GNAQ_DROME
ID GNAQ_DROME Reviewed; 353 AA.
AC P23625; A4UZE6; P54400; Q29QX1; Q540Y7; Q9I7C8; Q9V6E2;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=G protein alpha q subunit;
DE AltName: Full=Guanine nucleotide-binding protein G(q) subunit alpha;
DE AltName: Full=Guanine nucleotide-binding protein alpha-q;
DE AltName: Full=dGQalpha;
GN Name=Galphaq;
GN Synonyms=dgq {ECO:0000312|FlyBase:FBgn0004435},
GN dGqalpha {ECO:0000312|FlyBase:FBgn0004435},
GN Galpha {ECO:0000312|FlyBase:FBgn0004435},
GN Galpha49b {ECO:0000312|FlyBase:FBgn0004435},
GN Gq {ECO:0000312|FlyBase:FBgn0004435},
GN Gqalpha {ECO:0000312|FlyBase:FBgn0004435};
GN ORFNames=CG17759 {ECO:0000312|FlyBase:FBgn0004435};
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], ALTERNATIVE SPLICING (ISOFORMS A AND D),
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=2125225; DOI=10.1016/0896-6273(90)90349-k;
RA Lee Y.-J., Dobbs M.B., Verardi M.L., Hyde D.R.;
RT "Dgq: a Drosophila gene encoding a visual system-specific G alpha
RT molecule.";
RL Neuron 5:889-898(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Oregon-R;
RX PubMed=8524786; DOI=10.1073/pnas.92.25.11475;
RA Talluri S., Bhatt A., Smith D.P.;
RT "Identification of a Drosophila G protein alpha subunit (dGq alpha-3)
RT expressed in chemosensory cells and central neurons.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:11475-11479(1995).
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 A).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
RC STRAIN=Berkeley;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems. Could be the transducin analog, an amplifier and one of the
CC transducers of a visual impulse that performs the coupling between
CC opsin and cGMP-phosphodiesterase. Could mediate a subset of olfactory
CC and gustatory responses. {ECO:0000269|PubMed:2125225,
CC ECO:0000269|PubMed:8524786}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=D {ECO:0000312|FlyBase:FBgn0004435};
CC IsoId=P23625-1; Sequence=Displayed;
CC Name=A {ECO:0000312|FlyBase:FBgn0004435}; Synonyms=C
CC {ECO:0000312|FlyBase:FBgn0004435}, E {ECO:0000312|FlyBase:FBgn0004435},
CC G {ECO:0000312|FlyBase:FBgn0004435};
CC IsoId=P23625-2; Sequence=VSP_001835, VSP_001836;
CC -!- TISSUE SPECIFICITY: Isoform D is expressed only in the retina and
CC ocellus of the adult head. Isoform A is expressed in chemosensory cells
CC of the olfactory and taste structures, including a subset of olfactory
CC and gustatory neurons, and in cells of the central nervous system,
CC including neurons in the lamina ganglionaris.
CC {ECO:0000269|PubMed:2125225, ECO:0000269|PubMed:8524786}.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(q) subfamily.
CC {ECO:0000305}.
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DR EMBL; M58016; AAA28460.1; -; Genomic_DNA.
DR EMBL; U31092; AAC46943.1; -; mRNA.
DR EMBL; AE013599; AAF58485.2; -; Genomic_DNA.
DR EMBL; AE013599; AAM68627.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68628.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68629.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68631.1; -; Genomic_DNA.
DR EMBL; AY118511; AAM49880.1; -; mRNA.
DR EMBL; BT024269; ABC86331.1; -; mRNA.
DR PIR; JN0115; JN0115.
DR RefSeq; NP_725191.1; NM_165919.2. [P23625-2]
DR RefSeq; NP_725193.1; NM_165921.2. [P23625-2]
DR RefSeq; NP_725194.1; NM_165922.2. [P23625-2]
DR RefSeq; NP_725195.1; NM_165923.2. [P23625-2]
DR RefSeq; NP_725196.1; NM_165924.2. [P23625-1]
DR RefSeq; NP_725197.2; NM_165925.3. [P23625-2]
DR AlphaFoldDB; P23625; -.
DR SMR; P23625; -.
DR BioGRID; 62158; 20.
DR IntAct; P23625; 6.
DR SwissPalm; P23625; -.
DR PRIDE; P23625; -.
DR DNASU; 36384; -.
DR EnsemblMetazoa; FBtr0087829; FBpp0086942; FBgn0004435. [P23625-2]
DR EnsemblMetazoa; FBtr0087830; FBpp0086943; FBgn0004435. [P23625-2]
DR EnsemblMetazoa; FBtr0087831; FBpp0086944; FBgn0004435. [P23625-2]
DR EnsemblMetazoa; FBtr0087832; FBpp0086945; FBgn0004435. [P23625-1]
DR EnsemblMetazoa; FBtr0087833; FBpp0086946; FBgn0004435. [P23625-2]
DR EnsemblMetazoa; FBtr0304955; FBpp0293494; FBgn0004435. [P23625-2]
DR GeneID; 36384; -.
DR KEGG; dme:Dmel_CG17759; -.
DR UCSC; CG17759-RC; d. melanogaster.
DR CTD; 36384; -.
DR FlyBase; FBgn0004435; Galphaq.
DR VEuPathDB; VectorBase:FBgn0004435; -.
DR GeneTree; ENSGT00940000162569; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; P23625; -.
DR PhylomeDB; P23625; -.
DR Reactome; R-DME-112043; PLC beta mediated events.
DR Reactome; R-DME-202040; G-protein activation.
DR Reactome; R-DME-416476; G alpha (q) signalling events.
DR Reactome; R-DME-418592; ADP signalling through P2Y purinoceptor 1.
DR Reactome; R-DME-428930; Thromboxane signalling through TP receptor.
DR Reactome; R-DME-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR SignaLink; P23625; -.
DR BioGRID-ORCS; 36384; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 36384; -.
DR PRO; PR:P23625; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0004435; Expressed in head capsule and 33 other tissues.
DR Genevisible; P23625; DM.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; ISS:FlyBase.
DR GO; GO:0016027; C:inaD signaling complex; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; HDA:FlyBase.
DR GO; GO:0016028; C:rhabdomere; 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; IMP:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007202; P:activation of phospholipase C activity; IGI:FlyBase.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0016199; P:axon midline choice point recognition; IMP:FlyBase.
DR GO; GO:0071244; P:cellular response to carbon dioxide; IMP:FlyBase.
DR GO; GO:0007629; P:flight behavior; IGI:FlyBase.
DR GO; GO:0016060; P:metarhodopsin inactivation; IMP:FlyBase.
DR GO; GO:0002385; P:mucosal immune response; IMP:FlyBase.
DR GO; GO:0046673; P:negative regulation of compound eye retinal cell programmed cell death; IMP:FlyBase.
DR GO; GO:0070050; P:neuron cellular homeostasis; IGI:FlyBase.
DR GO; GO:0060158; P:phospholipase C-activating dopamine receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007602; P:phototransduction; IDA:FlyBase.
DR GO; GO:1900073; P:regulation of neuromuscular synaptic transmission; IGI:FlyBase.
DR GO; GO:0016056; P:rhodopsin mediated signaling pathway; IMP:FlyBase.
DR GO; GO:0007608; P:sensory perception of smell; IMP:FlyBase.
DR GO; GO:0030322; P:stabilization of membrane potential; IGI:FlyBase.
DR GO; GO:0043052; P:thermotaxis; IDA:FlyBase.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd00066; G-alpha; 1.
DR Gene3D; 1.10.400.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR000654; Gprotein_alpha_Q.
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; PR00442; GPROTEINAQ.
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; Sensory transduction;
KW Transducer; Vision.
FT CHAIN 1..353
FT /note="G protein alpha q subunit"
FT /id="PRO_0000203769"
FT DOMAIN 32..353
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 172..180
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 195..204
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 264..271
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 323..328
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 174..180
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 199..203
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 268..271
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 325
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 156..194
FT /note="SDLARIEQADYLPTEQDILRARVPTTGILEYPFDLDGIV -> KDLDRVAQP
FT AYLPTEQDILRVRVPTTGIIEYPFDLEEIR (in isoform A)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:8524786"
FT /id="VSP_001835"
FT VAR_SEQ 293..353
FT /note="KQDHAAAKQFVLKKYLACNPDPERQCYSHFTTATDTENIKLVFCAVKDTIMQ
FT NALKEFNLG -> QRDAITAREFILRMFVDLNPDSEKIIYSHFTCATDTENIRFVFAAV
FT KDTILQSNLKEYNLV (in isoform A)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:8524786"
FT /id="VSP_001836"
SQ SEQUENCE 353 AA; 41295 MW; A742A7C9CB23FD19 CRC64;
MECCLSEEAK EQKRINQEIE KQLRRDKRDA RRELKLLLLG TGESGKSTFI KQMRIIHGSG
YSDEDKRGYI KLVFQNIFMA MQSMIKAMDM LKISYGQGEH SELADLVMSI DYETVTTFED
PYLNAIKTLW DDAGIQECYD RRREYQLTDS AKYYLSDLAR IEQADYLPTE QDILRARVPT
TGILEYPFDL DGIVFRMVDV GGQRSERRKW IHCFENVTSI IFLVALSEYD QILFESDNEN
RMEESKALFR TIITYPWFQN SSVILFLNKK DLLEEKIMYS HLVDYFPEYD GPKQDHAAAK
QFVLKKYLAC NPDPERQCYS HFTTATDTEN IKLVFCAVKD TIMQNALKEF NLG
