Q9NFZ3 (GBGE_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Guanine nucleotide-binding protein subunit gamma-e
Short name=Ggamma(e)

Gene names

Name:	Ggamma30A
ORF Names:	CG3694

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	72 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	G proteins are composed of 3 units, alpha, beta and gamma.
Subcellular location	Cell membrane; Lipid-anchor; Cytoplasmic side Potential.
Sequence similarities	Belongs to the G protein gamma family.
Sequence caution	The sequence AAL28579.1 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.

Ontologies

Keywords
Biological process	Sensory transduction Vision
Cellular component	Cell membrane Membrane
Molecular function	Transducer
PTM	Acetylation Lipoprotein Methylation Prenylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G-protein coupled receptor signaling pathway Inferred from electronic annotation. Source: InterPro cellular response to carbon dioxide Inferred from mutant phenotype PubMed 20357107. Source: FlyBase phototransduction Inferred from physical interaction Ref.1. Source: FlyBase visual perception Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay Ref.1. Source: FlyBase heterotrimeric G-protein complex Inferred from physical interaction Ref.1. Source: FlyBase rhabdomere Inferred from direct assay Ref.1. Source: FlyBase
Molecular_function	signal transducer activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Gbeta76C	P29829	2	EBI-2695634,EBI-128499

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 69	68	Guanine nucleotide-binding protein subunit gamma-e		PRO_0000012679
	Propeptide	70 – 72	3	Removed in mature form By similarity		PRO_0000012680
Amino acid modifications
	Modified residue	2	1	N-acetylaspartate Ref.5
	Modified residue	69	1	Cysteine methyl ester Ref.5
	Lipidation	69	1	S-farnesyl cysteine Ref.5
Experimental info
	Mutagenesis	69	1	C → G: Loss of farnesylation. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q9NFZ3 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: B0FC6DC9170EDA70	FASTA	72	8,398
	10 20 30 40 50 60 MDPSALQNMD RDALKKQIEN MKYQASMERW PLSKSIAEMR SFIEENEKND PLINAPDKKN 70 NPWAEKGKCV IM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[4]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
RefSeq	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.
UniGene	Dm.1453.
3D structure databases
ProteinModelPortal	Q9NFZ3.
SMR	Q9NFZ3. Positions 8-65.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NFZ3. 1 interaction.
Proteomic databases
PaxDb	Q9NFZ3.
PRIDE	Q9NFZ3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0079795; FBpp0079395; FBgn0028433. FBtr0079796; FBpp0079396; FBgn0028433. FBtr0079797; FBpp0079397; FBgn0028433. FBtr0301856; FBpp0291070; FBgn0028433. FBtr0303895; FBpp0292898; FBgn0028433. FBtr0309247; FBpp0301186; FBgn0028433. FBtr0330019; FBpp0303053; FBgn0028433.
GeneID	14462729. 45234.
KEGG	dme:Dmel_CG3694.
Organism-specific databases
CTD	45234.
FlyBase	FBgn0028433. Ggamma30A.
Phylogenomic databases
eggNOG	NOG293449.
GeneTree	ENSGT00530000064157.
InParanoid	Q9NFZ3.
KO	K04547.
OMA	EKGKCSI.
OrthoDB	EOG4MW6PN.
PhylomeDB	Q9NFZ3.
Gene expression databases
Bgee	Q9NFZ3.
GermOnline	CG3694. Drosophila melanogaster.
Family and domain databases
Gene3D	4.10.260.10. 1 hit.
InterPro	IPR015898. G-protein_gamma-like_dom. IPR001770. Gprotein-gamma. [Graphical view]
Pfam	PF00631. G-gamma. 1 hit. [Graphical view]
PRINTS	PR00321. GPROTEING.
SMART	SM00224. GGL. 1 hit. [Graphical view]
SUPFAM	SSF48670. G-protein_gamma-like. 1 hit.
PROSITE	PS50058. G_PROTEIN_GAMMA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	45234.
NextBio	837925.

Entry information

Entry name

GBGE_DROME

Accession

Primary (citable) accession number: Q9NFZ3
Secondary accession number(s): A4V0H1, Q95RZ3, Q9VLD3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2001
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project