ID ACC2_CAEEL Reviewed; 445 AA.
AC Q18812;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 167.
DE RecName: Full=Acetylcholine-gated chloride channel subunit acc-2 {ECO:0000305};
DE Flags: Precursor;
GN Name=acc-2 {ECO:0000312|WormBase:C53D6.3};
GN ORFNames=C53D6.3 {ECO:0000312|WormBase:C53D6.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=15579462; DOI=10.1074/jbc.m412644200;
RA Putrenko I., Zakikhani M., Dent J.A.;
RT "A family of acetylcholine-gated chloride channel subunits in
RT Caenorhabditis elegans.";
RL J. Biol. Chem. 280:6392-6398(2005).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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 TISSUE SPECIFICITY.
RX PubMed=26705699; DOI=10.7554/elife.12432;
RA Pereira L., Kratsios P., Serrano-Saiz E., Sheftel H., Mayo A.E., Hall D.H.,
RA White J.G., LeBoeuf B., Garcia L.R., Alon U., Hobert O.;
RT "A cellular and regulatory map of the cholinergic nervous system of C.
RT elegans.";
RL Elife 4:12432-12477(2015).
RN [4] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=27782882; DOI=10.7554/elife.21734;
RA Takayanagi-Kiya S., Zhou K., Jin Y.;
RT "Release-dependent feedback inhibition by a presynaptically localized
RT ligand-gated anion channel.";
RL Elife 5:21734-21749(2016).
CC -!- FUNCTION: Acetylcholine-gated chloride channel subunit. Currents in
CC channels are triggered in response to acetylcholine. Channel properties
CC may be modulated by the formation of homomeric and heteromeric
CC channels. {ECO:0000269|PubMed:15579462}.
CC -!- SUBUNIT: Homopentamer (in vitro). May interact with either acc-3 or
CC acc-4; the interactions do not result in significant heteropentameric
CC ion channel activity. {ECO:0000269|PubMed:15579462}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15579462};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in RIA, RIG, PHA and AIZ glutamatergic
CC neurons, URX and RIH cholinergic neurons, and in male-specific MCM
CC neurons. {ECO:0000269|PubMed:26705699}.
CC -!- DISRUPTION PHENOTYPE: Grossly normal movement.
CC {ECO:0000269|PubMed:27782882}.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC {ECO:0000305}.
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DR EMBL; BX284604; CAA94228.1; -; Genomic_DNA.
DR PIR; T20190; T20190.
DR RefSeq; NP_501567.1; NM_069166.1.
DR AlphaFoldDB; Q18812; -.
DR SMR; Q18812; -.
DR STRING; 6239.C53D6.3.1; -.
DR GlyCosmos; Q18812; 5 sites, No reported glycans.
DR PaxDb; 6239-C53D6-3; -.
DR EnsemblMetazoa; C53D6.3.1; C53D6.3.1; WBGene00008280.
DR GeneID; 183758; -.
DR KEGG; cel:CELE_C53D6.3; -.
DR UCSC; C53D6.3; c. elegans.
DR AGR; WB:WBGene00008280; -.
DR WormBase; C53D6.3; CE05488; WBGene00008280; acc-2.
DR eggNOG; KOG3644; Eukaryota.
DR HOGENOM; CLU_010920_1_3_1; -.
DR InParanoid; Q18812; -.
DR OMA; IYITETW; -.
DR OrthoDB; 2873291at2759; -.
DR PhylomeDB; Q18812; -.
DR Reactome; R-CEL-112314; Neurotransmitter receptors and postsynaptic signal transmission.
DR PRO; PR:Q18812; -.
DR Proteomes; UP000001940; Chromosome IV.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma 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:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:1904315; F:transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR CDD; cd18990; LGIC_ECD_GABAAR; 1.
DR CDD; cd19049; LGIC_TM_anion; 1.
DR Gene3D; 2.70.170.10; Neurotransmitter-gated ion-channel ligand-binding domain; 1.
DR Gene3D; 1.20.58.390; Neurotransmitter-gated ion-channel transmembrane domain; 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:SF569; ACETYLCHOLINE-GATED CHLORIDE CHANNEL SUBUNIT ACC-2; 1.
DR PANTHER; PTHR18945; NEUROTRANSMITTER GATED ION CHANNEL; 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; SSF90112; Neurotransmitter-gated ion-channel transmembrane pore; 1.
DR SUPFAM; SSF63712; Nicotinic receptor ligand binding domain-like; 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 Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..445
FT /note="Acetylcholine-gated chloride channel subunit acc-2"
FT /evidence="ECO:0000305"
FT /id="PRO_5004186831"
FT TOPO_DOM 27..258
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280..286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..326
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..407
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 429..445
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 177..191
FT /evidence="ECO:0000250|UniProtKB:P02712"
SQ SEQUENCE 445 AA; 51686 MW; 3F60AE853A50F4FC CRC64;
MIFTLLSTLP VLIITTELDY SELVHSAELV SSSSYIHHKT NKKPDNCTRD TDIIDRLLNG
TGYNKFRIPQ EEGMTVVVEI WIQAITSIDE LTNDFDMDIY ITETWLDPAL NFQTMTPCKG
NLSLNHQVLD RLWTPNSCFI NSKVAQIHNS PFRSVFLMLF PNGTVMVNYR VRVKGPCSLD
LSNFPLDLQK CSLIYESFNY NRQEVEMRWS DAEHPVFNLS KIMLPDFDLF EIQTERRQEP
YPAGMWDELH VTIIFERRFI WYFMQAYLPT YLTIFISWIS FSLGSRAIPA RTMLGVNSLL
AIVFSFGNIM RNLPRVSYIK GIDVWMLVSM TFIFCSLLEL AIVGFMVRDE TVAKKKQQKK
ISGNISREES PHGIISERRF MFPPGCSESS KSLSSCTSGW TPERIDSISS VMFPFSFFVF
NIIYWFYYIH RKEIIKQNLI NRVDG
//
