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 16-JUN-2009, entry version 85. 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; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Canton-S; TISSUE=Pupae; RX MEDLINE=93290631; 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) RT receptor 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 MEDLINE=20196006; 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., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA 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., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA 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., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., RA Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; 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., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., 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 MEDLINE=94297578; 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 RT genes in 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 RT GABA-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 CC subunit GRD to form cation-selective GABA-gated ion channels when CC coexpressed in Xenopus laevis oocytes. CC -!- SUBUNIT: Generally pentameric. There are five types of GABA(A) CC receptor chains: alpha, beta, gamma, delta, and rho. Interacts CC with Grd (alpha chain). 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 ionic channel (TC 1.A.9) CC family. 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; AAF48540.1; -; Genomic_DNA. DR EMBL; AE014298; AAN09377.1; -; Genomic_DNA. DR EMBL; AE014298; AAS65370.1; -; Genomic_DNA. DR EMBL; AY060660; AAL28208.1; -; mRNA. DR PIR; JN0603; JN0603. DR RefSeq; NP_523356.2; -. DR RefSeq; NP_727916.1; -. DR RefSeq; NP_996469.1; -. DR UniGene; Dm.6661; -. DR HSSP; P23415; 1MOT. DR SMR; Q08832; 287-342. DR Ensembl; FBgn0010240; Drosophila melanogaster. DR GeneID; 32554; -. DR KEGG; dme:Dmel_CG17336; -. DR FlyBase; FBgn0010240; Lcch3. DR HOGENOM; Q08832; -. DR OMA; Q08832; GKSERSE. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-002084-MON; -. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-002085-MON; -. DR NextBio; 779108; -. DR ArrayExpress; Q08832; -. DR GermOnline; CG17336; Drosophila melanogaster. DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW. DR GO; GO:0031404; F:chloride ion binding; IEA:UniProtKB-KW. DR GO; GO:0005230; F:extracellular ligand-gated ion channel acti...; IEA:InterPro. DR GO; GO:0004890; F:GABA-A receptor activity; IDA:FlyBase. DR GO; GO:0030594; F:neurotransmitter receptor activity; IEA:InterPro. DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW. DR InterPro; IPR006028; GABAA_rcpt. DR InterPro; IPR002289; GABAAb_rcpt. DR InterPro; IPR006029; Neu_channel_TM. DR InterPro; IPR006202; Neur_chan_lig_bd. DR InterPro; IPR006201; Neur_channel. DR InterPro; IPR018000; Neurotransmitter_ion_chnl_CS. DR Gene3D; G3DSA:2.70.170.10; Neur_chan_lig_bd; 1. DR PANTHER; PTHR18945; Neur_channel; 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 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; KW Complete proteome; Disulfide bond; Glycoprotein; Ion transport; KW Ionic channel; Membrane; Postsynaptic cell membrane; Signal; Synapse; KW Transmembrane; Transport. FT SIGNAL 1 20 Or 27 (Potential). FT CHAIN 21 496 Gamma-aminobutyric acid receptor subunit FT beta-like. FT /FTId=PRO_0000000454. FT TOPO_DOM 21 258 Extracellular (Potential). FT TRANSMEM 259 280 Potential. FT TRANSMEM 285 306 Potential. FT TRANSMEM 318 342 Potential. FT TOPO_DOM 343 472 Cytoplasmic (Potential). FT TRANSMEM 473 494 Potential. FT CARBOHYD 39 39 N-linked (GlcNAc...) (Potential). FT CARBOHYD 189 189 N-linked (GlcNAc...) (Potential). FT DISULFID 176 190 By similarity. FT CONFLICT 12 12 G -> S (in Ref. 1; AAA28559/AAB27090). FT CONFLICT 324 324 V -> C (in Ref. 5). 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 //