GBGE_DROME
ID GBGE_DROME Reviewed; 72 AA.
AC Q9NFZ3; A4V0H1; Q95RZ3; Q9VLD3;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Guanine nucleotide-binding protein subunit gamma-e;
DE Short=Ggamma(e);
DE Flags: Precursor;
GN Name=Ggamma30A {ECO:0000312|FlyBase:FBgn0267252}; Synonyms=Gy30A;
GN ORFNames=CG3694 {ECO:0000312|FlyBase:FBgn0267252};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Eye;
RX PubMed=10608815; DOI=10.1074/jbc.274.53.37605;
RA Schulz S., Huber A., Schwab K., Paulsen R.;
RT "A novel Ggamma isolated from Drosophila constitutes a visual G protein
RT gamma subunit of the fly compound eye.";
RL J. Biol. Chem. 274:37605-37610(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP ACETYLATION AT ASP-2, ISOPRENYLATION AT CYS-69, METHYLATION AT CYS-69, AND
RP MUTAGENESIS OF CYS-69.
RX PubMed=15205461; DOI=10.1074/jbc.m404611200;
RA Schillo S., Belusic G., Hartmann K., Franz C., Kuhl B., Brenner-Weiss G.,
RA Paulsen R., Huber A.;
RT "Targeted mutagenesis of the farnesylation site of Drosophila Ggammae
RT disrupts membrane association of the G protein betagamma complex and
RT affects the light sensitivity of the visual system.";
RL J. Biol. Chem. 279:36309-36316(2004).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as a modulator or transducer in various transmembrane signaling
CC systems. The beta and gamma chains are required for the GTPase
CC activity, for replacement of GDP by GTP, and for G protein-effector
CC interaction. This subunit functions in visual transduction in the
CC compound eye.
CC -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma.
CC -!- INTERACTION:
CC Q9NFZ3; P29829: Gbeta76C; NbExp=2; IntAct=EBI-2695634, EBI-128499;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the G protein gamma family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL28579.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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DR EMBL; AJ250440; CAB70093.1; -; mRNA.
DR EMBL; AE014134; AAF52759.2; -; Genomic_DNA.
DR EMBL; AE014134; AAF52760.2; -; Genomic_DNA.
DR EMBL; AE014134; AAF52761.2; -; Genomic_DNA.
DR EMBL; AY061031; AAL28579.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001162918.1; NM_001169447.2.
DR RefSeq; NP_001188749.1; NM_001201820.2.
DR RefSeq; NP_001245950.1; NM_001259021.2.
DR RefSeq; NP_524807.1; NM_080068.4.
DR RefSeq; NP_723451.1; NM_164851.3.
DR RefSeq; NP_723452.1; NM_164852.3.
DR AlphaFoldDB; Q9NFZ3; -.
DR SMR; Q9NFZ3; -.
DR BioGRID; 69527; 1.
DR IntAct; Q9NFZ3; 1.
DR STRING; 7227.FBpp0291070; -.
DR iPTMnet; Q9NFZ3; -.
DR PaxDb; Q9NFZ3; -.
DR DNASU; 45234; -.
DR EnsemblMetazoa; FBtr0079795; FBpp0079395; FBgn0267252.
DR EnsemblMetazoa; FBtr0079796; FBpp0079396; FBgn0267252.
DR EnsemblMetazoa; FBtr0079797; FBpp0079397; FBgn0267252.
DR EnsemblMetazoa; FBtr0303895; FBpp0292898; FBgn0267252.
DR EnsemblMetazoa; FBtr0309247; FBpp0301186; FBgn0267252.
DR EnsemblMetazoa; FBtr0330019; FBpp0303053; FBgn0267252.
DR GeneID; 45234; -.
DR KEGG; dme:Dmel_CG3694; -.
DR CTD; 45234; -.
DR FlyBase; FBgn0267252; Ggamma30A.
DR VEuPathDB; VectorBase:FBgn0267252; -.
DR eggNOG; KOG4119; Eukaryota.
DR HOGENOM; CLU_1295607_0_0_1; -.
DR InParanoid; Q9NFZ3; -.
DR OMA; MDEWELP; -.
DR OrthoDB; 1597581at2759; -.
DR PhylomeDB; Q9NFZ3; -.
DR Reactome; R-DME-1296041; Activation of G protein gated Potassium channels.
DR Reactome; R-DME-202040; G-protein activation.
DR Reactome; R-DME-381753; Olfactory Signaling Pathway.
DR Reactome; R-DME-392170; ADP signalling through P2Y purinoceptor 12.
DR Reactome; R-DME-392451; G beta:gamma signalling through PI3Kgamma.
DR Reactome; R-DME-392851; Prostacyclin signalling through prostacyclin receptor.
DR Reactome; R-DME-400042; Adrenaline,noradrenaline inhibits insulin secretion.
DR Reactome; R-DME-4086398; Ca2+ pathway.
DR Reactome; R-DME-416476; G alpha (q) signalling events.
DR Reactome; R-DME-416482; G alpha (12/13) signalling events.
DR Reactome; R-DME-418217; G beta:gamma signalling through PLC beta.
DR Reactome; R-DME-418555; G alpha (s) signalling events.
DR Reactome; R-DME-418594; G alpha (i) signalling events.
DR Reactome; R-DME-418597; G alpha (z) signalling events.
DR Reactome; R-DME-428930; Thromboxane signalling through TP receptor.
DR Reactome; R-DME-500657; Presynaptic function of Kainate receptors.
DR Reactome; R-DME-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR Reactome; R-DME-8964315; G beta:gamma signalling through BTK.
DR Reactome; R-DME-8964616; G beta:gamma signalling through CDC42.
DR Reactome; R-DME-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-DME-9717207; Sensory perception of sweet, bitter, and umami (glutamate) taste.
DR Reactome; R-DME-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR BioGRID-ORCS; 45234; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 45234; -.
DR PRO; PR:Q9NFZ3; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0267252; Expressed in brain and 21 other tissues.
DR ExpressionAtlas; Q9NFZ3; baseline and differential.
DR Genevisible; Q9NFZ3; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IPI:FlyBase.
DR GO; GO:0016028; C:rhabdomere; IDA:FlyBase.
DR GO; GO:0031681; F:G-protein beta-subunit binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:FlyBase.
DR GO; GO:0071244; P:cellular response to carbon dioxide; IMP:FlyBase.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0007602; P:phototransduction; IPI:FlyBase.
DR GO; GO:0050909; P:sensory perception of taste; IEA:InterPro.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd00068; GGL; 1.
DR Gene3D; 4.10.260.10; -; 1.
DR InterPro; IPR015898; G-protein_gamma-like_dom.
DR InterPro; IPR036284; GGL_sf.
DR InterPro; IPR039227; GNG13.
DR InterPro; IPR001770; Gprotein-gamma.
DR PANTHER; PTHR15936; PTHR15936; 1.
DR Pfam; PF00631; G-gamma; 1.
DR PRINTS; PR00321; GPROTEING.
DR SMART; SM00224; GGL; 1.
DR SUPFAM; SSF48670; SSF48670; 1.
DR PROSITE; PS50058; G_PROTEIN_GAMMA; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Lipoprotein; Membrane; Methylation;
KW Prenylation; Reference proteome; Sensory transduction; Transducer; Vision.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:15205461"
FT CHAIN 2..69
FT /note="Guanine nucleotide-binding protein subunit gamma-e"
FT /id="PRO_0000012679"
FT PROPEP 70..72
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000012680"
FT MOD_RES 2
FT /note="N-acetylaspartate"
FT /evidence="ECO:0000269|PubMed:15205461"
FT MOD_RES 69
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000269|PubMed:15205461"
FT LIPID 69
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:15205461"
FT MUTAGEN 69
FT /note="C->G: Loss of farnesylation."
FT /evidence="ECO:0000269|PubMed:15205461"
SQ SEQUENCE 72 AA; 8398 MW; B0FC6DC9170EDA70 CRC64;
MDPSALQNMD RDALKKQIEN MKYQASMERW PLSKSIAEMR SFIEENEKND PLINAPDKKN
NPWAEKGKCV IM
