GNAO_DROME
ID GNAO_DROME Reviewed; 354 AA.
AC P16378; A4UZB6; A4UZC1; B7FF70; P16377; P16707; Q540V8; Q8IGI5; Q9V5L5;
AC Q9V5L6;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=G protein alpha o subunit;
DE AltName: Full=Guanine nucleotide-binding protein G(o) subunit alpha 47A;
GN Name=Galphao; Synonyms=G-oa47A, G-oalpha47A; ORFNames=CG2204;
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=2519611; DOI=10.1091/mbc.1.1.125;
RA Schmidt C.J., Garen-Fazio S., Chow Y.K., Neer E.J.;
RT "Neuronal expression of a newly identified Drosophila melanogaster G
RT protein alpha 0 subunit.";
RL Cell Regul. 1:125-134(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS A AND B), ALTERNATIVE
RP SPLICING, AND TISSUE SPECIFICITY.
RC TISSUE=Head;
RX PubMed=2509462; DOI=10.1016/s0021-9258(18)51501-5;
RA Yoon J., Shortridge R.D., Bloomquist B.T., Schneuwly S., Perdew M.H.,
RA Pak W.L.;
RT "Molecular characterization of Drosophila gene encoding G0 alpha subunit
RT homolog.";
RL J. Biol. Chem. 264:18536-18543(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), NUCLEOTIDE SEQUENCE [GENOMIC
RP DNA] OF 156-354, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S; TISSUE=Embryo, and Head;
RX PubMed=2509463; DOI=10.1016/s0021-9258(18)51502-7;
RA de Sousa S.M., Hoveland L.L., Yarfitz S., Hurley J.B.;
RT "The Drosophila Go alpha-like G protein gene produces multiple transcripts
RT and is expressed in the nervous system and in ovaries.";
RL J. Biol. Chem. 264:18544-18551(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), AND TISSUE SPECIFICITY.
RX PubMed=2509464; DOI=10.1016/s0021-9258(18)51503-9;
RA Thambi N.C., Quan F., Wolfgang W.J., Spiegel A., Forte M.A.;
RT "Immunological and molecular characterization of Go alpha-like proteins in
RT the Drosophila central nervous system.";
RL J. Biol. Chem. 264:18552-18560(1989).
RN [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Head, and Ovary;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley;
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=10079238; DOI=10.1242/dev.126.8.1781;
RA Granderath S., Stollewerk A., Greig S., Goodman C.S., O'Kane C.J.,
RA Klambt C.;
RT "loco encodes an RGS protein required for Drosophila glial
RT differentiation.";
RL Development 126:1781-1791(1999).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems. Plays a role in glial cell differentiation during
CC embryogenesis; loco, Galphai and the G-protein coupled receptor, moody,
CC are required in the surface glia to achieve effective insulation of the
CC nerve cord. {ECO:0000269|PubMed:10079238}.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site.
CC -!- INTERACTION:
CC P16378; Q9VB22: pins; NbExp=2; IntAct=EBI-197464, EBI-116643;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A; Synonyms=I;
CC IsoId=P16378-1; Sequence=Displayed;
CC Name=B; Synonyms=D, E, F, G, H;
CC IsoId=P16378-2; Sequence=VSP_001830;
CC -!- TISSUE SPECIFICITY: Expressed primarily in neuronal cell bodies in the
CC brain, optic lobe, and thoracic and abdominal ganglia. Also expressed
CC in antenna, oocytes and ovarian nurse cells.
CC {ECO:0000269|PubMed:2509462, ECO:0000269|PubMed:2509463,
CC ECO:0000269|PubMed:2509464, ECO:0000269|PubMed:2519611}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the surface glial cells of the nerve
CC cords at the larval stage (at protein level). Expressed throughout
CC development. {ECO:0000269|PubMed:10079238, ECO:0000269|PubMed:2509463}.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN71523.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; M86660; AAA28577.1; -; mRNA.
DR EMBL; M29602; AAA28587.1; -; mRNA.
DR EMBL; M31203; AAA28586.1; -; Genomic_DNA.
DR EMBL; M29601; AAA28586.1; JOINED; Genomic_DNA.
DR EMBL; M31198; AAA28586.1; JOINED; Genomic_DNA.
DR EMBL; M31199; AAA28586.1; JOINED; Genomic_DNA.
DR EMBL; M31200; AAA28586.1; JOINED; Genomic_DNA.
DR EMBL; M31201; AAA28586.1; JOINED; Genomic_DNA.
DR EMBL; M31202; AAA28586.1; JOINED; Genomic_DNA.
DR EMBL; M30151; AAA28584.1; -; mRNA.
DR EMBL; M30152; AAA28585.1; -; mRNA.
DR EMBL; M31129; AAA28583.1; -; Genomic_DNA.
DR EMBL; M29731; AAA28580.1; -; mRNA.
DR EMBL; M29732; AAA28581.1; -; mRNA.
DR EMBL; AE013599; AAF58789.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF58790.1; -; Genomic_DNA.
DR EMBL; AE013599; AAO41420.1; -; Genomic_DNA.
DR EMBL; AE013599; AAO41421.1; -; Genomic_DNA.
DR EMBL; AE013599; AAO41422.1; -; Genomic_DNA.
DR EMBL; AE013599; AAO41423.1; -; Genomic_DNA.
DR EMBL; AE013599; AAS64872.1; -; Genomic_DNA.
DR EMBL; AE013599; AAS64873.1; -; Genomic_DNA.
DR EMBL; AY121631; AAM51958.1; -; mRNA.
DR EMBL; BT001768; AAN71523.1; ALT_SEQ; mRNA.
DR EMBL; BT046134; ACK77603.1; -; mRNA.
DR PIR; A34304; RGFFO1.
DR PIR; B34304; RGFFO2.
DR RefSeq; NP_523684.2; NM_078960.5. [P16378-1]
DR RefSeq; NP_724934.1; NM_165772.4. [P16378-2]
DR RefSeq; NP_724935.1; NM_165773.3. [P16378-1]
DR RefSeq; NP_788304.1; NM_176124.3. [P16378-2]
DR RefSeq; NP_788305.1; NM_176125.3. [P16378-2]
DR RefSeq; NP_788306.1; NM_176126.3. [P16378-2]
DR RefSeq; NP_788307.1; NM_176127.3. [P16378-2]
DR RefSeq; NP_995801.1; NM_206079.2. [P16378-1]
DR RefSeq; NP_995802.1; NM_206080.2. [P16378-2]
DR AlphaFoldDB; P16378; -.
DR SMR; P16378; -.
DR BioGRID; 61922; 29.
DR DIP; DIP-17224N; -.
DR IntAct; P16378; 6.
DR STRING; 7227.FBpp0087359; -.
DR PaxDb; P16378; -.
DR PRIDE; P16378; -.
DR DNASU; 36104; -.
DR EnsemblMetazoa; FBtr0088264; FBpp0087359; FBgn0001122. [P16378-2]
DR EnsemblMetazoa; FBtr0088265; FBpp0087360; FBgn0001122. [P16378-1]
DR EnsemblMetazoa; FBtr0088266; FBpp0087361; FBgn0001122. [P16378-1]
DR EnsemblMetazoa; FBtr0088267; FBpp0087362; FBgn0001122. [P16378-2]
DR EnsemblMetazoa; FBtr0088268; FBpp0087363; FBgn0001122. [P16378-2]
DR EnsemblMetazoa; FBtr0088269; FBpp0087364; FBgn0001122. [P16378-2]
DR EnsemblMetazoa; FBtr0088270; FBpp0087365; FBgn0001122. [P16378-2]
DR EnsemblMetazoa; FBtr0088271; FBpp0089315; FBgn0001122. [P16378-2]
DR EnsemblMetazoa; FBtr0088272; FBpp0089316; FBgn0001122. [P16378-1]
DR GeneID; 36104; -.
DR KEGG; dme:Dmel_CG2204; -.
DR CTD; 36104; -.
DR FlyBase; FBgn0001122; Galphao.
DR VEuPathDB; VectorBase:FBgn0001122; -.
DR eggNOG; KOG0082; Eukaryota.
DR GeneTree; ENSGT00940000155883; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; P16378; -.
DR OMA; QVIWADA; -.
DR PhylomeDB; P16378; -.
DR Reactome; R-DME-4086398; Ca2+ pathway.
DR SignaLink; P16378; -.
DR BioGRID-ORCS; 36104; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Galphao; fly.
DR GenomeRNAi; 36104; -.
DR PRO; PR:P16378; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0001122; Expressed in brain and 43 other tissues.
DR ExpressionAtlas; P16378; baseline and differential.
DR Genevisible; P16378; DM.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; HDA:FlyBase.
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; IDA:FlyBase.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0008356; P:asymmetric cell division; IMP:FlyBase.
DR GO; GO:0032291; P:axon ensheathment in central nervous system; IMP:UniProtKB.
DR GO; GO:0042595; P:behavioral response to starvation; IMP:FlyBase.
DR GO; GO:0019722; P:calcium-mediated signaling; IMP:FlyBase.
DR GO; GO:0061343; P:cell adhesion involved in heart morphogenesis; IMP:FlyBase.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0060857; P:establishment of glial blood-brain barrier; IMP:FlyBase.
DR GO; GO:0001737; P:establishment of imaginal disc-derived wing hair orientation; IMP:FlyBase.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0007507; P:heart development; TAS:FlyBase.
DR GO; GO:0045886; P:negative regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR GO; GO:0035567; P:non-canonical Wnt signaling pathway; IMP:FlyBase.
DR GO; GO:0050916; P:sensory perception of sweet taste; IMP:FlyBase.
DR GO; GO:0019991; P:septate junction assembly; IMP:FlyBase.
DR GO; GO:0007419; P:ventral cord development; IMP:FlyBase.
DR CDD; cd00066; G-alpha; 1.
DR Gene3D; 1.10.400.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR001408; Gprotein_alpha_I.
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; PR00441; GPROTEINAI.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF47895; SSF47895; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51882; G_ALPHA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; GTP-binding; Lipoprotein; Magnesium; Metal-binding;
KW Myristate; Nucleotide-binding; Palmitate; Reference proteome; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..354
FT /note="G protein alpha o subunit"
FT /id="PRO_0000203716"
FT DOMAIN 32..354
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 35..48
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 174..182
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 197..206
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 266..273
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 324..329
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 40..47
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 176..182
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 201..205
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 270..273
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 4..21
FT /note="AQSAEERAAAARSRLIER -> TTSAEERAAIQRSKQIEK (in isoform
FT B)"
FT /evidence="ECO:0000303|PubMed:2509462,
FT ECO:0000303|PubMed:2509463, ECO:0000303|PubMed:2509464,
FT ECO:0000303|PubMed:2519611"
FT /id="VSP_001830"
FT CONFLICT 88
FT /note="M -> I (in Ref. 3; AAA28585)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 40476 MW; 3C5DA142B4CF7DD2 CRC64;
MGCAQSAEER AAAARSRLIE RNLKEDGIQA AKDIKLLLLG AGESGKSTIV KQMKIIHESG
FTAEDFKQYR PVVYSNTIQS LVAILRAMPT LSIQYSNNER ESDAKMVFDV CQRMHDTEPF
SEELLAAMKR LWQDAGVQEC FSRSNEYQLN DSAKYFLDDL DRLGAKDYQP TEQDILRTRV
KTTGIVEVHF SFKNLNFKLF DVGGQRSERK KWIHCFEDVT AIIFCVAMSE YDQVLHEDET
TNRMQESLKL FDSICNNKWF TDTSIILFLN KKDLFEEKIR KSPLTICFPE YTGGQEYGEA
AAYIQAQFEA KNKSTSKEIY CHMTCATDTN NIQFVFDAVT DVIIANNLRG CGLY
