Reviewed, UniProtKB/Swiss-Prot P25157 (GNAL_DROME)

Names and origin

Protein names

Recommended name:
    Guanine nucleotide-binding protein subunit alpha homolog
Alternative name(s):
    Protein concertina

Gene names

Name:	cta
Synonyms:	CTR
ORF Names:	CG17678

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	457 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	May play a role in a signal transduction pathway used during gastrulation. Required specifically for the ventral furrow and posterior midgut invaginations, where it is necessary for coordinating cell shape changes. Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.
Subunit structure	G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site.
Tissue specificity	Distributed uniformly.
Developmental stage	Gastrulation.
Sequence similarities	Belongs to the G-alpha family. G(12) subfamily.

Ontologies

Keywords
Biological process	Gastrulation
Ligand	GTP-binding Nucleotide-binding
Molecular function	Developmental protein Transducer
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	G-protein coupled receptor protein signaling pathway Inferred from electronic annotation. Source: InterPro gastrulation involving germ band extension Ref.1 Inferred from mutant phenotype. Source: FlyBase regulation of embryonic cell shape Ref.1 Inferred from mutant phenotype. Source: FlyBase
Cellular component	heterotrimeric G-protein complex Non-traceable author statement. Source: FlyBase
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW signal transducer activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 457	457	Guanine nucleotide-binding protein subunit alpha homolog		PRO_0000203776
Regions
	Nucleotide binding	139 – 146	8	GTP By similarity
	Nucleotide binding	299 – 303	5	GTP By similarity
	Nucleotide binding	369 – 372	4	GTP By similarity

Sequences

	Sequence		Length	Mass (Da)
	P25157-1 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: D204415C4BC2CEC7	FASTA	457	52,753
	10 20 30 40 50 60 MSGITLTKLT QERISIPNNN VITNGVENNI DSDTLSGTLT HLMEEHRTRV GAVTGPEAAT 70 80 90 100 110 120 TSTDGLISNG AERLRLQGSR LQTSRFACFR CCGNIITYLV RLRSTPEELE QRYKSKEIDK 130 140 150 160 170 180 FLEKEKHTFR RQVKLLLLGA GESGKSTFLK QMRIIHGVNF DYELLLEYQS VIYQNVIRGM 190 200 210 220 230 240 QVLLDAREKL NIAWGSDGRE QDAYDAKLME CNSLDVPKFM EYAPPISRLW QDRGIRRAFE 250 260 270 280 290 300 RRREFQISDS VSYFLDEIQR LATPDYVPTH KDILHCRKAT KGVYEFCVKV QNIPFVFVDV 310 320 330 340 350 360 GGQRTQRQKW TRCFDSSVTS IIFLVSSSEF DQVLAEDRKT NRLEESKNIF DTIVNNATFK 370 380 390 400 410 420 GISIILFLNK TDLLEQKVCN PETDIRWYYP HFNGNPHSVL DVQNFILQMF MSVRRSSSIS 430 440 450 RIYHHFTTAI DTRNINVVFN SVKDTILQRN LNALMLQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Drosophila gastrulation gene concertina encodes a G alpha-like protein." Parks S., Wieschaus E. Cell 64:447-458(1991) [PubMed: 1899050] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Oregon-R. Tissue: Ovary.
[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: 10731132] [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: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[4]	"Heterochromatic sequences in a Drosophila whole-genome shotgun assembly." Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., Karpen G.H. Genome Biol. 3:RESEARCH0085.1-RESEARCH0085.16(2002) [PubMed: 12537574] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[5]	"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: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[6]	"Identification of in vivo DNA targets of chromatin proteins using tethered dam methyltransferase." van Steensel B., Henikoff S. Nat. Biotechnol. 18:424-428(2000) [PubMed: 10748524] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 233-324.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M94285 mRNA. Translation: AAA82939.1. AE014134 Genomic DNA. Translation: EAA46036.2. AY089534 mRNA. Translation: AAL90272.1. AF211849 Genomic DNA. Translation: AAF17622.1.
PIR	A38567.
RefSeq	NP_001036421.1.
UniGene	Dm.2855
3D structure databases
HSSP	HSSP built from PDB template 1CUL based on UniProtKB P04896.
ModBase	Search...
Protein-protein interaction databases
IntAct	P25157. 3 interactions.
Proteomic databases
PRIDE	P25157.
Genome annotation databases
Ensembl	FBgn0000384. Drosophila melanogaster. [Contig view]
GeneID	3355131.
KEGG	dme:Dmel_CG17678.
Organism-specific databases
FlyBase	FBgn0000384. cta.
Phylogenomic databases
HOGENOM	P25157.
Gene expression databases
GermOnline	CG17678. Drosophila melanogaster.
Family and domain databases
InterPro	IPR001019. Gprotein_alph_bd. IPR000469. Gprotein_alpha12. [Graphical view]
PANTHER	PTHR10218. Gprotein_alph_bd. 1 hit.
Pfam	PF00503. G-alpha. 1 hit. [Graphical view]
PRINTS	PR00318. GPROTEINA. PR00440. GPROTEINA12.
ProDom	PD000281. Gprotein_alpha. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...
Other Resources
NextBio	850770.

Entry information

Entry name

GNAL_DROME

Accession

Primary (citable) accession number: P25157
Secondary accession number(s): Q7PL79, Q9U3X3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	June 16, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project