GBRB_CAEEL
ID GBRB_CAEEL Reviewed; 550 AA.
AC O18276; Q8ITG2;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 3.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Gamma-aminobutyric acid receptor subunit beta;
DE AltName: Full=GABA(A) receptor subunit beta;
DE Flags: Precursor;
GN Name=gab-1; ORFNames=ZC482.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=12421359; DOI=10.1046/j.1471-4159.2002.01199.x;
RA Feng X.-P., Hayashi J., Beech R.N., Prichard R.K.;
RT "Study of the nematode putative GABA type-A receptor subunits: evidence for
RT modulation by ivermectin.";
RL J. Neurochem. 83:870-878(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: GABA, an inhibitory neurotransmitter, mediates neuronal
CC inhibition by binding to the GABA receptor and opening an integral
CC chloride channel. {ECO:0000250, ECO:0000269|PubMed:12421359}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
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; AF498370; AAN65376.1; -; mRNA.
DR EMBL; Z93397; CAB07719.3; -; Genomic_DNA.
DR PIR; T27614; T27614.
DR RefSeq; NP_499661.2; NM_067260.3.
DR AlphaFoldDB; O18276; -.
DR SMR; O18276; -.
DR BioGRID; 41867; 2.
DR STRING; 6239.ZC482.1; -.
DR DrugCentral; O18276; -.
DR PaxDb; O18276; -.
DR EnsemblMetazoa; ZC482.1.1; ZC482.1.1; WBGene00001512.
DR GeneID; 176691; -.
DR KEGG; cel:CELE_ZC482.1; -.
DR UCSC; ZC482.1; c. elegans.
DR CTD; 176691; -.
DR WormBase; ZC482.1; CE33742; WBGene00001512; gab-1.
DR eggNOG; KOG3643; Eukaryota.
DR GeneTree; ENSGT00940000166778; -.
DR HOGENOM; CLU_010920_0_1_1; -.
DR InParanoid; O18276; -.
DR OMA; EIPIDEM; -.
DR OrthoDB; 480926at2759; -.
DR PhylomeDB; O18276; -.
DR Reactome; R-CEL-977443; GABA receptor activation.
DR PRO; PR:O18276; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00001512; Expressed in larva and 2 other tissues.
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:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0005230; F:extracellular ligand-gated ion channel activity; IDA:WormBase.
DR GO; GO:0004890; F:GABA-A receptor activity; IDA:WormBase.
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; ISS:WormBase.
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:0006811; P:ion transport; IDA:WormBase.
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 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; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..550
FT /note="Gamma-aminobutyric acid receptor subunit beta"
FT /id="PRO_0000255714"
FT TOPO_DOM 25..264
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 345..527
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 528..548
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 405..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 180..194
FT /evidence="ECO:0000250"
FT CONFLICT 16
FT /note="L -> S (in Ref. 1; AAN65376)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="P -> S (in Ref. 1; AAN65376)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="Q -> E (in Ref. 1; AAN65376)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="V -> D (in Ref. 1; AAN65376)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 550 AA; 62457 MW; 5DF089E1101438E5 CRC64;
MRRSKTRRIF HVSITLLLVS TIFCQNGTKP HNNSTSDQMS SSWSNRSQTM YSNASSLLSD
LLLDYDIRLR PGFGGDALLL TMDIIIASFD SISEVDMDYT LTMYLHQYWT DERLRWSNEI
PIDEMTLSGE FSQNIWVPDT FLANDKHSYL HEVTERNKML RINVDGKVAY GMRLTSTLSC
SMNLRNFPLD SQNCTVEIES YGYTTSEVLM KWNYPLAVHG VEQADVPQFT ITGFHTEDSI
VSTATGSYQR LSLVFQLRRS VGYFIFQTYL PCVLIVMLSW VSFWINHEAT SARVALGITT
VLTMTTISTG VRQSLPRISY VKSIDIYLVM CFVFVFAALL EYAAVNYSYW GRERGKGGGG
NEWPVNGANK EDRESAVNVQ KWVPSGLMDG VPQPQDRRVE ALEEAMSTSN TAAQNNNFES
TSKPKKRSSS PIPPLCRAGN TISEESESPD YPRYSTTSLK GARPHASLNH KTHHLKGRSS
ARAKRRMTLA RMNVSMKQSI SGIGRRARKV IPTIRVRDVN LIDKYSRVVF PVCFIVFNLF
YWSYYMMVPS
