GBRB_MUSDO
ID GBRB_MUSDO Reviewed; 576 AA.
AC Q75NA5; O76472;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Gamma-aminobutyric acid receptor subunit beta;
DE AltName: Full=GABA(A) receptor subunit beta;
DE AltName: Full=MdRdl;
DE Flags: Precursor;
GN Name=Rdl {ECO:0000303|PubMed:17201770, ECO:0000312|EMBL:AAC23602.1};
OS Musca domestica (House fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Musca.
OX NCBI_TaxID=7370;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAD16658.2}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBUNIT.
RC STRAIN=WHO/SRS {ECO:0000269|PubMed:17201770};
RC TISSUE=Head {ECO:0000312|EMBL:BAD16658.2};
RX PubMed=17201770; DOI=10.1111/j.1365-2583.2006.00680.x;
RA Eguchi Y., Ihara M., Ochi E., Shibata Y., Matsuda K., Fushiki S.,
RA Sugama H., Hamasaki Y., Niwa H., Wada M., Ozoe F., Ozoe Y.;
RT "Functional characterization of Musca glutamate- and GABA-gated chloride
RT channels expressed independently and coexpressed in Xenopus oocytes.";
RL Insect Mol. Biol. 15:773-783(2006).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAC23602.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 107-558.
RA Glueck S.B., Hook-d'Innocenzo L.E., MacIntyre R.J.;
RT "Molecular evolution of Rdl in insects.";
RL Submitted (JUN-1998) 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:0000269|PubMed:17201770}.
CC -!- SUBUNIT: Homomultimer. {ECO:0000269|PubMed:17201770}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:P25123}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P25123}. Cell membrane
CC {ECO:0000250|UniProtKB:P25123}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P25123}.
CC -!- MISCELLANEOUS: Flies carrying the Rdl-S mutation are resistant to
CC dieldrin. {ECO:0000269|Ref.2}.
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; AB177547; BAD16658.2; -; mRNA.
DR EMBL; AF070935; AAC23602.1; -; mRNA.
DR RefSeq; NP_001292048.1; NM_001305119.1.
DR AlphaFoldDB; Q75NA5; -.
DR SMR; Q75NA5; -.
DR STRING; 7370.XP_005187964.1; -.
DR BindingDB; Q75NA5; -.
DR ChEMBL; CHEMBL3986; -.
DR DrugCentral; Q75NA5; -.
DR GeneID; 101900690; -.
DR KEGG; mde:101900690; -.
DR CTD; 101900690; -.
DR VEuPathDB; VectorBase:MDOA001163; -.
DR eggNOG; KOG3643; Eukaryota.
DR Proteomes; UP000095301; Whole Genome Shotgun Assembly.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008503; F:benzodiazepine receptor activity; ISS:UniProtKB.
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:0007214; P:gamma-aminobutyric acid signaling pathway; ISS:UniProtKB.
DR GO; GO:0006836; P:neurotransmitter transport; ISS:UniProtKB.
DR GO; GO:0001505; P:regulation of neurotransmitter levels; 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 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; Signal; Synapse; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..576
FT /note="Gamma-aminobutyric acid receptor subunit beta"
FT /evidence="ECO:0000255"
FT /id="PRO_0000326433"
FT TOPO_DOM 30..268
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 351..540
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 541..561
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 372..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..494
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 183..197
FT /evidence="ECO:0000250|UniProtKB:P58154"
FT CONFLICT 120
FT /note="R -> G (in Ref. 2; AAC23602)"
FT /evidence="ECO:0000305"
FT CONFLICT 144..154
FT /note="FFVNEKQSYFH -> S (in Ref. 2; AAC23602)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="S -> G (in Ref. 2; AAC23602)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="M -> V (in Ref. 2; AAC23602)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="S -> C (in Ref. 2; AAC23602)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="E -> G (in Ref. 2; AAC23602)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="G -> GGG (in Ref. 2; AAC23602)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 576 AA; 63638 MW; 75F066045FD6F347 CRC64;
MSDSMLYQTL QTCLPKSRLI TLWLAFTLAM LIQEPRRHAA TVNAATAGGS MLGDVNISAI
LDSFSVSYDK RVRPNYGGPP VEVGVTMYVL SISSLSEVKM DFTLDFYFRQ FWTDPRLAYR
KRPGVETLSV GSEFIKNIWV PDTFFVNEKQ SYFHIATTSN EFIRVHHSGS ITRSIRLTIT
ASCPMNLQYF PMDRQLCHIE IESFGYTMRD IRYKWNEGPN SVGVSSEVSL PQFKVLGHRQ
RAVEISLTTG NYSRLACEIQ FVRSMGYYLI QIYIPSGLIV VISWVSFWLN RNATPARVAL
GVTTVLTMTT LMSSTNAALP KISYVKSIDV YLGTCFVMVF ASLLEYATVG YMAKRIQMRK
QRFMTIQKMA EQKKQQQLDG VQPPPNPNPN TMVDHGGHGH GHGHHSHGHP HVPKQTVSNR
PIGFQTMQQQ NIGGRGCSIV GPLFQEVRFK VHDPKAHSKG GTLENTVNGG RGGPPVGPHG
PGPQGPPGGP PAGGGGGGAP PEGGDAEAAV PAHLLHPGKV KKDINKLLGI TPSDIDKYSR
IVFPVCFVCF NLMYWIIYLH VSDVVADDLV LLGEEK
