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G protein alpha o subunit (Guanine nucleotide-binding protein G(o) subunit alpha 47A)

 GNAO_DROME              Reviewed;         354 AA.
P16378; A4UZB6; A4UZC1; B7FF70; P16377; P16707; Q540V8; Q8IGI5;
Q9V5L5; Q9V5L6;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
01-AUG-1990, sequence version 1.
25-OCT-2017, entry version 173.
RecName: Full=G protein alpha o subunit;
AltName: Full=Guanine nucleotide-binding protein G(o) subunit alpha 47A;
Name=Galphao; Synonyms=G-oa47A, G-oalpha47A; ORFNames=CG2204;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND TISSUE SPECIFICITY.
PubMed=2519611;
Schmidt C.J., Garen-Fazio S., Chow Y.K., Neer E.J.;
"Neuronal expression of a newly identified Drosophila melanogaster G
protein alpha 0 subunit.";
Cell Regul. 1:125-134(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS A AND B),
ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
TISSUE=Head;
PubMed=2509462;
Yoon J., Shortridge R.D., Bloomquist B.T., Schneuwly S., Perdew M.H.,
Pak W.L.;
"Molecular characterization of Drosophila gene encoding G0 alpha
subunit homolog.";
J. Biol. Chem. 264:18536-18543(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), NUCLEOTIDE SEQUENCE
[GENOMIC DNA] OF 156-354, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
STRAIN=Canton-S; TISSUE=Embryo, and Head;
PubMed=2509463;
de Sousa S.M., Hoveland L.L., Yarfitz S., Hurley J.B.;
"The Drosophila Go alpha-like G protein gene produces multiple
transcripts and is expressed in the nervous system and in ovaries.";
J. Biol. Chem. 264:18544-18551(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), AND TISSUE SPECIFICITY.
PubMed=2509464;
Thambi N.C., Quan F., Wolfgang W.J., Spiegel A., Forte M.A.;
"Immunological and molecular characterization of Go alpha-like
proteins in the Drosophila central nervous system.";
J. Biol. Chem. 264:18552-18560(1989).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[6]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
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.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
STRAIN=Berkeley; TISSUE=Head, and Ovary;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
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.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
STRAIN=Berkeley;
Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
[9]
FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=10079238;
Granderath S., Stollewerk A., Greig S., Goodman C.S., O'Kane C.J.,
Klambt C.;
"loco encodes an RGS protein required for Drosophila glial
differentiation.";
Development 126:1781-1791(1999).
-!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are
involved as modulators or transducers in various transmembrane
signaling systems. Plays a role in glial cell differentiation
during embryogenesis; loco, Galphai and the G-protein coupled
receptor, moody, are required in the surface glia to achieve
effective insulation of the nerve cord.
{ECO:0000269|PubMed:10079238}.
-!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and
gamma. The alpha chain contains the guanine nucleotide binding
site.
-!- INTERACTION:
Q9VB22:pins; NbExp=2; IntAct=EBI-197464, EBI-116643;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=A; Synonyms=I;
IsoId=P16378-1; Sequence=Displayed;
Name=B; Synonyms=D, E, F, G, H;
IsoId=P16378-2; Sequence=VSP_001830;
-!- TISSUE SPECIFICITY: Expressed primarily in neuronal cell bodies in
the brain, optic lobe, and thoracic and abdominal ganglia. Also
expressed in antenna, oocytes and ovarian nurse cells.
{ECO:0000269|PubMed:2509462, ECO:0000269|PubMed:2509463,
ECO:0000269|PubMed:2509464, ECO:0000269|PubMed:2519611}.
-!- DEVELOPMENTAL STAGE: Expressed in the surface glial cells of the
nerve cords at the larval stage (at protein level). Expressed
throughout development. {ECO:0000269|PubMed:10079238,
ECO:0000269|PubMed:2509463}.
-!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAN71523.1; Type=Erroneous termination; Positions=44; Note=Translated as Ser.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; M86660; AAA28577.1; -; mRNA.
EMBL; M29602; AAA28587.1; -; mRNA.
EMBL; M31203; AAA28586.1; -; Genomic_DNA.
EMBL; M29601; AAA28586.1; JOINED; Genomic_DNA.
EMBL; M31198; AAA28586.1; JOINED; Genomic_DNA.
EMBL; M31199; AAA28586.1; JOINED; Genomic_DNA.
EMBL; M31200; AAA28586.1; JOINED; Genomic_DNA.
EMBL; M31201; AAA28586.1; JOINED; Genomic_DNA.
EMBL; M31202; AAA28586.1; JOINED; Genomic_DNA.
EMBL; M30151; AAA28584.1; -; mRNA.
EMBL; M30152; AAA28585.1; -; mRNA.
EMBL; M31129; AAA28583.1; -; Genomic_DNA.
EMBL; M29731; AAA28580.1; -; mRNA.
EMBL; M29732; AAA28581.1; -; mRNA.
EMBL; AE013599; AAF58789.1; -; Genomic_DNA.
EMBL; AE013599; AAF58790.1; -; Genomic_DNA.
EMBL; AE013599; AAO41420.1; -; Genomic_DNA.
EMBL; AE013599; AAO41421.1; -; Genomic_DNA.
EMBL; AE013599; AAO41422.1; -; Genomic_DNA.
EMBL; AE013599; AAO41423.1; -; Genomic_DNA.
EMBL; AE013599; AAS64872.1; -; Genomic_DNA.
EMBL; AE013599; AAS64873.1; -; Genomic_DNA.
EMBL; AY121631; AAM51958.1; -; mRNA.
EMBL; BT001768; AAN71523.1; ALT_SEQ; mRNA.
EMBL; BT046134; ACK77603.1; -; mRNA.
PIR; A34304; RGFFO1.
PIR; B34304; RGFFO2.
RefSeq; NP_523684.2; NM_078960.5. [P16378-1]
RefSeq; NP_724934.1; NM_165772.4. [P16378-2]
RefSeq; NP_724935.1; NM_165773.3. [P16378-1]
RefSeq; NP_788304.1; NM_176124.3. [P16378-2]
RefSeq; NP_788305.1; NM_176125.3. [P16378-2]
RefSeq; NP_788306.1; NM_176126.3. [P16378-2]
RefSeq; NP_788307.1; NM_176127.3. [P16378-2]
RefSeq; NP_995801.1; NM_206079.2. [P16378-1]
RefSeq; NP_995802.1; NM_206080.2. [P16378-2]
UniGene; Dm.12982; -.
ProteinModelPortal; P16378; -.
SMR; P16378; -.
BioGrid; 61922; 29.
DIP; DIP-17224N; -.
IntAct; P16378; 6.
STRING; 7227.FBpp0087359; -.
PaxDb; P16378; -.
PRIDE; P16378; -.
EnsemblMetazoa; FBtr0088264; FBpp0087359; FBgn0001122. [P16378-2]
EnsemblMetazoa; FBtr0088265; FBpp0087360; FBgn0001122. [P16378-1]
EnsemblMetazoa; FBtr0088266; FBpp0087361; FBgn0001122. [P16378-1]
EnsemblMetazoa; FBtr0088267; FBpp0087362; FBgn0001122. [P16378-2]
EnsemblMetazoa; FBtr0088268; FBpp0087363; FBgn0001122. [P16378-2]
EnsemblMetazoa; FBtr0088269; FBpp0087364; FBgn0001122. [P16378-2]
EnsemblMetazoa; FBtr0088270; FBpp0087365; FBgn0001122. [P16378-2]
EnsemblMetazoa; FBtr0088271; FBpp0089315; FBgn0001122. [P16378-2]
EnsemblMetazoa; FBtr0088272; FBpp0089316; FBgn0001122. [P16378-1]
GeneID; 36104; -.
KEGG; dme:Dmel_CG2204; -.
CTD; 36104; -.
FlyBase; FBgn0001122; Galphao.
eggNOG; KOG0082; Eukaryota.
eggNOG; ENOG410XNVQ; LUCA.
GeneTree; ENSGT00760000118851; -.
InParanoid; P16378; -.
KO; K04534; -.
OMA; VARMEDT; -.
OrthoDB; EOG091G0VUT; -.
PhylomeDB; P16378; -.
Reactome; R-DME-112043; PLC beta mediated events.
Reactome; R-DME-202040; G-protein activation.
Reactome; R-DME-4086398; Ca2+ pathway.
ChiTaRS; G-oalpha47A; fly.
GenomeRNAi; 36104; -.
PRO; PR:P16378; -.
Proteomes; UP000000803; Chromosome 2R.
Bgee; FBgn0001122; -.
ExpressionAtlas; P16378; differential.
Genevisible; P16378; DM.
GO; GO:0005834; C:heterotrimeric G-protein complex; IDA:FlyBase.
GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
GO; GO:0001664; F:G-protein coupled receptor binding; IBA:GO_Central.
GO; GO:0005525; F:GTP binding; IDA:FlyBase.
GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004871; F:signal transducer activity; IBA:GO_Central.
GO; GO:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; IBA:GO_Central.
GO; GO:0008356; P:asymmetric cell division; IMP:FlyBase.
GO; GO:0032291; P:axon ensheathment in central nervous system; IMP:UniProtKB.
GO; GO:0042595; P:behavioral response to starvation; IMP:FlyBase.
GO; GO:0019722; P:calcium-mediated signaling; IMP:FlyBase.
GO; GO:0061343; P:cell adhesion involved in heart morphogenesis; IMP:FlyBase.
GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:UniProtKB.
GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; IMP:FlyBase.
GO; GO:0014045; P:establishment of endothelial blood-brain barrier; IMP:UniProtKB.
GO; GO:0060857; P:establishment of glial blood-brain barrier; IMP:FlyBase.
GO; GO:0001737; P:establishment of imaginal disc-derived wing hair orientation; IMP:FlyBase.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IMP:UniProtKB.
GO; GO:0007507; P:heart development; TAS:FlyBase.
GO; GO:0050774; P:negative regulation of dendrite morphogenesis; IMP:FlyBase.
GO; GO:0045886; P:negative regulation of synaptic growth at neuromuscular junction; IMP:FlyBase.
GO; GO:0050916; P:sensory perception of sweet taste; IMP:FlyBase.
GO; GO:0019991; P:septate junction assembly; IMP:FlyBase.
GO; GO:0007419; P:ventral cord development; IMP:FlyBase.
GO; GO:0016055; P:Wnt signaling pathway; IMP:FlyBase.
CDD; cd00066; G-alpha; 1.
Gene3D; 1.10.400.10; -; 1.
InterPro; IPR001408; Gprotein_alpha_I.
InterPro; IPR001019; Gprotein_alpha_su.
InterPro; IPR011025; GproteinA_insert.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR10218; PTHR10218; 1.
Pfam; PF00503; G-alpha; 1.
PRINTS; PR00318; GPROTEINA.
PRINTS; PR00441; GPROTEINAI.
SMART; SM00275; G_alpha; 1.
SUPFAM; SSF47895; SSF47895; 1.
SUPFAM; SSF52540; SSF52540; 2.
1: Evidence at protein level;
Alternative splicing; Complete proteome; GTP-binding; Lipoprotein;
Magnesium; Metal-binding; Myristate; Nucleotide-binding; Palmitate;
Reference proteome; Transducer.
INIT_MET 1 1 Removed. {ECO:0000250}.
CHAIN 2 354 G protein alpha o subunit.
/FTId=PRO_0000203716.
NP_BIND 40 47 GTP. {ECO:0000250}.
NP_BIND 176 182 GTP. {ECO:0000250}.
NP_BIND 201 205 GTP. {ECO:0000250}.
NP_BIND 270 273 GTP. {ECO:0000250}.
METAL 47 47 Magnesium. {ECO:0000250}.
METAL 182 182 Magnesium. {ECO:0000250}.
BINDING 326 326 GTP; via amide nitrogen. {ECO:0000250}.
LIPID 2 2 N-myristoyl glycine. {ECO:0000255}.
LIPID 3 3 S-palmitoyl cysteine. {ECO:0000255}.
VAR_SEQ 4 21 AQSAEERAAAARSRLIER -> TTSAEERAAIQRSKQIEK
(in isoform B).
{ECO:0000303|PubMed:2509462,
ECO:0000303|PubMed:2509463,
ECO:0000303|PubMed:2509464,
ECO:0000303|PubMed:2519611}.
/FTId=VSP_001830.
CONFLICT 88 88 M -> I (in Ref. 3; AAA28585).
{ECO:0000305}.
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


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