBiEOG73NG4F.
PhylomeDBiP38979.

Enzyme and pathway databases

ReactomeiR-DME-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-DME-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-DME-6791226. Major pathway of rRNA processing in the nucleolus.
R-DME-72649. Translation initiation complex formation.
R-DME-72689. Formation of a pool of free 40S subunits.
R-DME-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-DME-72702. Ribosomal scanning and start codon recognition.
R-DME-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-DME-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-DME-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

GenomeRNAii31106.
PROiP38979.

Gene expression databases

BgeeiP38979.
GenevisibleiP38979. DM.

Family and domain databases

HAMAPiMF_03015. Ribosomal_S2_euk.
InterProiIPR032281. 40S_SA_C.
IPR001865. Ribosomal_S2.
IPR018130. Ribosomal_S2_CS.
IPR027498. Ribosomal_S2_euk.
IPR005707. Ribosomal_S2_euk/arc.
IPR023591. Ribosomal_S2_flav_dom.
[Graphical view]
PANTHERiPTHR11489. PTHR11489. 1 hit.
PfamiPF16122. 40S_SA_C. 1 hit.
PF00318. Ribosomal_S2. 2 hits.
[Graphical view]
PRINTSiPR00395. RIBOSOMALS2.
SUPFAMiSSF52313. SSF52313. 1 hit.
TIGRFAMsiTIGR01012. uS2_euk_arch. 1 hit.
PROSITEiPS00962. RIBOSOMAL_S2_1. 1 hit.
PS00963. RIBOSOMAL_S2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Drosophila stubarista phenotype is associated with a dosage effect of the putative ribosome-associated protein D-p40 on spineless."
    Melnick M.B., Noll E., Perrimon N.
    Genetics 135:553-564(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM A), FUNCTION, DEVELOPMENTAL STAGE.
    Tissue: Embryo.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Oregon-R.
  5. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    Strain: Berkeley.
    Tissue: Embryo.
  6. Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    Strain: Berkeley.
  7. "A mammalian laminin receptor homolog from Drosophila."
    Kim Y.J., Baker B.S.
    Submitted (OCT-1991) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 45-313.
    Strain: Canton-S.
  8. "Down-regulation of RpS21, a putative translation initiation factor interacting with P40, produces viable minute imagos and larval lethality with overgrown hematopoietic organs and imaginal discs."
    Toeroek I., Herrmann-Horle D., Kiss I., Tick G., Speer G., Schmitt R., Mechler B.M.
    Mol. Cell. Biol. 19:2308-2321(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RPS21.
  9. "Ribosome components are associated with sites of transcription."
    Brogna S., Sato T., Rosbash M.
    Mol. Cell 10:93-104(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  10. Erratum
    Brogna S., Sato T., Rosbash M.
    Mol. Cell 10:959-959(2002) [PubMed] [Europe PMC] [Abstract]
  11. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF THE 80S RIBOSOME.

Entry informationi

Entry nameiRSSA_DROME
AccessioniPrimary (citable) accession number: P38979
Secondary accession number(s): Q058X4, Q7KW10, Q9W583
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: June 26, 2007
Last modified: June 8, 2016
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Caution

Was originally thought to be a laminin receptor.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.