GNAL_DROME
ID GNAL_DROME Reviewed; 457 AA.
AC P25157; Q7PL79; Q9U3X3;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Guanine nucleotide-binding protein subunit alpha homolog;
DE AltName: Full=Protein concertina;
GN Name=cta; Synonyms=CTR; ORFNames=CG17678;
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Oregon-R; TISSUE=Ovary;
RX PubMed=1899050; DOI=10.1016/0092-8674(91)90652-f;
RA Parks S., Wieschaus E.;
RT "The Drosophila gastrulation gene concertina encodes a G alpha-like
RT protein.";
RL Cell 64:447-458(1991).
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=Embryo;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 233-324.
RX PubMed=10748524; DOI=10.1038/74487;
RA van Steensel B., Henikoff S.;
RT "Identification of in vivo DNA targets of chromatin proteins using tethered
RT dam methyltransferase.";
RL Nat. Biotechnol. 18:424-428(2000).
CC -!- FUNCTION: May play a role in a signal transduction pathway used during
CC gastrulation. Required specifically for the ventral furrow and
CC posterior midgut invaginations, where it is necessary for coordinating
CC cell shape changes. {ECO:0000269|PubMed:1899050}.
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems. {ECO:0000269|PubMed:1899050}.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1899050}.
CC -!- TISSUE SPECIFICITY: In ovary, expressed in nurse cells and oocyte. In
CC early embryos, distributed uniformly. At the extended germband stage,
CC accumulates in the mesoderm. {ECO:0000269|PubMed:1899050}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout oogenesis. In early embryos,
CC expression drops during cellularization, remains low throughout
CC gastrulation and increases once germband extension has begun.
CC {ECO:0000269|PubMed:1899050}.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(12) subfamily.
CC {ECO:0000305}.
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DR EMBL; M94285; AAA82939.1; -; mRNA.
DR EMBL; AE014134; EAA46036.2; -; Genomic_DNA.
DR EMBL; AY089534; AAL90272.1; -; mRNA.
DR EMBL; AF211849; AAF17622.1; -; Genomic_DNA.
DR PIR; A38567; A38567.
DR RefSeq; NP_001036421.1; NM_001042956.2.
DR RefSeq; NP_001260696.1; NM_001273767.1.
DR AlphaFoldDB; P25157; -.
DR SMR; P25157; -.
DR BioGRID; 78256; 7.
DR STRING; 7227.FBpp0110418; -.
DR PaxDb; P25157; -.
DR PRIDE; P25157; -.
DR DNASU; 3355131; -.
DR EnsemblMetazoa; FBtr0111126; FBpp0110418; FBgn0000384.
DR EnsemblMetazoa; FBtr0334157; FBpp0306274; FBgn0000384.
DR GeneID; 3355131; -.
DR KEGG; dme:Dmel_CG17678; -.
DR UCSC; CG17678-RA; d. melanogaster.
DR CTD; 3355131; -.
DR FlyBase; FBgn0000384; cta.
DR VEuPathDB; VectorBase:FBgn0000384; -.
DR eggNOG; KOG0082; Eukaryota.
DR GeneTree; ENSGT00940000168398; -.
DR HOGENOM; CLU_014184_3_2_1; -.
DR InParanoid; P25157; -.
DR OMA; TSRFACM; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; P25157; -.
DR Reactome; R-DME-193648; NRAGE signals death through JNK.
DR Reactome; R-DME-416482; G alpha (12/13) signalling events.
DR Reactome; R-DME-428930; Thromboxane signalling through TP receptor.
DR Reactome; R-DME-9013148; CDC42 GTPase cycle.
DR Reactome; R-DME-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 3355131; 0 hits in 3 CRISPR screens.
DR ChiTaRS; cta; fly.
DR GenomeRNAi; 3355131; -.
DR PRO; PR:P25157; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0000384; Expressed in ovary and 12 other tissues.
DR ExpressionAtlas; P25157; baseline and differential.
DR Genevisible; P25157; DM.
DR GO; GO:0031526; C:brush border membrane; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; ISS:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0031752; F:D5 dopamine receptor binding; IBA:GO_Central.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; ISS:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070252; P:actin-mediated cell contraction; IGI:FlyBase.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0003384; P:apical constriction involved in gastrulation; IGI:FlyBase.
DR GO; GO:0060027; P:convergent extension involved in gastrulation; IMP:FlyBase.
DR GO; GO:0003380; P:establishment or maintenance of cytoskeleton polarity involved in gastrulation; IMP:FlyBase.
DR GO; GO:0010004; P:gastrulation involving germ band extension; IMP:FlyBase.
DR GO; GO:0048383; P:mesectoderm development; IMP:FlyBase.
DR GO; GO:0016476; P:regulation of embryonic cell shape; IMP:FlyBase.
DR GO; GO:0010470; P:regulation of gastrulation; IMP:FlyBase.
DR GO; GO:0043519; P:regulation of myosin II filament organization; IMP:FlyBase.
DR GO; GO:0007266; P:Rho protein signal transduction; IBA:GO_Central.
DR CDD; cd00066; G-alpha; 1.
DR Gene3D; 1.10.400.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR000469; Gprotein_alpha_12/13.
DR InterPro; IPR001019; Gprotein_alpha_su.
DR InterPro; IPR011025; GproteinA_insert.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10218; PTHR10218; 1.
DR Pfam; PF00503; G-alpha; 1.
DR PRINTS; PR00318; GPROTEINA.
DR PRINTS; PR00440; GPROTEINA12.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF47895; SSF47895; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51882; G_ALPHA; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Developmental protein; Gastrulation; GTP-binding; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome; Transducer.
FT CHAIN 1..457
FT /note="Guanine nucleotide-binding protein subunit alpha
FT homolog"
FT /id="PRO_0000203776"
FT DOMAIN 131..457
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 134..147
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 272..280
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 295..304
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 365..372
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 427..432
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 139..146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 274..280
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 299..303
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 369..372
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 429
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 457 AA; 52753 MW; D204415C4BC2CEC7 CRC64;
MSGITLTKLT QERISIPNNN VITNGVENNI DSDTLSGTLT HLMEEHRTRV GAVTGPEAAT
TSTDGLISNG AERLRLQGSR LQTSRFACFR CCGNIITYLV RLRSTPEELE QRYKSKEIDK
FLEKEKHTFR RQVKLLLLGA GESGKSTFLK QMRIIHGVNF DYELLLEYQS VIYQNVIRGM
QVLLDAREKL NIAWGSDGRE QDAYDAKLME CNSLDVPKFM EYAPPISRLW QDRGIRRAFE
RRREFQISDS VSYFLDEIQR LATPDYVPTH KDILHCRKAT KGVYEFCVKV QNIPFVFVDV
GGQRTQRQKW TRCFDSSVTS IIFLVSSSEF DQVLAEDRKT NRLEESKNIF DTIVNNATFK
GISIILFLNK TDLLEQKVCN PETDIRWYYP HFNGNPHSVL DVQNFILQMF MSVRRSSSIS
RIYHHFTTAI DTRNINVVFN SVKDTILQRN LNALMLQ
