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G protein alpha i subunit (Guanine nucleotide-binding protein G(i) subunit alpha 65A)

 GNAI_DROME              Reviewed;         355 AA.
P20353; Q9VS04;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 2.
25-OCT-2017, entry version 171.
RecName: Full=G protein alpha i subunit;
AltName: Full=Guanine nucleotide-binding protein G(i) subunit alpha 65A;
Name=Galphai; Synonyms=G-ialpha65A, G-OA65C; ORFNames=CG10060;
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 [GENOMIC DNA], AND DEVELOPMENTAL STAGE.
STRAIN=Canton-S;
PubMed=3136172;
Provost N.M., Somers D.E., Hurley J.B.;
"A Drosophila melanogaster G protein alpha subunit gene is expressed
primarily in embryos and pupae.";
J. Biol. Chem. 263:12070-12076(1988).
[2]
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).
[3]
GENOME REANNOTATION.
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
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).
[5]
FUNCTION, INTERACTION WITH LOCO, 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).
[6]
FUNCTION, INTERACTION WITH LOCO AND RAPS/PINS, SUBCELLULAR LOCATION,
AND MUTAGENESIS OF GLN-205.
PubMed=15937221; DOI=10.1101/gad.1295505;
Yu F., Wang H., Qian H., Kaushik R., Bownes M., Yang X., Chia W.;
"Locomotion defects, together with Pins, regulates heterotrimeric G-
protein signaling during Drosophila neuroblast asymmetric divisions.";
Genes Dev. 19:1341-1353(2005).
-!- 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, Galphao 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, ECO:0000269|PubMed:15937221}.
-!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and
gamma. The alpha chain contains the guanine nucleotide binding
site. Interacts (via GDP- or GTP-bound forms) with loco (via
GoLoco and RGS domains). Interacts with raps/pins.
{ECO:0000269|PubMed:10079238, ECO:0000269|PubMed:15937221}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15937221}.
Apical cell membrane {ECO:0000269|PubMed:15937221}.
Note=Colocalizes with loco and raps/pins at the apical cortex
throughout mitosis in neuroblasts.
-!- DEVELOPMENTAL STAGE: Expressed in the surface glial cells of the
nerve cords at the larval stage (at protein level). Expressed
primarily in embryos and pupae. {ECO:0000269|PubMed:10079238,
ECO:0000269|PubMed:3136172}.
-!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
{ECO:0000305}.
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EMBL; M23093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M23094; AAA28565.1; -; Genomic_DNA.
EMBL; AE014296; AAF50626.1; -; Genomic_DNA.
EMBL; AY051670; AAK93094.1; -; mRNA.
PIR; A31076; RGFFA.
RefSeq; NP_477502.1; NM_058154.5.
UniGene; Dm.33467; -.
ProteinModelPortal; P20353; -.
SMR; P20353; -.
BioGrid; 64214; 10.
DIP; DIP-17262N; -.
IntAct; P20353; 3.
MINT; MINT-771407; -.
STRING; 7227.FBpp0076643; -.
PaxDb; P20353; -.
PRIDE; P20353; -.
EnsemblMetazoa; FBtr0076934; FBpp0076643; FBgn0001104.
GeneID; 38765; -.
KEGG; dme:Dmel_CG10060; -.
CTD; 38765; -.
FlyBase; FBgn0001104; Galphai.
eggNOG; KOG0082; Eukaryota.
eggNOG; ENOG410XNVQ; LUCA.
GeneTree; ENSGT00760000118851; -.
InParanoid; P20353; -.
KO; K04630; -.
OMA; YSGANKY; -.
OrthoDB; EOG091G0VUT; -.
PhylomeDB; P20353; -.
Reactome; R-DME-112043; PLC beta mediated events.
Reactome; R-DME-202040; G-protein activation.
Reactome; R-DME-418597; G alpha (z) signalling events.
ChiTaRS; G-ialpha65A; fly.
GenomeRNAi; 38765; -.
PRO; PR:P20353; -.
Proteomes; UP000000803; Chromosome 3L.
Bgee; FBgn0001104; -.
Genevisible; P20353; DM.
GO; GO:0045179; C:apical cortex; IDA:UniProtKB.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005938; C:cell cortex; TAS:FlyBase.
GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
GO; GO:0003677; F:DNA binding; 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; IEA:UniProtKB-KW.
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:0055059; P:asymmetric neuroblast division; IMP:FlyBase.
GO; GO:0045167; P:asymmetric protein localization involved in cell fate determination; IMP:FlyBase.
GO; GO:0032291; P:axon ensheathment in central nervous system; IMP:UniProtKB.
GO; GO:0019722; P:calcium-mediated signaling; IMP:FlyBase.
GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:UniProtKB.
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:0051294; P:establishment of spindle orientation; IMP:FlyBase.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IMP:UniProtKB.
GO; GO:0032880; P:regulation of protein localization; IMP:FlyBase.
GO; GO:0019991; P:septate junction assembly; IMP:FlyBase.
GO; GO:0007419; P:ventral cord development; 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;
Cell membrane; Complete proteome; Differentiation; GTP-binding;
Lipoprotein; Magnesium; Membrane; Metal-binding; Myristate;
Nucleotide-binding; Palmitate; Reference proteome; Transducer.
INIT_MET 1 1 Removed. {ECO:0000250}.
CHAIN 2 355 G protein alpha i subunit.
/FTId=PRO_0000203689.
NP_BIND 41 48 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 48 48 Magnesium. {ECO:0000250}.
METAL 182 182 Magnesium. {ECO:0000250}.
BINDING 327 327 GTP; via amide nitrogen. {ECO:0000250}.
LIPID 2 2 N-myristoyl glycine. {ECO:0000255}.
LIPID 3 3 S-palmitoyl cysteine. {ECO:0000255}.
MUTAGEN 205 205 Q->L: Inhibits interaction with loco.
Does not inhibit apical cell membrane
localization in neuroblasts.
{ECO:0000269|PubMed:15937221}.
CONFLICT 140 140 S -> T (in Ref. 1; AAA28565).
{ECO:0000305}.
SEQUENCE 355 AA; 40596 MW; 69DF15754EB22F9D CRC64;
MGCAVSTARD KEAIERSKNI DRALRAEGER AASEVKLLLL GAGESGKSTI VKQMKIIHDT
GYSQEECEEY RRVVFSNTVQ SLMVIIRAMG RLKIEFADPS RTDIARQFFT HASAADEGIL
LPEIVLLMKK LWADGGVQQS FARSREYQLN DSAGYYLNSL DRIAQPNYIP TQQDVLRTRV
KTTGIIETHF SCKQLHFKLF DVGGQRSERK KWIHCFEGVT AIIFCVALSG YDLVLAEDEE
MNRMIESLKL FDSICNSKWF VETSIILFLN KKDLFEEKIK RSPLTICFPE YTGTNTFEEA
ANYIRMKFEN LNKRKDQKEI YTHLTCATDT NNVKFVFDAV TDVIIKNNLK QIGLF


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