ACC3_CAEEL
ID ACC3_CAEEL Reviewed; 517 AA.
AC G5EDN0;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Acetylcholine-gated chloride channel subunit acc-3 {ECO:0000305};
DE Flags: Precursor;
GN Name=acc-3 {ECO:0000312|WormBase:F55D10.5};
GN ORFNames=F55D10.5 {ECO:0000312|WormBase:F55D10.5};
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 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: Probable acetylcholine-gated chloride channel regulatory
CC subunit. Does not have ion channel activity alone as a homopentamer,
CC but forms a functional heteropentameric ion channel with acc-1.
CC {ECO:0000269|PubMed:15579462}.
CC -!- SUBUNIT: Does not form a functional homopentameric ion channel. Forms a
CC functional heteropentameric ion channel composed of acc-1 and acc-3.
CC May interact with acc-2; the interaction does not result in significant
CC heteropentameric ion channel activity. {ECO:0000269|PubMed:15579462}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:15579462};
CC Multi-pass membrane protein {ECO:0000255}.
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; AY849796; AAW34234.1; -; mRNA.
DR EMBL; BX284606; CCD67091.1; -; Genomic_DNA.
DR PIR; T16458; T16458.
DR RefSeq; NP_508810.2; NM_076409.4.
DR AlphaFoldDB; G5EDN0; -.
DR SMR; G5EDN0; -.
DR STRING; 6239.F55D10.5; -.
DR PaxDb; G5EDN0; -.
DR EnsemblMetazoa; F55D10.5.1; F55D10.5.1; WBGene00018880.
DR EnsemblMetazoa; F55D10.5.2; F55D10.5.2; WBGene00018880.
DR GeneID; 186307; -.
DR KEGG; cel:CELE_F55D10.5; -.
DR CTD; 186307; -.
DR WormBase; F55D10.5; CE38372; WBGene00018880; acc-3.
DR eggNOG; KOG3644; Eukaryota.
DR HOGENOM; CLU_010920_1_3_1; -.
DR InParanoid; G5EDN0; -.
DR OMA; VWNELTM; -.
DR OrthoDB; 607837at2759; -.
DR PhylomeDB; G5EDN0; -.
DR Reactome; R-CEL-977443; GABA receptor activation.
DR PRO; PR:G5EDN0; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00018880; Expressed in larva and 2 other tissues.
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 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 Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..517
FT /note="Acetylcholine-gated chloride channel subunit acc-3"
FT /evidence="ECO:0000305"
FT /id="PRO_5008958394"
FT TOPO_DOM 20..277
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..304
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 305..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..338
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 360..494
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 495..515
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 516..517
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT REGION 368..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 191..205
FT /evidence="ECO:0000250|UniProtKB:P02712"
SQ SEQUENCE 517 AA; 59497 MW; 689E41C60A78C2F2 CRC64;
MIRTRHVFLF AVLLAFASSQ TPTPEAKSSE QSLEENKFFP LPPTTPFPTN AVAATDEDGE
ELCTSDKTII EKLLNNYKSF RTPSESGVIV WIEVWVQEVN SVNEITSDFD MDIYVTELWM
DSALRYEHLN PCKYNLSLNS EILDQIWKPN TVFINSKSAN IHKSPFKNVF LMIYPNGTVW
VNYRVQVKGP CSMDFSAFPM DQQSCHLTLE SFSYNNQEVD MQWMNWTTPL SLLKKEIVLP
DFVMSNYSTS LKHEIYPAGV WNELTMTFVF SRRYGWYIFQ AYIPTYLTIF ISWISFCLGP
KMIPARTMLG VNSLLALTFQ FGNIMRNLPR VSYVKALDVW MLVCLTFVFC SLLELAIIGS
MGARSENRQA QQQKQQDEEA TKHQKGRENS TCSHLMSPSS CPNSPRICRN HIPNDVPQSF
KSYGSTDPRM RKRLIIASSS TISHAPNANR SEKVLLLDGL EETQFSQVET KFSSMASIKM
KKHWTTEEID RLSMIMFPGL FTLFNIIYWT YYLTVNT
