GNAS_DROME
ID GNAS_DROME Reviewed; 385 AA.
AC P20354; E1JGV3; P20355; Q2MGN1; Q9W1F9;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=G protein alpha s subunit;
DE AltName: Full=Adenylate cyclase-stimulating G alpha protein;
DE AltName: Full=Guanine nucleotide-binding protein G(s) subunit alpha;
GN Name=Galphas; Synonyms=G-sa60A, G-salpha60A; ORFNames=CG2835;
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] (ISOFORM B), AND TISSUE SPECIFICITY.
RX PubMed=2498884; DOI=10.1073/pnas.86.11.4321;
RA Quan F., Wolfgang W.J., Forte M.A.;
RT "The Drosophila gene coding for the alpha subunit of a stimulatory G
RT protein is preferentially expressed in the nervous system.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:4321-4325(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=2106072; DOI=10.1128/mcb.10.3.910-917.1990;
RA Quan F., Forte M.A.;
RT "Two forms of Drosophila melanogaster Gs alpha are produced by alternate
RT splicing involving an unusual splice site.";
RL Mol. Cell. Biol. 10:910-917(1990).
RN [3]
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 [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
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).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems. The G(s) protein is involved in hormonal regulation of
CC adenylate cyclase: it activates the cyclase (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B; Synonyms=D;
CC IsoId=P20354-1; Sequence=Displayed;
CC Name=A; Synonyms=C;
CC IsoId=P20354-2; Sequence=VSP_001831;
CC -!- TISSUE SPECIFICITY: Preferentially expressed in the nervous system and
CC in the eyes. {ECO:0000269|PubMed:2498884}.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(s) subfamily.
CC {ECO:0000305}.
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DR EMBL; M23233; AAA28917.1; -; mRNA.
DR EMBL; M33998; AAA28578.1; -; Genomic_DNA.
DR EMBL; M33997; AAA28578.1; JOINED; Genomic_DNA.
DR EMBL; M33998; AAA28579.1; -; Genomic_DNA.
DR EMBL; M33997; AAA28579.1; JOINED; Genomic_DNA.
DR EMBL; AE013599; AAF47108.2; -; Genomic_DNA.
DR EMBL; AE013599; AAM68282.2; -; Genomic_DNA.
DR EMBL; AE013599; ACZ94555.1; -; Genomic_DNA.
DR EMBL; AY058572; AAL13801.1; -; mRNA.
DR PIR; A34754; RGFFAL.
DR PIR; B34754; RGFFAS.
DR RefSeq; NP_001163283.1; NM_001169812.2. [P20354-1]
DR RefSeq; NP_001286798.1; NM_001299869.1. [P20354-2]
DR RefSeq; NP_477505.1; NM_058157.5. [P20354-1]
DR RefSeq; NP_477506.1; NM_058158.5. [P20354-2]
DR RefSeq; NP_726388.1; NM_166640.3. [P20354-2]
DR AlphaFoldDB; P20354; -.
DR SMR; P20354; -.
DR BioGRID; 63395; 16.
DR DIP; DIP-19026N; -.
DR IntAct; P20354; 5.
DR STRING; 7227.FBpp0072052; -.
DR SwissPalm; P20354; -.
DR PaxDb; P20354; -.
DR PRIDE; P20354; -.
DR DNASU; 37805; -.
DR EnsemblMetazoa; FBtr0072142; FBpp0072051; FBgn0001123. [P20354-2]
DR EnsemblMetazoa; FBtr0072143; FBpp0072052; FBgn0001123. [P20354-1]
DR EnsemblMetazoa; FBtr0072144; FBpp0072053; FBgn0001123. [P20354-2]
DR EnsemblMetazoa; FBtr0301411; FBpp0290625; FBgn0001123. [P20354-1]
DR EnsemblMetazoa; FBtr0343279; FBpp0309944; FBgn0001123. [P20354-2]
DR GeneID; 37805; -.
DR KEGG; dme:Dmel_CG2835; -.
DR CTD; 37805; -.
DR FlyBase; FBgn0001123; Galphas.
DR VEuPathDB; VectorBase:FBgn0001123; -.
DR eggNOG; KOG0099; Eukaryota.
DR GeneTree; ENSGT00940000172018; -.
DR InParanoid; P20354; -.
DR OMA; QENRATC; -.
DR PhylomeDB; P20354; -.
DR Reactome; R-DME-170660; Adenylate cyclase activating pathway.
DR Reactome; R-DME-170670; Adenylate cyclase inhibitory pathway.
DR Reactome; R-DME-381753; Olfactory Signaling Pathway.
DR Reactome; R-DME-392851; Prostacyclin signalling through prostacyclin receptor.
DR Reactome; R-DME-418555; G alpha (s) signalling events.
DR SignaLink; P20354; -.
DR BioGRID-ORCS; 37805; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Galphas; fly.
DR GenomeRNAi; 37805; -.
DR PRO; PR:P20354; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0001123; Expressed in eye disc (Drosophila) and 42 other tissues.
DR ExpressionAtlas; P20354; baseline and differential.
DR Genevisible; P20354; DM.
DR GO; GO:0005604; C:basement membrane; IDA:FlyBase.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0045202; C:synapse; IEA:GOC.
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; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0048148; P:behavioral response to cocaine; NAS:FlyBase.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:FlyBase.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IGI:FlyBase.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0002165; P:instar larval or pupal development; NAS:FlyBase.
DR GO; GO:0007611; P:learning or memory; NAS:FlyBase.
DR GO; GO:0007528; P:neuromuscular junction development; IMP:FlyBase.
DR GO; GO:2000253; P:positive regulation of feeding behavior; IGI:FlyBase.
DR GO; GO:0010353; P:response to trehalose; IMP:FlyBase.
DR GO; GO:0007606; P:sensory perception of chemical stimulus; IBA:GO_Central.
DR GO; GO:0050916; P:sensory perception of sweet taste; IMP:FlyBase.
DR GO; GO:0007632; P:visual behavior; NAS:FlyBase.
DR CDD; cd00066; G-alpha; 1.
DR Gene3D; 1.10.400.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR000367; Gprotein_alpha_S.
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; PR00443; GPROTEINAS.
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 Alternative splicing; GTP-binding; Lipoprotein; Magnesium; Metal-binding;
KW Nucleotide-binding; Palmitate; Reference proteome; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..385
FT /note="G protein alpha s subunit"
FT /id="PRO_0000203731"
FT DOMAIN 42..385
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..58
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 184..192
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 207..216
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 276..283
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 355..360
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 50..57
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 186..192
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 211..215
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 280..283
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 357
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-palmitoyl glycine"
FT /evidence="ECO:0000250"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 310..313
FT /note="IDTG -> S (in isoform A)"
FT /evidence="ECO:0000305"
FT /id="VSP_001831"
SQ SEQUENCE 385 AA; 44999 MW; CC9F004F314AC48F CRC64;
MGCFGSPTSK QSDVNSEDSK SQKRRSDAIS RQLQKDKQLY RATHRLLLLG AGESGKSTIV
KQMRILHVDG FSDSEKKQKI DDIKKNIRDA ILTITGAMST LNPPVALEKK ENEPRVEYIQ
DYASSPDFNY PPEFYEHTEE LWKDKGVLQT YERSNEYQLI DCAKYFLDRV STIKNPNYTP
NEQDILRCRV LTSGIFETRF QVDKVNFHMF DVGGQRDERR KWIQCFNDVT AIIFVTACSS
YNMVLREDPT QNRLRESLDL FKSIWNNRWL RTISIILFLN KQDLLAEKIK AGKSKLSEYF
SEFNKYQTPI DTGDAIMESN DDPEVIRAKY FIRDEFLRIS TASGDGKHYC YPHFTCAVDT
ENIKRVFNDC RDIIQRMHLR QYELL
