GNAI_DROME
ID GNAI_DROME Reviewed; 355 AA.
AC P20353; Q9VS04;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=G protein alpha i subunit;
DE AltName: Full=Guanine nucleotide-binding protein G(i) subunit alpha 65A;
GN Name=Galphai; Synonyms=G-ialpha65A, G-OA65C; ORFNames=CG10060;
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 [GENOMIC DNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S;
RX PubMed=3136172; DOI=10.1016/s0021-9258(18)37894-3;
RA Provost N.M., Somers D.E., Hurley J.B.;
RT "A Drosophila melanogaster G protein alpha subunit gene is expressed
RT primarily in embryos and pupae.";
RL J. Biol. Chem. 263:12070-12076(1988).
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 FUNCTION, INTERACTION WITH LOCO, 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).
RN [6]
RP FUNCTION, INTERACTION WITH LOCO AND RAPS/PINS, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF GLN-205.
RX PubMed=15937221; DOI=10.1101/gad.1295505;
RA Yu F., Wang H., Qian H., Kaushik R., Bownes M., Yang X., Chia W.;
RT "Locomotion defects, together with Pins, regulates heterotrimeric G-protein
RT signaling during Drosophila neuroblast asymmetric divisions.";
RL Genes Dev. 19:1341-1353(2005).
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, Galphao 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, ECO:0000269|PubMed:15937221}.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site. Interacts
CC (via GDP- or GTP-bound forms) with loco (via GoLoco and RGS domains).
CC Interacts with raps/pins. {ECO:0000269|PubMed:10079238,
CC ECO:0000269|PubMed:15937221}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15937221}.
CC Apical cell membrane {ECO:0000269|PubMed:15937221}. Note=Colocalizes
CC with loco and raps/pins at the apical cortex throughout mitosis in
CC neuroblasts.
CC -!- DEVELOPMENTAL STAGE: Expressed in the surface glial cells of the nerve
CC cords at the larval stage (at protein level). Expressed primarily in
CC embryos and pupae. {ECO:0000269|PubMed:10079238,
CC ECO:0000269|PubMed:3136172}.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
CC {ECO:0000305}.
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DR EMBL; M23093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M23094; AAA28565.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF50626.1; -; Genomic_DNA.
DR EMBL; AY051670; AAK93094.1; -; mRNA.
DR PIR; A31076; RGFFA.
DR RefSeq; NP_477502.1; NM_058154.5.
DR AlphaFoldDB; P20353; -.
DR SMR; P20353; -.
DR BioGRID; 64214; 11.
DR DIP; DIP-17262N; -.
DR IntAct; P20353; 3.
DR STRING; 7227.FBpp0076643; -.
DR SwissPalm; P20353; -.
DR PaxDb; P20353; -.
DR PRIDE; P20353; -.
DR EnsemblMetazoa; FBtr0076934; FBpp0076643; FBgn0001104.
DR GeneID; 38765; -.
DR KEGG; dme:Dmel_CG10060; -.
DR CTD; 38765; -.
DR FlyBase; FBgn0001104; Galphai.
DR VEuPathDB; VectorBase:FBgn0001104; -.
DR eggNOG; KOG0082; Eukaryota.
DR GeneTree; ENSGT00940000165593; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; P20353; -.
DR OMA; GMGCTVS; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; P20353; -.
DR Reactome; R-DME-170670; Adenylate cyclase inhibitory pathway.
DR Reactome; R-DME-2485179; Activation of the phototransduction cascade.
DR Reactome; R-DME-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Reactome; R-DME-392170; ADP signalling through P2Y purinoceptor 12.
DR Reactome; R-DME-400042; Adrenaline,noradrenaline inhibits insulin secretion.
DR Reactome; R-DME-4086398; Ca2+ pathway.
DR Reactome; R-DME-418594; G alpha (i) signalling events.
DR Reactome; R-DME-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-DME-9717207; Sensory perception of sweet, bitter, and umami (glutamate) taste.
DR SignaLink; P20353; -.
DR BioGRID-ORCS; 38765; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Galphai; fly.
DR GenomeRNAi; 38765; -.
DR PRO; PR:P20353; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0001104; Expressed in embryonic/larval hemocyte (Drosophila) and 31 other tissues.
DR Genevisible; P20353; DM.
DR GO; GO:0045179; C:apical cortex; IDA:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005938; C:cell cortex; TAS:FlyBase.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IDA: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; 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: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:0055059; P:asymmetric neuroblast division; IMP:FlyBase.
DR GO; GO:0045167; P:asymmetric protein localization involved in cell fate determination; IMP:FlyBase.
DR GO; GO:0032291; P:axon ensheathment in central nervous system; IMP:UniProtKB.
DR GO; GO:0019722; P:calcium-mediated signaling; 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:0051294; P:establishment of spindle orientation; IMP:FlyBase.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; 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 Cell membrane; Differentiation; GTP-binding; Lipoprotein; Magnesium;
KW Membrane; Metal-binding; Myristate; Nucleotide-binding; Palmitate;
KW Reference proteome; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..355
FT /note="G protein alpha i subunit"
FT /id="PRO_0000203689"
FT DOMAIN 33..355
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 36..49
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 325..330
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 41..48
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 48
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 327
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 MUTAGEN 205
FT /note="Q->L: Inhibits interaction with loco. Does not
FT inhibit apical cell membrane localization in neuroblasts."
FT /evidence="ECO:0000269|PubMed:15937221"
FT CONFLICT 140
FT /note="S -> T (in Ref. 1; AAA28565)"
FT /evidence="ECO:0000305"
SQ 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
