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Protein

Guanine nucleotide-binding protein subunit gamma-e

Gene

Ggamma30A

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

Functioni

Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. This subunit functions in visual transduction in the compound eye.

GO - Molecular functioni

  • protein heterodimerization activity Source: FlyBase
  • signal transducer activity Source: UniProtKB-KW

GO - Biological processi

  • cellular response to carbon dioxide Source: FlyBase
  • G-protein coupled receptor signaling pathway Source: InterPro
  • phototransduction Source: FlyBase
  • visual perception Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Transducer

Keywords - Biological processi

Sensory transduction, Vision

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide-binding protein subunit gamma-e
Short name:
Ggamma(e)
Gene namesi
Name:Ggamma30A
ORF Names:CG3694
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0028433. Ggamma30A.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: FlyBase
  • heterotrimeric G-protein complex Source: FlyBase
  • plasma membrane Source: FlyBase
  • rhabdomere Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi69 – 691C → G: Loss of farnesylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 6968Guanine nucleotide-binding protein subunit gamma-ePRO_0000012679Add
BLAST
Propeptidei70 – 723Removed in mature formBy similarityPRO_0000012680

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylaspartate1 Publication
Modified residuei69 – 691Cysteine methyl ester1 Publication
Lipidationi69 – 691S-farnesyl cysteine1 Publication

Keywords - PTMi

Acetylation, Lipoprotein, Methylation, Prenylation

Proteomic databases

PaxDbiQ9NFZ3.
PRIDEiQ9NFZ3.

Expressioni

Gene expression databases

BgeeiQ9NFZ3.
GenevisibleiQ9NFZ3. DM.

Interactioni

Subunit structurei

G proteins are composed of 3 units, alpha, beta and gamma.

Binary interactionsi

WithEntry#Exp.IntActNotes
Gbeta76CP298292EBI-2695634,EBI-128499

Protein-protein interaction databases

BioGridi69527. 1 interaction.
IntActiQ9NFZ3. 1 interaction.
STRINGi7227.FBpp0291070.

Structurei

3D structure databases

ProteinModelPortaliQ9NFZ3.
SMRiQ9NFZ3. Positions 8-65.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the G protein gamma family.Curated

Phylogenomic databases

eggNOGiNOG293449.
GeneTreeiENSGT00730000114118.
InParanoidiQ9NFZ3.
OMAiKWIEECV.
OrthoDBiEOG7H1JP7.
PhylomeDBiQ9NFZ3.

Family and domain databases

Gene3Di4.10.260.10. 1 hit.
InterProiIPR015898. G-protein_gamma-like_dom.
IPR001770. Gprotein-gamma.
[Graphical view]
PfamiPF00631. G-gamma. 1 hit.
[Graphical view]
PRINTSiPR00321. GPROTEING.
SMARTiSM00224. GGL. 1 hit.
[Graphical view]
SUPFAMiSSF48670. SSF48670. 1 hit.
PROSITEiPS50058. G_PROTEIN_GAMMA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9NFZ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDPSALQNMD RDALKKQIEN MKYQASMERW PLSKSIAEMR SFIEENEKND
60 70
PLINAPDKKN NPWAEKGKCV IM
Length:72
Mass (Da):8,398
Last modified:October 1, 2000 - v1
Checksum:iB0FC6DC9170EDA70
GO

Sequence cautioni

The sequence AAL28579.1 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ250440 mRNA. Translation: CAB70093.1.
AE014134 Genomic DNA. Translation: AAF52759.2.
AE014134 Genomic DNA. Translation: AAF52760.2.
AE014134 Genomic DNA. Translation: AAF52761.2.
AY061031 mRNA. Translation: AAL28579.1. Sequence problems.
RefSeqiNP_001162918.1. NM_001169447.2.
NP_001188749.1. NM_001201820.2.
NP_001245950.1. NM_001259021.2.
NP_524807.1. NM_080068.4.
NP_723451.1. NM_164851.3.
NP_723452.1. NM_164852.3.
UniGeneiDm.1453.

Genome annotation databases

EnsemblMetazoaiFBtr0079795; FBpp0079395; FBgn0267252.
FBtr0079796; FBpp0079396; FBgn0267252.
FBtr0079797; FBpp0079397; FBgn0267252.
FBtr0303895; FBpp0292898; FBgn0267252.
FBtr0309247; FBpp0301186; FBgn0267252.
FBtr0330019; FBpp0303053; FBgn0267252.
GeneIDi45234.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ250440 mRNA. Translation: CAB70093.1.
AE014134 Genomic DNA. Translation: AAF52759.2.
AE014134 Genomic DNA. Translation: AAF52760.2.
AE014134 Genomic DNA. Translation: AAF52761.2.
AY061031 mRNA. Translation: AAL28579.1. Sequence problems.
RefSeqiNP_001162918.1. NM_001169447.2.
NP_001188749.1. NM_001201820.2.
NP_001245950.1. NM_001259021.2.
NP_524807.1. NM_080068.4.
NP_723451.1. NM_164851.3.
NP_723452.1. NM_164852.3.
UniGeneiDm.1453.

3D structure databases

ProteinModelPortaliQ9NFZ3.
SMRiQ9NFZ3. Positions 8-65.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi69527. 1 interaction.
IntActiQ9NFZ3. 1 interaction.
STRINGi7227.FBpp0291070.

Proteomic databases

PaxDbiQ9NFZ3.
PRIDEiQ9NFZ3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0079795; FBpp0079395; FBgn0267252.
FBtr0079796; FBpp0079396; FBgn0267252.
FBtr0079797; FBpp0079397; FBgn0267252.
FBtr0303895; FBpp0292898; FBgn0267252.
FBtr0309247; FBpp0301186; FBgn0267252.
FBtr0330019; FBpp0303053; FBgn0267252.
GeneIDi45234.

Organism-specific databases

CTDi45234.
FlyBaseiFBgn0028433. Ggamma30A.

Phylogenomic databases

eggNOGiNOG293449.
GeneTreeiENSGT00730000114118.
InParanoidiQ9NFZ3.
OMAiKWIEECV.
OrthoDBiEOG7H1JP7.
PhylomeDBiQ9NFZ3.

Miscellaneous databases

GenomeRNAii45234.
NextBioi837925.
PROiQ9NFZ3.

Gene expression databases

BgeeiQ9NFZ3.
GenevisibleiQ9NFZ3. DM.

Family and domain databases

Gene3Di4.10.260.10. 1 hit.
InterProiIPR015898. G-protein_gamma-like_dom.
IPR001770. Gprotein-gamma.
[Graphical view]
PfamiPF00631. G-gamma. 1 hit.
[Graphical view]
PRINTSiPR00321. GPROTEING.
SMARTiSM00224. GGL. 1 hit.
[Graphical view]
SUPFAMiSSF48670. SSF48670. 1 hit.
PROSITEiPS50058. G_PROTEIN_GAMMA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel Ggamma isolated from Drosophila constitutes a visual G protein gamma subunit of the fly compound eye."
    Schulz S., Huber A., Schwab K., Paulsen R.
    J. Biol. Chem. 274:37605-37610(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Eye.
  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: Head.
  5. "Targeted mutagenesis of the farnesylation site of Drosophila Ggammae disrupts membrane association of the G protein betagamma complex and affects the light sensitivity of the visual system."
    Schillo S., Belusic G., Hartmann K., Franz C., Kuhl B., Brenner-Weiss G., Paulsen R., Huber A.
    J. Biol. Chem. 279:36309-36316(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT ASP-2, ISOPRENYLATION AT CYS-69, METHYLATION AT CYS-69, MUTAGENESIS OF CYS-69.

Entry informationi

Entry nameiGBGE_DROME
AccessioniPrimary (citable) accession number: Q9NFZ3
Secondary accession number(s): A4V0H1, Q95RZ3, Q9VLD3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: October 1, 2000
Last modified: July 22, 2015
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.