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Q9NFZ3

- GBGE_DROME

UniProt

Q9NFZ3 - GBGE_DROME

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Protein

Guanine nucleotide-binding protein subunit gamma-e

Gene

Ggamma30A

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - 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

  1. signal transducer activity Source: UniProtKB-KW

GO - Biological processi

  1. G-protein coupled receptor signaling pathway Source: InterPro
  2. 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: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0028433. Ggamma30A.

Subcellular locationi

Cell membrane Curated; Lipid-anchor Curated; Cytoplasmic side Curated

GO - Cellular componenti

  1. heterotrimeric G-protein complex Source: InterPro
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.

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.

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.
KOiK04547.
OMAiWIEEGIP.
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 [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 databases

Select the link destinations:
EMBL
GenBank
DDBJ
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; FBgn0028433.
FBtr0079796; FBpp0079396; FBgn0028433.
FBtr0079797; FBpp0079397; FBgn0028433.
FBtr0301856; FBpp0291070; FBgn0028433.
FBtr0303895; FBpp0292898; FBgn0028433.
FBtr0309247; FBpp0301186; FBgn0028433.
FBtr0330019; FBpp0303053; FBgn0028433.
GeneIDi45234.
KEGGidme:Dmel_CG3694.
dme:Dmel_CG43733.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
RefSeqi NP_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.
UniGenei Dm.1453.

3D structure databases

ProteinModelPortali Q9NFZ3.
SMRi Q9NFZ3. Positions 8-65.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 69527. 1 interaction.
IntActi Q9NFZ3. 1 interaction.

Proteomic databases

PaxDbi Q9NFZ3.
PRIDEi Q9NFZ3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0079795 ; FBpp0079395 ; FBgn0028433 .
FBtr0079796 ; FBpp0079396 ; FBgn0028433 .
FBtr0079797 ; FBpp0079397 ; FBgn0028433 .
FBtr0301856 ; FBpp0291070 ; FBgn0028433 .
FBtr0303895 ; FBpp0292898 ; FBgn0028433 .
FBtr0309247 ; FBpp0301186 ; FBgn0028433 .
FBtr0330019 ; FBpp0303053 ; FBgn0028433 .
GeneIDi 45234.
KEGGi dme:Dmel_CG3694.
dme:Dmel_CG43733.

Organism-specific databases

CTDi 45234.
FlyBasei FBgn0028433. Ggamma30A.

Phylogenomic databases

eggNOGi NOG293449.
GeneTreei ENSGT00730000114118.
InParanoidi Q9NFZ3.
KOi K04547.
OMAi WIEEGIP.
OrthoDBi EOG7H1JP7.
PhylomeDBi Q9NFZ3.

Miscellaneous databases

NextBioi 837925.
PROi Q9NFZ3.

Gene expression databases

Bgeei Q9NFZ3.

Family and domain databases

Gene3Di 4.10.260.10. 1 hit.
InterProi IPR015898. G-protein_gamma-like_dom.
IPR001770. Gprotein-gamma.
[Graphical view ]
Pfami PF00631. G-gamma. 1 hit.
[Graphical view ]
PRINTSi PR00321. GPROTEING.
SMARTi SM00224. GGL. 1 hit.
[Graphical view ]
SUPFAMi SSF48670. SSF48670. 1 hit.
PROSITEi PS50058. G_PROTEIN_GAMMA. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 108 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