GBRAL_DROME
ID GBRAL_DROME Reviewed; 686 AA.
AC Q24352; Q9TX50; Q9VVL3;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Gamma-aminobutyric acid receptor alpha-like;
DE AltName: Full=GABA(A) receptor alpha-like and glycine receptor-like subunit of Drosophila;
DE Short=GRD;
DE Flags: Precursor;
GN Name=Grd; ORFNames=CG7446;
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].
RC STRAIN=Berlin; TISSUE=Head, and Salivary gland;
RX PubMed=8189252; DOI=10.1046/j.1471-4159.1994.62062480.x;
RA Harvey R.J., Schmitt B., Hermans-Borgmeyer I., Gundelfinger E.D., Betz H.,
RA Darlison M.G.;
RT "Sequence of a Drosophila ligand-gated ion-channel polypeptide with an
RT unusual amino-terminal extracellular domain.";
RL J. Neurochem. 62:2480-2483(1994).
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 FUNCTION, AND INTERACTION WITH LCCH3.
RX PubMed=15148245; DOI=10.1038/sj.bjp.0705818;
RA Gisselmann G., Plonka J., Pusch H., Hatt H.;
RT "Drosophila melanogaster GRD and LCCH3 subunits form heteromultimeric GABA-
RT gated cation channels.";
RL Br. J. Pharmacol. 142:409-413(2004).
CC -!- FUNCTION: GABA, an inhibitory neurotransmitter, mediates neuronal
CC inhibition by binding to the GABA receptor and opening an integral
CC chloride channel. May combine with the ligand-gated ion channel subunit
CC Lcch3 to form cation-selective GABA-gated ion channels.
CC {ECO:0000269|PubMed:15148245}.
CC -!- SUBUNIT: Generally pentameric. There are five types of GABA(A) receptor
CC chains: alpha, beta, gamma, delta, and rho. Interacts with Lcch3 (beta
CC chain). {ECO:0000269|PubMed:15148245}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC protein. Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily. {ECO:0000305}.
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DR EMBL; X78349; CAA55144.1; -; mRNA.
DR EMBL; AE014296; AAF49298.2; -; Genomic_DNA.
DR PIR; S60749; S60749.
DR RefSeq; NP_524131.1; NM_079407.3.
DR AlphaFoldDB; Q24352; -.
DR SMR; Q24352; -.
DR STRING; 7227.FBpp0074905; -.
DR TCDB; 1.A.9.5.6; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
DR GlyGen; Q24352; 2 sites.
DR PaxDb; Q24352; -.
DR PRIDE; Q24352; -.
DR DNASU; 39984; -.
DR EnsemblMetazoa; FBtr0075139; FBpp0074905; FBgn0001134.
DR GeneID; 39984; -.
DR KEGG; dme:Dmel_CG7446; -.
DR CTD; 39984; -.
DR FlyBase; FBgn0001134; Grd.
DR VEuPathDB; VectorBase:FBgn0001134; -.
DR eggNOG; KOG3642; Eukaryota.
DR GeneTree; ENSGT00940000171178; -.
DR HOGENOM; CLU_010920_2_2_1; -.
DR InParanoid; Q24352; -.
DR OMA; YYRREEM; -.
DR OrthoDB; 1057372at2759; -.
DR PhylomeDB; Q24352; -.
DR Reactome; R-DME-977443; GABA receptor activation.
DR BioGRID-ORCS; 39984; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 39984; -.
DR PRO; PR:Q24352; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0001134; Expressed in brain and 2 other tissues.
DR ExpressionAtlas; Q24352; baseline and differential.
DR Genevisible; Q24352; DM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; TAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:FlyBase.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0005261; F:cation channel activity; IDA:UniProtKB.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0016933; F:extracellularly glycine-gated ion channel activity; ISS:FlyBase.
DR GO; GO:0004890; F:GABA-A receptor activity; IDA:UniProtKB.
DR GO; GO:0022851; F:GABA-gated chloride ion channel activity; IDA:FlyBase.
DR GO; GO:0022852; F:glycine-gated chloride ion channel activity; TAS:FlyBase.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IDA:UniProtKB.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006811; P:ion transport; IDA:UniProtKB.
DR GO; GO:1904456; P:negative regulation of neuronal action potential; IMP:FlyBase.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:FlyBase.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0060012; P:synaptic transmission, glycinergic; IGI:FlyBase.
DR Gene3D; 1.20.58.390; -; 2.
DR Gene3D; 2.70.170.10; -; 1.
DR InterPro; IPR006028; GABAA/Glycine_rcpt.
DR InterPro; IPR006202; Neur_chan_lig-bd.
DR InterPro; IPR036734; Neur_chan_lig-bd_sf.
DR InterPro; IPR006201; Neur_channel.
DR InterPro; IPR036719; Neuro-gated_channel_TM_sf.
DR InterPro; IPR038050; Neuro_actylchol_rec.
DR InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR PANTHER; PTHR18945; PTHR18945; 1.
DR Pfam; PF02931; Neur_chan_LBD; 1.
DR Pfam; PF02932; Neur_chan_memb; 1.
DR PRINTS; PR00253; GABAARECEPTR.
DR PRINTS; PR00252; NRIONCHANNEL.
DR SUPFAM; SSF63712; SSF63712; 1.
DR SUPFAM; SSF90112; SSF90112; 1.
DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Chloride; Chloride channel; Disulfide bond; Glycoprotein;
KW Ion channel; Ion transport; Ligand-gated ion channel; Membrane;
KW Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..58
FT /evidence="ECO:0000255"
FT CHAIN 59..686
FT /note="Gamma-aminobutyric acid receptor alpha-like"
FT /id="PRO_0000000451"
FT TOPO_DOM 97..393
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..414
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..441
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 456..476
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 477..650
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 651..671
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 570..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..637
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 233..247
FT /evidence="ECO:0000250"
SQ SEQUENCE 686 AA; 76558 MW; E2BD771B7E3BAC7A CRC64;
MCTMPATRDA SGSGDASTDL IAARSLSSHQ GQRSNLRIFK LLISCCLLML CIYPNAWPWS
IGPGSGPFSV SADSIKGRGD THRLGEMGTS LSSSLPSSWL TQSNNHANIS ELLDNLLRGY
DNSIRPDFGG PPATIEVDIM VRSMGPISEV DMTYSMDCYF RQSWVDKRLA FEGAQDTLAL
SVSMLARIWK PDTYFYNGKQ SYLHTITTPN KFVRIYQNGR VLYSSRLTIK AGCPMNLADF
PMDIQKCPLK FGSFGYTTSD VIYRWNKERP PVAIAEDMKL SQFDLVDCPA GNLTDIVYKA
AAPRPQRRPF NNKDPPRPTS KVMTTFAGPA AKNQHVRGTG LKLDKGAFGT GRDATGGSGS
TTGLSGTITL ETNHPSEYSM LMVNFHLQRH MGNFLIQVYG PCCLLVVLSW VSFWLNREAT
ADRVSLGITT VLTMTFLGLE ARTDLPKVSY PTALDFFVFL SFGFIFATIL QFAVVHYYTK
YGSGECYFII EELDSESGES ETEPLTSDFR GSTESKIYEV IPLSMCAISM PPPPTRLGML
TSRNRRPRNR RHGLWSMKLL GLFDWRRRRK PPRADSDEDE DDEQTQLRAN EAPTTSAAAA
AAQAAAQAAR ISPPTGGRRR MSYYRREEME ARRKGKRTPQ YNSVSKIDRA SRIVFPLLFI
LINVFYWYGY LSRSSRILAN TPDAST
