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Q9NFZ3

- GBGE_DROME

UniProt

Q9NFZ3 - GBGE_DROME

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
  1. 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. protein binding Source: IntAct
    2. signal transducer activity Source: UniProtKB-KW

    GO - Biological processi

    1. G-protein coupled receptor signaling pathway Source: InterPro
    2. visual perception Source: UniProtKB-KW

    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

    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.

    Q9NFZ3-1 [UniParc]FASTAAdd to Basket

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    MDPSALQNMD RDALKKQIEN MKYQASMERW PLSKSIAEMR SFIEENEKND   50
    PLINAPDKKN NPWAEKGKCV IM 72
    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_001260281.1. NM_001273352.1.
    NP_001260282.1. NM_001273353.1.
    NP_001260283.1. NM_001273354.1.
    NP_001260284.1. NM_001273355.1.
    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.
    GeneIDi14462729.
    45234.
    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_001260281.1. NM_001273352.1.
    NP_001260282.1. NM_001273353.1.
    NP_001260283.1. NM_001273354.1.
    NP_001260284.1. NM_001273355.1.
    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 14462729.
    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

    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 1, 2014
    This is version 107 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