ACH1_CAEEL
ID ACH1_CAEEL Reviewed; 498 AA.
AC P48180; Q8I932;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Acetylcholine receptor subunit alpha-type acr-16;
DE Flags: Precursor;
GN Name=acr-16; Synonyms=Ce21; ORFNames=F25G6.3;
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] (ISOFORMS A AND B), AND FUNCTION.
RC STRAIN=Bristol N2;
RX PubMed=8627624; DOI=10.1006/jmbi.1996.0248;
RA Ballivet M., Alliod C., Bertrand S., Bertrand D.;
RT "Nicotinic acetylcholine receptors in the nematode Caenorhabditis
RT elegans.";
RL J. Mol. Biol. 258:261-269(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Bristol N2;
RA Kohara Y., Shin-i T., Suzuki Y., Sugano S., Thierry-Mieg D.,
RA Thierry-Mieg J.;
RT "The Caenorhabditis elegans transcriptome project, a complementary view of
RT the genome.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15917232; DOI=10.1074/jbc.m502818200;
RA Touroutine D., Fox R.M., Von Stetina S.E., Burdina A., Miller D.M. III,
RA Richmond J.E.;
RT "acr-16 encodes an essential subunit of the levamisole-resistant nicotinic
RT receptor at the Caenorhabditis elegans neuromuscular junction.";
RL J. Biol. Chem. 280:27013-27021(2005).
RN [5]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=15944127; DOI=10.1016/j.neuron.2005.04.010;
RA Francis M.M., Evans S.P., Jensen M., Madsen D.M., Mancuso J., Norman K.R.,
RA Maricq A.V.;
RT "The Ror receptor tyrosine kinase CAM-1 is required for ACR-16-mediated
RT synaptic transmission at the C. elegans neuromuscular junction.";
RL Neuron 46:581-594(2005).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=17128266; DOI=10.1038/nn1810;
RA Sieburth D., Madison J.M., Kaplan J.M.;
RT "PKC-1 regulates secretion of neuropeptides.";
RL Nat. Neurosci. 10:49-57(2007).
CC -!- FUNCTION: After binding acetylcholine, the AChR responds by an
CC extensive change in conformation that affects all subunits and leads to
CC opening of an ion-conducting channel across the plasma membrane (By
CC similarity). A subunit of the levamisole-insensitive nicotinic
CC receptor. {ECO:0000250, ECO:0000269|PubMed:15917232,
CC ECO:0000269|PubMed:8627624}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000269|PubMed:15944127}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15944127}. Cell membrane
CC {ECO:0000269|PubMed:15944127}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15944127}. Note=The cam-1 protein is required for
CC correct localization.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=P48180-1; Sequence=Displayed;
CC Name=b;
CC IsoId=P48180-2; Sequence=VSP_036472;
CC -!- TISSUE SPECIFICITY: Expressed in the body wall muscle.
CC {ECO:0000269|PubMed:15917232}.
CC -!- DISRUPTION PHENOTYPE: Uncoordinated movement and reduced body wall
CC muscle currents. These phenotypes are probably related.
CC {ECO:0000269|PubMed:15944127, ECO:0000269|PubMed:17128266}.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC Acetylcholine receptor (TC 1.A.9.1) subfamily. {ECO:0000305}.
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DR EMBL; X83887; CAA58764.1; -; mRNA.
DR EMBL; FO080489; CCD64102.1; -; Genomic_DNA.
DR EMBL; FO080489; CCD64103.1; -; Genomic_DNA.
DR EMBL; AY523511; AAR98633.1; -; mRNA.
DR PIR; S68588; S68588.
DR RefSeq; NP_505207.1; NM_072806.4. [P48180-1]
DR AlphaFoldDB; P48180; -.
DR SMR; P48180; -.
DR BioGRID; 44275; 1.
DR STRING; 6239.F25G6.3a; -.
DR TCDB; 1.A.9.1.15; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
DR PaxDb; P48180; -.
DR EnsemblMetazoa; F25G6.3.1; F25G6.3.1; WBGene00000055. [P48180-1]
DR GeneID; 179235; -.
DR KEGG; cel:CELE_F25G6.3; -.
DR UCSC; F25G6.3a.1; c. elegans.
DR CTD; 179235; -.
DR WormBase; F25G6.3; CE09639; WBGene00000055; acr-16. [P48180-1]
DR eggNOG; KOG3646; Eukaryota.
DR HOGENOM; CLU_018074_0_3_1; -.
DR InParanoid; P48180; -.
DR OMA; YNARALQ; -.
DR OrthoDB; 845098at2759; -.
DR PhylomeDB; P48180; -.
DR Reactome; R-CEL-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
DR PRO; PR:P48180; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00000055; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IDA:WormBase.
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:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IDA:WormBase.
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:0034220; P:ion transmembrane transport; IDA:WormBase.
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; -; 2.
DR Gene3D; 2.70.170.10; -; 1.
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 InterPro; IPR002394; Nicotinic_acetylcholine_rcpt.
DR PANTHER; PTHR18945; PTHR18945; 1.
DR Pfam; PF02931; Neur_chan_LBD; 1.
DR Pfam; PF02932; Neur_chan_memb; 1.
DR PRINTS; PR00254; NICOTINICR.
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 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; 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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..498
FT /note="Acetylcholine receptor subunit alpha-type acr-16"
FT /id="PRO_0000000395"
FT TOPO_DOM 20..230
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..472
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 147..161
FT /evidence="ECO:0000250"
FT DISULFID 211..212
FT /note="Associated with receptor activation"
FT /evidence="ECO:0000250"
FT VAR_SEQ 470..480
FT /note="VDRLCLYVFTI -> RTYISRKIENF (in isoform b)"
FT /evidence="ECO:0000303|PubMed:8627624"
FT /id="VSP_036472"
SQ SEQUENCE 498 AA; 57169 MW; E463ABB40AC9FA82 CRC64;
MSVCTLLISC AILAAPTLGS LQERRLYEDL MRNYNNLERP VANHSEPVTV HLKVALQQII
DVDEKNQVVY VNAWLDYTWN DYNLVWDKAE YGNITDVRFP AGKIWKPDVL LYNSVDTNFD
STYQTNMIVY STGLVHWVPP GIFKISCKID IQWFPFDEQK CFFKFGSWTY DGYKLDLQPA
TGGFDISEYI SNGEWALPLT TVERNEKFYD CCPEPYPDVH FYLHMRRRTL YYGFNLIMPC
ILTTLMTLLG FTLPPDAGEK ITLQITVLLS ICFFLSIVSE MSPPTSEAVP LLGIFFTCCM
IVVTASTVFT VYVLNLHYRT PETHDMGPWT RNLLLYWIPW ILRMKRPGHN LTYASLPSLF
STKPNRHSES LIRNIKDNEH SLSRANSFDA DCRLNQYIMT QSVSNGLTSL GSIPSTMISS
NGTTTDVSQQ ATLLILHRIY HELKIVTKRM IEGDKEEQAC NNWKFAAMVV DRLCLYVFTI
FIIVSTIGIF WSAPYLVA
