ACC1_CAEEL
ID ACC1_CAEEL Reviewed; 466 AA.
AC Q21005;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Acetylcholine-gated chloride channel subunit acc-1 {ECO:0000305};
DE Flags: Precursor;
GN Name=acc-1 {ECO:0000312|WormBase:F58G6.4a};
GN ORFNames=F58G6.4 {ECO:0000312|WormBase:F58G6.4a};
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. Forms
CC functional homopentameric (in vitro) and functional heteropentameric
CC ion channels with acc-3 and acc-4 ion channel subunits. Currents in
CC channels are triggered in response to acetylcholine, but not in
CC response to GABA, glutamate, glycine, histamine or dopamine.
CC {ECO:0000269|PubMed:15579462}.
CC -!- SUBUNIT: Homopentamer (in vitro). Forms heteropentamers composed of
CC acc-1 and acc-4 or acc-1 and acc-3. Both homopentamers and
CC heteropentamers form functional ion channels.
CC {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 a subset of cholinergic motor neurons
CC including cholinergic motor neurons in the ventral cord, the
CC retrovesicular ganglion and in head neurons such as the SMD, RMD motor
CC neurons, the AVA and AVE command interneurons and the SAA neurons. Also
CC expressed in a small number of glutamatergic neurons including the
CC pharyngeal neurons MI and M3, the PLM neurons and a pair of neurons in
CC the lateral ganglion. {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; CAA92466.2; -; Genomic_DNA.
DR PIR; T22947; T22947.
DR RefSeq; NP_501715.1; NM_069314.4.
DR AlphaFoldDB; Q21005; -.
DR SMR; Q21005; -.
DR STRING; 6239.F58G6.4; -.
DR PaxDb; Q21005; -.
DR EnsemblMetazoa; F58G6.4a.1; F58G6.4a.1; WBGene00010275.
DR EnsemblMetazoa; F58G6.4a.2; F58G6.4a.2; WBGene00010275.
DR GeneID; 177799; -.
DR UCSC; F58G6.4; c. elegans.
DR CTD; 177799; -.
DR WormBase; F58G6.4a; CE28039; WBGene00010275; acc-1.
DR eggNOG; KOG3644; Eukaryota.
DR HOGENOM; CLU_010920_1_3_1; -.
DR InParanoid; Q21005; -.
DR OrthoDB; 466513at2759; -.
DR PhylomeDB; Q21005; -.
DR Reactome; R-CEL-977443; GABA receptor activation.
DR PRO; PR:Q21005; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00010275; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; Q21005; baseline and differential.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
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: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: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; IBA:GO_Central.
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 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 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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..466
FT /note="Acetylcholine-gated chloride channel subunit acc-1"
FT /evidence="ECO:0000305"
FT /id="PRO_5004199465"
FT TOPO_DOM 25..242
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..272
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 273..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..304
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..427
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 428..448
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 449..466
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT REGION 333..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 158..172
FT /evidence="ECO:0000250|UniProtKB:P02712"
SQ SEQUENCE 466 AA; 54967 MW; 2D6B40994889C80D CRC64;
MSHPGWIMVS FLTELLSQSS KGIAQSLDNC ANDTEIINAL LKDSYNKHYI PSHPTHVRVD
MWVQEVTSVS ELTQDFEIDL YINEFWEDPA LVYEDMNPCK RNISFDDKVL QRLWLPNTCF
INSKSAAIHE SPFKNVFLMV FSNGTLWTNY RMKLTGPCDM KLKRFPFDKQ KCYLTFESFN
YNTGEVRMQW NQPYPVILLK RIELPDFKLV NFSVIAVEQM YPAGWWDELT VAFVFERRYG
WYVLQGYIPT MVTIVISWIS FYLGPRAIPA RTMLGVNSLL AMTFQFGNII RNLPRVSYVK
AIDVWMLSGM LFIFLSLLEL AVVGFMSRNE GLPPKVKKRK RQEDDDEGFS WKSMQTSPHL
ELRQFWVDKR VNSLRNDSAV PPVEDYAPME LEQPYQNITK RREKRKWMSG LRKKWRAMRE
LRPETVDFYS AIFFPTAYML FNISYWSFYL TSLSEYFDED VNIDQP
