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P55830 (RS3A_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
40S ribosomal protein S3a
Alternative name(s):
C3 protein
Gene names
Name:RpS3A
Synonyms:C3, M(4)101
ORF Names:CG2168
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length268 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Essential for oogenesis; required for late follicle cell development. Ref.1

Subunit structure

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) By similarity.

Subcellular location

Cytoplasm Ref.1.

Tissue specificity

Ubiquitously expressed in stage 8 embryos. During oogenesis, expression is located basally in somatic follicular epithelium and in the oocyte at the later stages. Ref.1

Developmental stage

Expressed both maternally and zygotically throughout all development. Ref.2

Disruption phenotype

Flies exhibit disappearance of the follicular cells of the ovary and abnormalities of the associated germline derivatives, leading to failure of egg production. Ref.1

Sequence similarities

Belongs to the ribosomal protein S3Ae family.

Sequence caution

The sequence AAL48571.1 differs from that shown. Reason: Frameshift at position 188.

The sequence ACQ89821.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 3 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]
Isoform A (identifier: P55830-1)

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.
Isoform B (identifier: P55830-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-63: MAVGKNKGLS...GQRIASDYLK → MSKLRICFKPVKS
Note: Produced by alternative splicing.
Isoform D (identifier: P55830-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-105: Missing.
Note: Produced by alternative initiation at Met-106 of isoform A.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 26826740S ribosomal protein S3a HAMAP-Rule MF_03122
PRO_0000153529

Natural variations

Alternative sequence1 – 105105Missing in isoform D.
VSP_038422
Alternative sequence1 – 6363MAVGK…SDYLK → MSKLRICFKPVKS in isoform B.
VSP_038423

Experimental info

Sequence conflict621L → F in CAA71201. Ref.1
Sequence conflict721A → VP in CAA71201. Ref.1
Sequence conflict821R → H in CAA71201. Ref.1
Sequence conflict160 – 1612QQ → HE in CAA71201. Ref.1
Sequence conflict1691A → SG in CAA71201. Ref.1
Sequence conflict253 – 2619VIDRPEGYE → PKSTALKVK in CAA71201. Ref.1
Sequence conflict2671A → S in CAA71201. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified March 2, 2010. Version 4.
Checksum: EA407157F81955C6

FASTA26830,340
        10         20         30         40         50         60 
MAVGKNKGLS KGGKKGGKKK VVDPFSRKDW YDVKAPNMFQ TRQIGKTLVN RTQGQRIASD 

        70         80         90        100        110        120 
YLKGRVFEVS LADLQKDIDP ERSFRKFRLI AEDVQDRNVL CNFHGMDLTT DKYRSMVKKW 

       130        140        150        160        170        180 
QTLIEAIVEA KTVDGYLLRV FCIGFTAKDQ QSQRKTCYAQ QSQVRKIRAR MTDIITNEVS 

       190        200        210        220        230        240 
GADLKQLVNK LALDSIAKDI EKSCQRIYPL HDVYIRKVKV LKKPRFDVSK LLELHGDGGG 

       250        260 
KSVEAVVSSE GAVIDRPEGY EPPVQEAV 

« Hide

Isoform B [UniParc].

Checksum: EBE6F16029A4817D
Show »

FASTA21824,822
Isoform D [UniParc].

Checksum: DDF1BD80CE79E3C0
Show »

FASTA16318,386

References

« Hide 'large scale' references
[1]"Antisense suppression of the putative ribosomal protein S3A gene disrupts ovarian development in Drosophila melanogaster."
Reynaud E., Bolshakov V.N., Barajas V.N., Kafatos F.C., Zurita M.
Mol. Gen. Genet. 256:462-467(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
Strain: Oregon-R.
Tissue: Embryo.
[2]"Drosophila RpS3a, a novel minute gene situated between the segment polarity genes cubitus interruptus and dTCF."
van Beest M., Mortin M., Clevers H.
Nucleic Acids Res. 26:4471-4475(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), DEVELOPMENTAL STAGE.
Strain: Berkeley.
Tissue: Embryo.
[3]"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. expand/collapse author list , 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.
[4]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
Strain: Berkeley.
[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]Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.
Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
Strain: Berkeley.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y10115 mRNA. Translation: CAA71201.1.
AF034971 mRNA. Translation: AAC62117.1.
AE014135 Genomic DNA. Translation: AAF59372.1.
AE014135 Genomic DNA. Translation: AAN06541.1.
AE014135 Genomic DNA. Translation: AAN06542.1.
AY070949 mRNA. Translation: AAL48571.1. Frameshift.
BT083412 mRNA. Translation: ACQ89821.1. Different initiation.
RefSeqNP_001245404.1. NM_001258475.2.
NP_524618.1. NM_079879.4.
NP_726518.1. NM_166714.4.
UniGeneDm.31437.
Dm.6768.

3D structure databases

ProteinModelPortalP55830.
SMRP55830. Positions 21-238.
ModBaseSearch...

Protein-protein interaction databases

IntActP55830. 2 interactions.
MINTMINT-923192.

Proteomic databases

PaxDbP55830.
PRIDEP55830.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0089175; FBpp0088242; FBgn0017545.
FBtr0308296; FBpp0300615; FBgn0017545.
GeneID43768.
KEGGdme:Dmel_CG2168.
UCSCCG2168-RB. d. melanogaster.
CG2168-RD. d. melanogaster.

Organism-specific databases

CTD6189.
FlyBaseFBgn0017545. RpS3A.

Phylogenomic databases

eggNOGCOG1890.
GeneTreeENSGT00390000018433.
InParanoidQ8IMB0.
KOK02984.
OMARSLIHKW.
OrthoDBEOG4DJHCB.
PhylomeDBP55830.

Gene expression databases

BgeeP55830.
GermOnlineCG2168. Drosophila melanogaster.

Family and domain databases

HAMAPMF_03122. Ribosomal_S3Ae_euk.
InterProIPR027500. Ribosomal_S1/3_euk.
IPR001593. Ribosomal_S3Ae.
IPR018281. Ribosomal_S3Ae_CS.
[Graphical view]
PfamPF01015. Ribosomal_S3Ae. 1 hit.
[Graphical view]
PROSITEPS01191. RIBOSOMAL_S3AE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRPS3A. drosophila.
GenomeRNAi43768.
NextBio835682.

Entry information

Entry nameRS3A_DROME
AccessionPrimary (citable) accession number: P55830
Secondary accession number(s): C4IXY1 expand/collapse secondary AC list , O44389, Q8IMA9, Q8IMB0, Q8SZD2, Q9V4A9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 2, 2010
Last modified: May 29, 2013
This is version 100 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Ribosomal proteins

Ribosomal proteins families and list of entries

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families