Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

60S ribosomal protein L7a

Gene

RpL7A

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  • RNA binding Source: GO_Central
  • structural constituent of ribosome Source: FlyBase

GO - Biological processi

  • centrosome duplication Source: FlyBase
  • centrosome organization Source: FlyBase
  • maturation of LSU-rRNA Source: GO_Central
  • mitotic spindle elongation Source: FlyBase
  • mitotic spindle organization Source: FlyBase
  • translation Source: GO_Central
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 L7a
Gene namesi
Name:RpL7A
Synonyms:SURF-3
ORF Names:CG3314
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0014026. RpL7A.

Subcellular locationi

GO - Cellular componenti

  • cytosolic large ribosomal subunit Source: GO_Central
  • ribosome Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 27127160S ribosomal protein L7aPRO_0000136755Add
BLAST

Proteomic databases

PaxDbiP46223.

Expressioni

Gene expression databases

ExpressionAtlasiP46223. differential.
GenevisibleiP46223. DM.

Interactioni

Protein-protein interaction databases

BioGridi58075. 26 interactions.
IntActiP46223. 2 interactions.
MINTiMINT-1546463.
STRINGi7227.FBpp0070877.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00CG1-271[»]
ProteinModelPortaliP46223.
SMRiP46223. Positions 132-228.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L7Ae family.Curated

Phylogenomic databases

eggNOGiKOG3166. Eukaryota.
COG1358. LUCA.
InParanoidiP46223.
KOiK02936.
OMAiTCTCVAF.
OrthoDBiEOG712TXC.
PhylomeDBiP46223.

Family and domain databases

Gene3Di3.30.1330.30. 1 hit.
InterProiIPR029064. L30e-like.
IPR001921. Ribosomal_L7A/L8.
IPR004038. Ribosomal_L7Ae/L30e/S12e/Gad45.
IPR018492. Ribosomal_L7Ae/L8/Nhp2.
IPR004037. Ribosomal_L7Ae_CS.
[Graphical view]
PfamiPF01248. Ribosomal_L7Ae. 1 hit.
[Graphical view]
PRINTSiPR00881. L7ARS6FAMILY.
PR00882. RIBOSOMALL7A.
SUPFAMiSSF55315. SSF55315. 1 hit.
PROSITEiPS01082. RIBOSOMAL_L7AE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P46223-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVVKKPRPKK KPVTKKVAPA PLAVKKPVVK KVVNQLFEKR PKNFGIGQNV
60 70 80 90 100
QPKRDLSRFV RWPKYIRVQR QKAVLQKRLK VPPPIHQFSQ TLDKTTAVKL
110 120 130 140 150
FKLLEKYRPE SPLAKKLRLK KIAEAKAKGK DVEPKKKPSY VSAGTNTVTK
160 170 180 190 200
LIEQKKAQLV VIAHDVDPLE LVLFLPALCR KMGVPYCIVK GKARLGRLVR
210 220 230 240 250
RKTCTTLALT TVDNNDKANF GKVLEAVKTN FNERHEEIRR HWGGGILGSK
260 270
SLARISKLER AKARELAQKQ G
Length:271
Mass (Da):30,732
Last modified:September 27, 2005 - v2
Checksum:iA31E9735E891E479
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti112 – 1121P → A in CAA58023 (PubMed:7739520).Curated
Sequence conflicti116 – 1172KL → NV in CAA58023 (PubMed:7739520).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82782 Genomic DNA. Translation: CAA58023.1.
AE014298 Genomic DNA. Translation: AAF46169.1.
AE014298 Genomic DNA. Translation: AAN09170.1.
AE014298 Genomic DNA. Translation: AAN09172.1.
AY089570 mRNA. Translation: AAL90308.1.
PIRiA57416.
RefSeqiNP_001284944.1. NM_001298015.1.
NP_001284945.1. NM_001298016.1.
NP_511063.1. NM_078508.6.
NP_727094.1. NM_167073.3.
NP_727096.1. NM_167075.2.
UniGeneiDm.7159.

Genome annotation databases

EnsemblMetazoaiFBtr0070915; FBpp0070877; FBgn0014026.
FBtr0070916; FBpp0070878; FBgn0014026.
FBtr0343328; FBpp0309986; FBgn0014026.
FBtr0343329; FBpp0309987; FBgn0014026.
FBtr0345293; FBpp0311460; FBgn0014026.
GeneIDi31588.
KEGGidme:Dmel_CG3314.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82782 Genomic DNA. Translation: CAA58023.1.
AE014298 Genomic DNA. Translation: AAF46169.1.
AE014298 Genomic DNA. Translation: AAN09170.1.
AE014298 Genomic DNA. Translation: AAN09172.1.
AY089570 mRNA. Translation: AAL90308.1.
PIRiA57416.
RefSeqiNP_001284944.1. NM_001298015.1.
NP_001284945.1. NM_001298016.1.
NP_511063.1. NM_078508.6.
NP_727094.1. NM_167073.3.
NP_727096.1. NM_167075.2.
UniGeneiDm.7159.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00CG1-271[»]
ProteinModelPortaliP46223.
SMRiP46223. Positions 132-228.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi58075. 26 interactions.
IntActiP46223. 2 interactions.
MINTiMINT-1546463.
STRINGi7227.FBpp0070877.

Proteomic databases

PaxDbiP46223.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0070915; FBpp0070877; FBgn0014026.
FBtr0070916; FBpp0070878; FBgn0014026.
FBtr0343328; FBpp0309986; FBgn0014026.
FBtr0343329; FBpp0309987; FBgn0014026.
FBtr0345293; FBpp0311460; FBgn0014026.
GeneIDi31588.
KEGGidme:Dmel_CG3314.

Organism-specific databases

CTDi6130.
FlyBaseiFBgn0014026. RpL7A.

Phylogenomic databases

eggNOGiKOG3166. Eukaryota.
COG1358. LUCA.
InParanoidiP46223.
KOiK02936.
OMAiTCTCVAF.
OrthoDBiEOG712TXC.
PhylomeDBiP46223.

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

ChiTaRSiRpL7A. fly.
GenomeRNAii31588.
PROiP46223.

Gene expression databases

ExpressionAtlasiP46223. differential.
GenevisibleiP46223. DM.

Family and domain databases

Gene3Di3.30.1330.30. 1 hit.
InterProiIPR029064. L30e-like.
IPR001921. Ribosomal_L7A/L8.
IPR004038. Ribosomal_L7Ae/L30e/S12e/Gad45.
IPR018492. Ribosomal_L7Ae/L8/Nhp2.
IPR004037. Ribosomal_L7Ae_CS.
[Graphical view]
PfamiPF01248. Ribosomal_L7Ae. 1 hit.
[Graphical view]
PRINTSiPR00881. L7ARS6FAMILY.
PR00882. RIBOSOMALL7A.
SUPFAMiSSF55315. SSF55315. 1 hit.
PROSITEiPS01082. RIBOSOMAL_L7AE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genomic organization of the region containing the Drosophila melanogaster rpL7a (Surf-3) gene differs from those of the mammalian and avian Surfeit loci."
    Armes N., Fried M.
    Mol. Cell. Biol. 15:2367-2373(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Canton-S.
  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.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  5. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF THE 80S RIBOSOME.

Entry informationi

Entry nameiRL7A_DROME
AccessioniPrimary (citable) accession number: P46223
Secondary accession number(s): A4V411, Q9W3Z2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: September 27, 2005
Last modified: July 6, 2016
This is version 113 of the entry and version 2 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.