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 23-FEB-2022, entry version 178. 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: Cell junction, synapse, postsynaptic cell CC membrane; Multi-pass membrane protein. Cell membrane; Multi-pass CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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; CLACCAQ; -. 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 central nervous system and 21 other tissues. DR Genevisible; Q08832; DM. 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: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: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 junction; Cell membrane; Chloride; Chloride channel; Disulfide bond; KW Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel; KW Membrane; Postsynaptic cell membrane; Receptor; Reference proteome; Signal; KW Synapse; 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 //