GLUCB_CAEEL
ID GLUCB_CAEEL Reviewed; 434 AA.
AC Q17328; O02524;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Glutamate-gated chloride channel subunit beta;
DE Short=Glu-Cl subunit beta;
DE AltName: Full=Avermectin-sensitive glutamate-gated chloride channel subunit;
DE Flags: Precursor;
GN Name=glc-2; ORFNames=F25F8.2;
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], FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND
RP INTERACTION WITH GLC-1.
RC STRAIN=Bristol N2;
RX PubMed=7935817; DOI=10.1038/371707a0;
RA Cully D.F., Vassilatis D.K., Liu K.K., Paress P.S., Van der Ploeg L.H.T.,
RA Schaeffer J.M., Arena J.P.;
RT "Cloning of an avermectin-sensitive glutamate-gated chloride channel from
RT Caenorhabditis elegans.";
RL Nature 371:707-711(1994).
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).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-50, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
CC -!- FUNCTION: Glutamate-gated chloride channel subunit; channel properties
CC depend on the subunit composition. Glutamate binding triggers a rapidly
CC reversible current in heteromeric channels formed by glc-1 and glc-2,
CC while the anti-helmintic drug ivermectin and other avermectins trigger
CC a permanently open channel configuration. Channels containing only glc-
CC 2 are activated by glutamate, but not by ivermectin (in vitro). The
CC heteromeric channel formed by glc-1 and glc-2 is also activated by
CC ibotenate, and it is blocked by picrotoxin and flufenamic acid
CC (PubMed:7935817). {ECO:0000269|PubMed:7935817}.
CC -!- SUBUNIT: Pentamer (By similarity). Homooligomer that can form
CC functional heterooligomers with glc-1 (PubMed:7935817).
CC {ECO:0000250|UniProtKB:G5EBR3, ECO:0000269|PubMed:7935817}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q94900}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q94900}. Cell membrane {ECO:0000255,
CC ECO:0000269|PubMed:7935817}; Multi-pass membrane protein {ECO:0000255,
CC ECO:0000269|PubMed:7935817}.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC Glutamate-gated chloride channel (TC 1.A.9.4) subfamily. {ECO:0000305}.
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DR EMBL; U14525; AAA50786.1; -; mRNA.
DR EMBL; FO080262; CCD62432.1; -; Genomic_DNA.
DR PIR; S50865; S50865.
DR RefSeq; NP_491470.1; NM_059069.3.
DR AlphaFoldDB; Q17328; -.
DR SMR; Q17328; -.
DR BioGRID; 37565; 4.
DR DIP; DIP-27494N; -.
DR STRING; 6239.F25F8.2; -.
DR iPTMnet; Q17328; -.
DR PaxDb; Q17328; -.
DR EnsemblMetazoa; F25F8.2.1; F25F8.2.1; WBGene00001592.
DR GeneID; 172103; -.
DR KEGG; cel:CELE_F25F8.2; -.
DR UCSC; F25F8.2; c. elegans.
DR CTD; 172103; -.
DR WormBase; F25F8.2; CE09636; WBGene00001592; glc-2.
DR eggNOG; KOG3644; Eukaryota.
DR GeneTree; ENSGT00940000172299; -.
DR HOGENOM; CLU_010920_1_4_1; -.
DR InParanoid; Q17328; -.
DR OMA; ENMFLRI; -.
DR OrthoDB; 614790at2759; -.
DR PhylomeDB; Q17328; -.
DR Reactome; R-CEL-112314; Neurotransmitter receptors and postsynaptic signal transmission.
DR PRO; PR:Q17328; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00001592; Expressed in larva and 3 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:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
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:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0008068; F:extracellularly glutamate-gated chloride channel activity; IDA:UniProtKB.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
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; IBA:GO_Central.
DR GO; GO:1902476; P:chloride transmembrane transport; IDA:UniProtKB.
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 CDD; cd19062; LGIC_TM_GluCl; 1.
DR Gene3D; 1.20.58.390; -; 1.
DR Gene3D; 2.70.170.10; -; 1.
DR InterPro; IPR006028; GABAA/Glycine_rcpt.
DR InterPro; IPR015680; Glu_Cl_Channel.
DR InterPro; IPR044721; GluCl_TM.
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 PANTHER; PTHR18945:SF504; PTHR18945:SF504; 1.
DR Pfam; PF02931; Neur_chan_LBD; 1.
DR Pfam; PF02932; Neur_chan_memb; 1.
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; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..434
FT /note="Glutamate-gated chloride channel subunit beta"
FT /id="PRO_0000255716"
FT TOPO_DOM 23..246
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT TRANSMEM 247..269
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT TOPO_DOM 270..274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT TRANSMEM 275..296
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT TOPO_DOM 297..303
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT TRANSMEM 304..324
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT TOPO_DOM 325..398
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT TRANSMEM 399..422
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT TOPO_DOM 423..434
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT BINDING 66
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT BINDING 85
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT BINDING 152
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT BINDING 181
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 161..175
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT DISULFID 223..234
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
SQ SEQUENCE 434 AA; 49893 MW; 754B973359834F75 CRC64;
MTTPSSFSIL LLLLLMPVVT NGEYSMQSEQ EILNALLKNY DMRVRPPPAN SSTEGAVNVR
VNIMIRMLSK IDVVNMEYSI QLTFREQWID PRLAYENLGF YNPPAFLTVP HVKKSLWIPD
TFFPTEKAAH RHLIDMENMF LRIYPDGKIL YSSRISLTSS CPMRLQLYPL DYQSCNFDLV
SYAHTMNDIM YEWDPSTPVQ LKPGVGSDLP NFILKNYTTN ADCTSHTNTG SYGCLRMQLL
FKRQFSYYLV QLYAPTTMIV IVSWVSFWID LHSTAGRVAL GVTTLLTMTT MQSAINAKLP
PVSYVKVVDV WLGACQTFVF GALLEYAFVS YQDSVRQNDR SREKAARKAQ RRREKLEMVD
AEVYQPPCTC HTFEARETFR DKVRRYFTKP DYLPAKIDFY ARFVVPLAFL AFNVIYWVSC
LIMSANASTP ESLV
