GBRB3_DROME
ID GBRB3_DROME Reviewed; 496 AA.
AC Q08832; A4V4J6; Q9TX49; Q9VXL8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Gamma-aminobutyric acid receptor subunit beta-like;
DE AltName: Full=GABA(A) receptor;
DE Flags: Precursor;
GN Name=Lcch3; ORFNames=CG17336;
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=Canton-S; TISSUE=Pupae;
RX PubMed=7685594; DOI=10.1006/bbrc.1993.1648;
RA Henderson J.E., Soderlund D.M., Knipple D.C.;
RT "Characterization of a putative gamma-aminobutyric acid (GABA) receptor
RT beta subunit gene from Drosophila melanogaster.";
RL Biochem. Biophys. Res. Commun. 193:474-482(1993).
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=Head;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 284-340.
RC STRAIN=Canton-S;
RX PubMed=8025558; DOI=10.1016/0965-1748(94)90029-9;
RA Henderson J.E., Knipple D.C., Soderlund D.M.;
RT "PCR-based homology probing reveals a family of GABA receptor-like genes in
RT Drosophila melanogaster.";
RL Insect Biochem. Mol. Biol. 24:363-371(1994).
RN [6]
RP FUNCTION, AND INTERACTION WITH GRD.
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. Combines with the ligand-gated ion channel subunit
CC GRD to form cation-selective GABA-gated ion channels when coexpressed
CC in Xenopus laevis oocytes. {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 Grd (alpha
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; L17436; AAA28559.1; -; mRNA.
DR EMBL; S62717; AAB27090.1; -; mRNA.
DR EMBL; AE014298; AAS65370.1; -; Genomic_DNA.
DR EMBL; AY060660; AAL28208.1; -; mRNA.
DR PIR; JN0603; JN0603.
DR RefSeq; NP_996469.1; NM_206746.2.
DR AlphaFoldDB; Q08832; -.
DR SMR; Q08832; -.
DR STRING; 7227.FBpp0089263; -.
DR TCDB; 1.A.9.5.6; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
DR GlyGen; Q08832; 2 sites.
DR PaxDb; Q08832; -.
DR PRIDE; Q08832; -.
DR DNASU; 32554; -.
DR EnsemblMetazoa; FBtr0074129; FBpp0089263; FBgn0010240.
DR GeneID; 32554; -.
DR KEGG; dme:Dmel_CG17336; -.
DR CTD; 32554; -.
DR FlyBase; FBgn0010240; Lcch3.
DR VEuPathDB; VectorBase:FBgn0010240; -.
DR eggNOG; KOG3643; Eukaryota.
DR GeneTree; ENSGT00940000166778; -.
DR HOGENOM; CLU_010920_0_0_1; -.
DR InParanoid; Q08832; -.
DR OMA; VYWIFYF; -.
DR OrthoDB; 480926at2759; -.
DR PhylomeDB; Q08832; -.
DR Reactome; R-DME-977443; GABA receptor activation.
DR BioGRID-ORCS; 32554; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Lcch3; fly.
DR GenomeRNAi; 32554; -.
DR PRO; PR:Q08832; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0010240; Expressed in brain and 10 other tissues.
DR ExpressionAtlas; Q08832; baseline and differential.
DR Genevisible; Q08832; 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:1902711; C:GABA-A receptor complex; IBA:GO_Central.
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; IDA:FlyBase.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0004890; F:GABA-A receptor activity; IEA:InterPro.
DR GO; GO:0022851; F:GABA-gated chloride ion channel activity; IDA:FlyBase.
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:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 1.20.58.390; -; 1.
DR Gene3D; 2.70.170.10; -; 1.
DR InterPro; IPR006028; GABAA/Glycine_rcpt.
DR InterPro; IPR002289; GABAAb_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; PR01160; GABAARBETA.
DR PRINTS; PR00253; GABAARECEPTR.
DR PRINTS; PR00252; NRIONCHANNEL.
DR SUPFAM; SSF63712; SSF63712; 1.
DR SUPFAM; SSF90112; SSF90112; 1.
DR TIGRFAMs; TIGR00860; LIC; 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..20
FT /note="Or 27"
FT /evidence="ECO:0000255"
FT CHAIN 21..496
FT /note="Gamma-aminobutyric acid receptor subunit beta-like"
FT /id="PRO_0000000454"
FT TOPO_DOM 21..258
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..472
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..494
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 176..190
FT /evidence="ECO:0000250"
FT CONFLICT 12
FT /note="G -> S (in Ref. 1; AAA28559/AAB27090)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="V -> C (in Ref. 5; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 496 AA; 56597 MW; 62C9A9E97E8DF681 CRC64;
MTCFTRVGVS CGLFFFLLGA QLQLIRCIRK DVLAGRLENV TQTISNILQG YDIRLRPNFG
GEPLHVGMDL TIASFDAISE VNMDYTITMY LNQYWRDERL AFNIFGQYFD DENDDGISDV
LTLSGDFAEK IWVPDTFFAN DKNSFLHDVT ERNKLVRLGG DGAVTYGMRF TTTLACMMDL
HYYPLDSQNC TVEIESYGYT VSDVVMYWKP TPVRGVEDAE LPQFTIIGYE TNDRKERLAT
GVYQRLSLSF KLQRNIGYFV FQTYLPSILI VMLSWVSFWI NHEATSARVA LGITTVLTMT
TISTGVRSSL PRISYVKAID IYLVMCFVFV FAALLEYAAV NYTYWGKRAK KKIKKVKECC
PGKIGKSERS ETCSTTEDII ELQDVRMSPI PSLRRGTYNA TLDSIGTETM NLGKFPPSFR
ITRNYGTGHS QLRRRAQRGI STRPRMLHAL KRGASAIKAT IPKIKDVNII DKYSRMIFPI
SFLAFNLGYW LFYILE
