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Protein

60S ribosomal protein L3

Gene

RpL3

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

The L3 protein is a component of the large subunit of cytoplasmic ribosomes.

GO - Molecular functioni

GO - Biological processi

  • centrosome duplication Source: FlyBase
  • centrosome organization Source: FlyBase
  • mitotic spindle elongation Source: FlyBase
  • mitotic spindle organization Source: FlyBase
  • sensory perception of pain Source: FlyBase
  • translation Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

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-72689. Formation of a pool of free 40S subunits.
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:
60S ribosomal protein L3
Gene namesi
Name:RpL3
ORF Names:CG4863
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0020910. RpL3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 41641560S ribosomal protein L3PRO_0000077237Add
BLAST

Proteomic databases

PaxDbiO16797.
PRIDEiO16797.

Expressioni

Gene expression databases

BgeeiO16797.
ExpressionAtlasiO16797. differential.
GenevisibleiO16797. DM.

Interactioni

Protein-protein interaction databases

BioGridi66481. 52 interactions.
DIPiDIP-17151N.
IntActiO16797. 3 interactions.
STRINGi7227.FBpp0081822.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00CB1-416[»]
ProteinModelPortaliO16797.
SMRiO16797. Positions 7-351.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L3P family.Curated

Phylogenomic databases

eggNOGiKOG0746. Eukaryota.
COG0087. LUCA.
GeneTreeiENSGT00390000017606.
InParanoidiO16797.
KOiK02925.
OMAiQESHSAM.
OrthoDBiEOG7HF1JK.
PhylomeDBiO16797.

Family and domain databases

InterProiIPR000597. Ribosomal_L3.
IPR019926. Ribosomal_L3_CS.
IPR009000. Transl_B-barrel.
[Graphical view]
PfamiPF00297. Ribosomal_L3. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 1 hit.
PROSITEiPS00474. RIBOSOMAL_L3. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: O16797-1) [UniParc]FASTAAdd to basket

Also known as: H

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
MSHRKFSAPR HGSMAFYPKK RSARHRGKVK AFPKDDASKP VHLTCFIGYK
60 70 80 90 100
AGMTHIVREA DRPGSKINKK EVVEAVTVLE TPPMIVVGAV GYIETPFGLR
110 120 130 140 150
ALVNVWAQHL SEECRRRFYK NWYKSKKKAF TKASKKWTDD LGKKSIENDF
160 170 180 190 200
RKMLRYCKVI RVIAHSQIRL IKQRQKKAHV MEIQLNGGSI EDKVKWAREH
210 220 230 240 250
LEKPIQVSNV FGQDEMIDCV GVTKGKGFKG VTSRWHTKKL PRKTHKGLRK
260 270 280 290 300
VACIGAWHPS RVSTTVARAG QKGYHHRTEI NKKIYRIGAG IHTKDGKVIK
310 320 330 340 350
NNASTEYDLT DKSITPMGGF PHYGEVNNDF VMIKGCCIGS KKRIITLRKS
360 370 380 390 400
LLKHTKRSAL EQIKLKFIDT SSKMGHGRFQ TPADKLAFMG PLKKDRLKEE
410
AAATTAAAAA ATTTSA
Length:416
Mass (Da):46,916
Last modified:January 23, 2007 - v3
Checksum:i779D843982334AA5
GO
Isoform G (identifier: O16797-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     122-138: WYKSKKKAFTKASKKWT → CSSISLLRELFKSLNVV
     139-416: Missing.

Note: No experimental confirmation available.
Show »
Length:138
Mass (Da):15,611
Checksum:i2CB26B658A5BEE98
GO
Isoform D (identifier: O16797-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     124-161: KSKKKAFTKA...KMLRYCKVIR → VSEDHVVVLP...ADTCFLLESG
     162-416: Missing.

Note: No experimental confirmation available.
Show »
Length:161
Mass (Da):18,136
Checksum:i03925456CDC7AED2
GO

Sequence cautioni

The sequence AAR96131.1 differs from that shown. Reason: Frameshift at position 403. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei122 – 13817WYKSK…SKKWT → CSSISLLRELFKSLNVV in isoform G. CuratedVSP_005714Add
BLAST
Alternative sequencei124 – 16138KSKKK…CKVIR → VSEDHVVVLPTPFVAIFFAP GVHTHKMAADTCFLLESG in isoform D. CuratedVSP_005715Add
BLAST
Alternative sequencei139 – 416278Missing in isoform G. CuratedVSP_005716Add
BLAST
Alternative sequencei162 – 416255Missing in isoform D. CuratedVSP_005717Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF016835 mRNA. Translation: AAC26144.1.
AE014297 Genomic DNA. Translation: AAF54610.2.
AE014297 Genomic DNA. Translation: AAF54611.2.
AE014297 Genomic DNA. Translation: AAF54612.2.
AE014297 Genomic DNA. Translation: AAN13496.2.
BT011339 mRNA. Translation: AAR96131.1. Frameshift.
RefSeqiNP_524316.1. NM_079592.3. [O16797-1]
NP_731547.1. NM_169377.2. [O16797-2]
NP_731548.2. NM_169378.2. [O16797-1]
NP_731550.2. NM_169380.2. [O16797-5]
UniGeneiDm.6703.

Genome annotation databases

EnsemblMetazoaiFBtr0082346; FBpp0081822; FBgn0020910. [O16797-1]
FBtr0336783; FBpp0307759; FBgn0020910. [O16797-1]
GeneIDi41347.
KEGGidme:Dmel_CG4863.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF016835 mRNA. Translation: AAC26144.1.
AE014297 Genomic DNA. Translation: AAF54610.2.
AE014297 Genomic DNA. Translation: AAF54611.2.
AE014297 Genomic DNA. Translation: AAF54612.2.
AE014297 Genomic DNA. Translation: AAN13496.2.
BT011339 mRNA. Translation: AAR96131.1. Frameshift.
RefSeqiNP_524316.1. NM_079592.3. [O16797-1]
NP_731547.1. NM_169377.2. [O16797-2]
NP_731548.2. NM_169378.2. [O16797-1]
NP_731550.2. NM_169380.2. [O16797-5]
UniGeneiDm.6703.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00CB1-416[»]
ProteinModelPortaliO16797.
SMRiO16797. Positions 7-351.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi66481. 52 interactions.
DIPiDIP-17151N.
IntActiO16797. 3 interactions.
STRINGi7227.FBpp0081822.

Proteomic databases

PaxDbiO16797.
PRIDEiO16797.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0082346; FBpp0081822; FBgn0020910. [O16797-1]
FBtr0336783; FBpp0307759; FBgn0020910. [O16797-1]
GeneIDi41347.
KEGGidme:Dmel_CG4863.

Organism-specific databases

CTDi6122.
FlyBaseiFBgn0020910. RpL3.

Phylogenomic databases

eggNOGiKOG0746. Eukaryota.
COG0087. LUCA.
GeneTreeiENSGT00390000017606.
InParanoidiO16797.
KOiK02925.
OMAiQESHSAM.
OrthoDBiEOG7HF1JK.
PhylomeDBiO16797.

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-72689. Formation of a pool of free 40S subunits.
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

ChiTaRSiRpL3. fly.
GenomeRNAii41347.
NextBioi823392.
PROiO16797.

Gene expression databases

BgeeiO16797.
ExpressionAtlasiO16797. differential.
GenevisibleiO16797. DM.

Family and domain databases

InterProiIPR000597. Ribosomal_L3.
IPR019926. Ribosomal_L3_CS.
IPR009000. Transl_B-barrel.
[Graphical view]
PfamiPF00297. Ribosomal_L3. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 1 hit.
PROSITEiPS00474. RIBOSOMAL_L3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of the gene for Drosophila L3 ribosomal protein."
    Chan H.Y.E., Zhang Y., Hoheisel J.D., O'Kane C.J.
    Gene 212:119-125(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
  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. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    Strain: Berkeley.
    Tissue: Head.
  5. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF THE 80S RIBOSOME.

Entry informationi

Entry nameiRL3_DROME
AccessioniPrimary (citable) accession number: O16797
Secondary accession number(s): Q0KI83
, Q6NNE9, Q9VGR4, Q9VGR5, Q9VGR6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 135 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

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.