GBR1_CAEEL
ID GBR1_CAEEL Reviewed; 539 AA.
AC G5ECJ0; Q6TXQ9;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Gamma-aminobutyric acid receptor exp-1 {ECO:0000303|PubMed:14555952};
DE AltName: Full=Expulsion defective protein 3 {ECO:0000303|PubMed:14555952};
DE AltName: Full=GABA(A) receptor {ECO:0000303|PubMed:14555952};
DE Flags: Precursor;
GN Name=exp-1 {ECO:0000312|EMBL:CCD70946.1, ECO:0000312|WormBase:H35N03.1};
GN ORFNames=H35N03.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAQ96595.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1A AND
RP 1B), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF SER-140; PRO-187; MET-233 AND ASP-280.
RX PubMed=14555952; DOI=10.1038/nn1136;
RA Beg A.A., Jorgensen E.M.;
RT "EXP-1 is an excitatory GABA-gated cation channel.";
RL Nat. Neurosci. 6:1145-1152(2003).
RN [2] {ECO:0000312|EMBL:CCD70946.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CCD70946.1};
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] {ECO:0000305}
RP FUNCTION.
RX PubMed=2323555; DOI=10.1093/genetics/124.4.855;
RA Thomas J.H.;
RT "Genetic analysis of defecation in Caenorhabditis elegans.";
RL Genetics 124:855-872(1990).
RN [4] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF ASP-280.
RX PubMed=16236771; DOI=10.1242/dev.02069;
RA Branicky R., Hekimi S.;
RT "Specification of muscle neurotransmitter sensitivity by a Paired-like
RT homeodomain protein in Caenorhabditis elegans.";
RL Development 132:4999-5009(2005).
RN [5] {ECO:0000305}
RP INTERACTION WITH TAX-6, AND DISRUPTION PHENOTYPE.
RX PubMed=16084527; DOI=10.1016/j.jmb.2005.07.032;
RA Lee J., Song H.O., Jee C., Vanoaica L., Ahnn J.;
RT "Calcineurin regulates enteric muscle contraction through EXP-1, excitatory
RT GABA-gated channel, in C. elegans.";
RL J. Mol. Biol. 352:313-318(2005).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF ASP-280.
RX PubMed=25849533; DOI=10.1371/journal.pone.0124515;
RA Sheng M., Hosseinzadeh A., Muralidharan S.V., Gaur R., Selstam E., Tuck S.;
RT "Aberrant fat metabolism in Caenorhabditis elegans mutants with defects in
RT the defecation motor program.";
RL PLoS ONE 10:E0124515-E0124515(2015).
CC -!- FUNCTION: GABA receptor that functions as an excitatory cation channel.
CC Permeable to monovalent cations such as Na(+) and K(+)
CC (PubMed:14555952). Has negligible divalent cation permeability
CC (PubMed:14555952). Does not act as a chloride channel
CC (PubMed:14555952). Mediates enteric muscle contractions required for
CC defecation (PubMed:14555952, PubMed:2323555, PubMed:16236771). Probably
CC by regulating the defecation motor program, required for fatty acid
CC uptake by intestinal cells (PubMed:25849533).
CC {ECO:0000269|PubMed:14555952, ECO:0000269|PubMed:16236771,
CC ECO:0000269|PubMed:2323555, ECO:0000269|PubMed:25849533}.
CC -!- SUBUNIT: Interacts with tax-6; tax-6 may be involved in negative
CC regulation of exp-1 activity. May self-associate to form homodimer.
CC {ECO:0000269|PubMed:16084527, ECO:0000303|PubMed:14555952}.
CC -!- SUBCELLULAR LOCATION: Synapse {ECO:0000269|PubMed:14555952}. Cell
CC membrane {ECO:0000250|UniProtKB:P18505}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P18505}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1B {ECO:0000269|PubMed:14555952};
CC IsoId=G5ECJ0-1; Sequence=Displayed;
CC Name=1A {ECO:0000269|PubMed:14555952};
CC IsoId=G5ECJ0-2; Sequence=VSP_053252;
CC -!- TISSUE SPECIFICITY: Expressed in the intestinal and anal depressor
CC muscles but not in the sphincter muscle. Also detected in the RID and
CC SABD ring interneurons, the ADE sensory neuron and the PDA motor
CC neuron. {ECO:0000269|PubMed:14555952, ECO:0000269|PubMed:16236771}.
CC -!- DISRUPTION PHENOTYPE: Defective in enteric muscle contraction resulting
CC in abnormal defecation cycles and moderate to severe constipation.
CC {ECO:0000269|PubMed:16084527}.
CC -!- MISCELLANEOUS: Resistant to channel blocking activity of mecamylamine
CC and bicuculline. {ECO:0000269|PubMed:14555952}.
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:0000255}.
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DR EMBL; AY383563; AAQ96594.1; -; Genomic_DNA.
DR EMBL; AY383563; AAQ96595.1; -; Genomic_DNA.
DR EMBL; FO081349; CCD70946.1; -; Genomic_DNA.
DR PIR; T33513; T33513.
DR RefSeq; NP_495229.3; NM_062828.4. [G5ECJ0-1]
DR AlphaFoldDB; G5ECJ0; -.
DR SMR; G5ECJ0; -.
DR BioGRID; 51521; 1.
DR STRING; 6239.H35N03.1; -.
DR PaxDb; G5ECJ0; -.
DR EnsemblMetazoa; H35N03.1.1; H35N03.1.1; WBGene00001373. [G5ECJ0-1]
DR GeneID; 186801; -.
DR KEGG; cel:CELE_H35N03.1; -.
DR UCSC; H35N03.1; c. elegans.
DR CTD; 186801; -.
DR WormBase; H35N03.1; CE37026; WBGene00001373; exp-1. [G5ECJ0-1]
DR eggNOG; KOG3643; Eukaryota.
DR HOGENOM; CLU_010920_7_0_1; -.
DR InParanoid; G5ECJ0; -.
DR OMA; ISLVCEC; -.
DR OrthoDB; 957366at2759; -.
DR PhylomeDB; G5ECJ0; -.
DR Reactome; R-CEL-977443; GABA receptor activation.
DR PRO; PR:G5ECJ0; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00001373; Expressed in larva and 3 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0031594; C:neuromuscular junction; IDA:WormBase.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IDA:WormBase.
DR GO; GO:0016917; F:GABA 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; IBA:GO_Central.
DR GO; GO:0030421; P:defecation; IMP:WormBase.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0010877; P:lipid transport involved in lipid storage; IMP:UniProtKB.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:1904731; P:positive regulation of intestinal lipid absorption; IMP:UniProtKB.
DR GO; GO:0045933; P:positive regulation of muscle contraction; IMP:WormBase.
DR GO; GO:0006813; P:potassium ion transport; IDA:WormBase.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0006814; P:sodium ion transport; IDA:WormBase.
DR Gene3D; 1.20.58.390; -; 1.
DR Gene3D; 2.70.170.10; -; 1.
DR InterPro; IPR006028; GABAA/Glycine_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; PR00253; GABAARECEPTR.
DR PRINTS; PR00252; NRIONCHANNEL.
DR SUPFAM; SSF63712; SSF63712; 1.
DR SUPFAM; SSF90112; SSF90112; 1.
DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Ion channel;
KW Ion transport; Membrane; Receptor; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..539
FT /note="Gamma-aminobutyric acid receptor exp-1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000423667"
FT TOPO_DOM 17..314
FT /note="Extracellular"
FT /evidence="ECO:0000255, ECO:0000305"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000305"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000305"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000305"
FT TOPO_DOM 395..493
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255, ECO:0000305"
FT TRANSMEM 494..514
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000305"
FT REGION 48..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 231..245
FT /evidence="ECO:0000250|UniProtKB:P02712"
FT VAR_SEQ 92..97
FT /note="Missing (in isoform 1A)"
FT /evidence="ECO:0000303|PubMed:14555952"
FT /id="VSP_053252"
FT MUTAGEN 140
FT /note="S->F: In n2570; Defective enteric muscle
FT contraction."
FT /evidence="ECO:0000269|PubMed:14555952"
FT MUTAGEN 187
FT /note="P->S: In n2676; Defective enteric muscle
FT contraction."
FT /evidence="ECO:0000269|PubMed:14555952"
FT MUTAGEN 233
FT /note="M->I: In n2641; Defective enteric muscle
FT contraction."
FT /evidence="ECO:0000269|PubMed:14555952"
FT MUTAGEN 280
FT /note="D->N: In sa6; Defective enteric muscle contraction
FT and shortening of defecation cycle. Reduced fatty acid
FT uptake by intestinal cells."
FT /evidence="ECO:0000269|PubMed:14555952,
FT ECO:0000269|PubMed:16236771, ECO:0000269|PubMed:25849533"
SQ SEQUENCE 539 AA; 62554 MW; 3522DBD4585F4EAF CRC64;
MSASILILAT CHQVLADFNS YVVPQPHAQR DHRQDISQHY DYLMEENDEP LGRGAAPSKY
RSSHGQAQHR PEMTESENFA QPNTESVFSS GGVDSYGETR DFLQFLRRIQ YDHRQVPENE
KGEATYVEVS VVVSNIRAVS EVTMDYALEL FYRESWRDPR LQYDRKLFKN KTELALHESY
TNFLWFPDTF VPNAIASKNP QRNSISHRSL LRLDETGKLL YSRRISLVCE CTMDLTLFPF
DKQLCKLGIE SYGYTADHVV YKWSKGARTA LELKKIRLPD FTIQEAYVTS QMESYATGNY
SRLYVCFVFS RSSGFCFLQL IIPSTAVVIT SWVSLWMETE TEFQDMISII LAITFLIFSY
NEMMPRVSYI KAMDIYLGVC FMIVFLSLIK LALVKYMRQK IMLTSDSGNS LREMSQMSTR
QRLRARKTSN MNFRNNGGGS IPINEEHQQM LTVPNGEDKM ANGDDKEANN NGKSHLSDML
EIRITQRTMH RFHWISQMLF FFGFVIFCLF YFLIYPNLHI VSVDPACDKN LAEWFADIY
