ID   GBRB_DROSI              Reviewed;         606 AA.
AC   Q9BLY8;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Gamma-aminobutyric acid receptor subunit beta;
DE   AltName: Full=GABA(A) receptor;
DE   AltName: Full=Protein cyclodiene resistance;
DE   Flags: Precursor;
GN   Name=Rdl;
OS   Drosophila simulans (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7240 {ECO:0000312|EMBL:AAK00512.1};
RN   [1] {ECO:0000312|EMBL:AAK00512.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Le Goff G., Berge J.-B., Amichot M.;
RT   "Cloning of a Drosophila simulans gamma-aminobutyric acid receptor.";
RL   Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: GABA, an inhibitory neurotransmitter, mediates neuronal
CC       inhibition by binding to the GABA receptor and opening an integral
CC       chloride channel. {ECO:0000305}.
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; AY017266; AAK00512.1; -; mRNA.
DR   AlphaFoldDB; Q9BLY8; -.
DR   SMR; Q9BLY8; -.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0034707; C:chloride channel complex; 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:0005230; F:extracellular ligand-gated ion channel activity; IEA:InterPro.
DR   GO; GO:0004890; F:GABA-A receptor activity; IEA:InterPro.
DR   GO; GO:0030594; F:neurotransmitter receptor activity; ISS:UniProtKB.
DR   GO; GO:0006811; P:ion transport; ISS:UniProtKB.
DR   Gene3D; 1.20.58.390; -; 2.
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   2: Evidence at transcript 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; Signal; Synapse; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL          1..44
FT                   /evidence="ECO:0000255"
FT   CHAIN           45..606
FT                   /note="Gamma-aminobutyric acid receptor subunit beta"
FT                   /id="PRO_0000000453"
FT   TOPO_DOM        45..268
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        269..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        297..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        333..356
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        357..568
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        569..590
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          376..451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          482..542
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..393
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        58
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        253
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   DISULFID        185..199
FT                   /evidence="ECO:0000250|UniProtKB:P02708"
SQ   SEQUENCE   606 AA;  65642 MW;  394D0275DA51800A CRC64;
     MSDSKMDKLA RMAPLPRTPL LTIWLAINMA LIAQETGHKR IHTVQAATGG GSMLGDVNIS
     AILDSFSVSY DKRVRPNYGG PPVEVGVTMY VLSISSLSEV KMDFTLDFYF RQFWTDPRLA
     YRKRPGVETL SVGSEFIKNI WVPDTFFVNE KQSYFHIATT SNEFIRVHHS GSITRSIRLT
     ITASCPMNLQ YFPMDRQLCH IEIESFGYTM RDIRYKWNEG PNSVGVSSEV SLPQFKVLGH
     RQRAMEISLT TGNYSRLACE IQFVRSMGYY LIQIYIPSGL IVVISWVSFW LNRNATPARV
     ALGVTTVLTM TTLMSSTNAA LPKISYVKSI DVYLGTCFVM VFASLLEYAT VGYMAKRIQM
     RKQRFMAIQK IAEQKKQQLD GANQQQANPN PNANVGGPGG VGVGPGGPGG PGGGVNVGVG
     MGMGPEHGHG HGHHAHSHGH PHAPKQTVSN RPIGFSNIQQ NVGTRGCSIV GPLFQEVRFK
     VHDPKAHSKG GTLENTVNGG RGGPQSHGPG PGQGGGPPGG GGGGGGGGGP PEGGGDPEAA
     VPAHLLHPGK VKKDINKLLG ITPSDIDKYS RIVFPVCFVC FNLMYWIIYL HVSDVVADDL
     VLLGEE