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Protein

Guanine nucleotide-binding protein subunit alpha homolog

Gene

cta

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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.1 Publication
Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi146 – 1461MagnesiumBy similarity
Metal bindingi280 – 2801MagnesiumBy similarity
Binding sitei429 – 4291GTP; via amide nitrogenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi139 – 1468GTPBy similarity
Nucleotide bindingi274 – 2807GTPBy similarity
Nucleotide bindingi299 – 3035GTPBy similarity
Nucleotide bindingi369 – 3724GTPBy similarity

GO - Molecular functioni

GO - Biological processi

  • actin-mediated cell contraction Source: FlyBase
  • adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: GO_Central
  • apical constriction involved in gastrulation Source: FlyBase
  • cell surface receptor signaling pathway Source: FlyBase
  • convergent extension involved in gastrulation Source: FlyBase
  • establishment or maintenance of cytoskeleton polarity involved in gastrulation Source: FlyBase
  • gastrulation Source: FlyBase
  • gastrulation involving germ band extension Source: FlyBase
  • mesectoderm development Source: FlyBase
  • posterior midgut invagination Source: FlyBase
  • regulation of cell shape Source: FlyBase
  • regulation of embryonic cell shape Source: FlyBase
  • regulation of gastrulation Source: FlyBase
  • regulation of myosin II filament organization Source: FlyBase
  • Rho protein signal transduction Source: GO_Central
  • ventral furrow formation Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Transducer

Keywords - Biological processi

Gastrulation

Keywords - Ligandi

GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-DME-416482. G alpha (12/13) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide-binding protein subunit alpha homolog
Alternative name(s):
Protein concertina
Gene namesi
Name:cta
Synonyms:CTR
ORF Names:CG17678
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0000384. cta.

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

  • brush border membrane Source: GO_Central
  • cytoplasm Source: UniProtKB-SubCell
  • heterotrimeric G-protein complex Source: GO_Central
  • plasma membrane Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 457457Guanine nucleotide-binding protein subunit alpha homologPRO_0000203776Add
BLAST

Proteomic databases

PaxDbiP25157.
PRIDEiP25157.

Expressioni

Tissue specificityi

In ovary, expressed in nurse cells and oocyte. In early embryos, distributed uniformly. At the extended germband stage, accumulates in the mesoderm.1 Publication

Developmental stagei

Expressed throughout oogenesis. In early embryos, expression drops during cellularization, remains low throughout gastrulation and increases once germband extension has begun.1 Publication

Gene expression databases

ExpressionAtlasiP25157. differential.
GenevisibleiP25157. DM.

Interactioni

Subunit structurei

G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi78256. 3 interactions.
MINTiMINT-1568125.
STRINGi7227.FBpp0110418.

Structurei

3D structure databases

ProteinModelPortaliP25157.
SMRiP25157. Positions 107-451.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the G-alpha family. G(12) subfamily.Curated

Phylogenomic databases

eggNOGiKOG0082. Eukaryota.
ENOG410XNVQ. LUCA.
GeneTreeiENSGT00770000120503.
InParanoidiP25157.
KOiK04346.
OMAiCFPGCVL.
OrthoDBiEOG7HF1JF.
PhylomeDBiP25157.

Family and domain databases

Gene3Di1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR000469. Gprotein_alpha_12/13.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10218. PTHR10218. 1 hit.
PfamiPF00503. G-alpha. 1 hit.
[Graphical view]
PRINTSiPR00318. GPROTEINA.
PR00440. GPROTEINA12.
SMARTiSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.

Sequencei

Sequence statusi: Complete.

P25157-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGITLTKLT QERISIPNNN VITNGVENNI DSDTLSGTLT HLMEEHRTRV
60 70 80 90 100
GAVTGPEAAT TSTDGLISNG AERLRLQGSR LQTSRFACFR CCGNIITYLV
110 120 130 140 150
RLRSTPEELE QRYKSKEIDK FLEKEKHTFR RQVKLLLLGA GESGKSTFLK
160 170 180 190 200
QMRIIHGVNF DYELLLEYQS VIYQNVIRGM QVLLDAREKL NIAWGSDGRE
210 220 230 240 250
QDAYDAKLME CNSLDVPKFM EYAPPISRLW QDRGIRRAFE RRREFQISDS
260 270 280 290 300
VSYFLDEIQR LATPDYVPTH KDILHCRKAT KGVYEFCVKV QNIPFVFVDV
310 320 330 340 350
GGQRTQRQKW TRCFDSSVTS IIFLVSSSEF DQVLAEDRKT NRLEESKNIF
360 370 380 390 400
DTIVNNATFK GISIILFLNK TDLLEQKVCN PETDIRWYYP HFNGNPHSVL
410 420 430 440 450
DVQNFILQMF MSVRRSSSIS RIYHHFTTAI DTRNINVVFN SVKDTILQRN

LNALMLQ
Length:457
Mass (Da):52,753
Last modified:May 1, 1992 - v1
Checksum:iD204415C4BC2CEC7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M94285 mRNA. Translation: AAA82939.1.
AE014134 Genomic DNA. Translation: EAA46036.2.
AY089534 mRNA. Translation: AAL90272.1.
AF211849 Genomic DNA. Translation: AAF17622.1.
PIRiA38567.
RefSeqiNP_001036421.1. NM_001042956.2.
NP_001260696.1. NM_001273767.1.
UniGeneiDm.2855.

Genome annotation databases

EnsemblMetazoaiFBtr0111126; FBpp0110418; FBgn0000384.
FBtr0334157; FBpp0306274; FBgn0000384.
GeneIDi3355131.
KEGGidme:Dmel_CG17678.
UCSCiCG17678-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M94285 mRNA. Translation: AAA82939.1.
AE014134 Genomic DNA. Translation: EAA46036.2.
AY089534 mRNA. Translation: AAL90272.1.
AF211849 Genomic DNA. Translation: AAF17622.1.
PIRiA38567.
RefSeqiNP_001036421.1. NM_001042956.2.
NP_001260696.1. NM_001273767.1.
UniGeneiDm.2855.

3D structure databases

ProteinModelPortaliP25157.
SMRiP25157. Positions 107-451.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi78256. 3 interactions.
MINTiMINT-1568125.
STRINGi7227.FBpp0110418.

Proteomic databases

PaxDbiP25157.
PRIDEiP25157.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0111126; FBpp0110418; FBgn0000384.
FBtr0334157; FBpp0306274; FBgn0000384.
GeneIDi3355131.
KEGGidme:Dmel_CG17678.
UCSCiCG17678-RA. d. melanogaster.

Organism-specific databases

CTDi3355131.
FlyBaseiFBgn0000384. cta.

Phylogenomic databases

eggNOGiKOG0082. Eukaryota.
ENOG410XNVQ. LUCA.
GeneTreeiENSGT00770000120503.
InParanoidiP25157.
KOiK04346.
OMAiCFPGCVL.
OrthoDBiEOG7HF1JF.
PhylomeDBiP25157.

Enzyme and pathway databases

ReactomeiR-DME-416482. G alpha (12/13) signalling events.

Miscellaneous databases

ChiTaRSicta. fly.
GenomeRNAii3355131.
PROiP25157.

Gene expression databases

ExpressionAtlasiP25157. differential.
GenevisibleiP25157. DM.

Family and domain databases

Gene3Di1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR000469. Gprotein_alpha_12/13.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10218. PTHR10218. 1 hit.
PfamiPF00503. G-alpha. 1 hit.
[Graphical view]
PRINTSiPR00318. GPROTEINA.
PR00440. GPROTEINA12.
SMARTiSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Drosophila gastrulation gene concertina encodes a G alpha-like protein."
    Parks S., Wieschaus E.
    Cell 64:447-458(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    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] [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: Embryo.
  5. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 233-324.

Entry informationi

Entry nameiGNAL_DROME
AccessioniPrimary (citable) accession number: P25157
Secondary accession number(s): Q7PL79, Q9U3X3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: July 6, 2016
This is version 135 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.