ID ACR7_CAEEL Reviewed; 538 AA. AC P45963; Q9GQV0; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 27-MAY-2002, sequence version 2. DT 02-SEP-2026, entry version 169. DE RecName: Full=Acetylcholine receptor subunit alpha-type acr-7; DE Flags: Precursor; GN Name=acr-7; ORFNames=T09A5.3; 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]. RC STRAIN=Bristol N2; RX PubMed=10100329; RA Mongan N.P., Baylis H.A., Adcock C., Smith G.R., Sansom M.S.P., RA Sattelle D.B.; RT "An extensive and diverse gene family of nicotinic acetylcholine receptor RT alpha subunits in Caenorhabditis elegans."; RL Recept. Channels 6:213-228(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-101, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC STRAIN=Bristol N2; RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200; RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., RA Taoka M., Takahashi N., Isobe T.; RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis RT elegans and suggests an atypical translocation mechanism for integral RT membrane proteins."; RL Mol. Cell. Proteomics 6:2100-2109(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. CC {ECO:0000250}. CC -!- SUBUNIT: Forms a homooligomeric channel blocked by alpha-bungarotoxin. CC The structure is probably pentameric (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. Cell membrane {ECO:0000305}; CC Multi-pass membrane protein {ECO:0000305}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF187012; AAG35182.1; -; mRNA. DR EMBL; Z36753; CAA85338.2; -; Genomic_DNA. DR PIR; T24724; T24724. DR RefSeq; NP_495647.1; NM_063246.5. DR AlphaFoldDB; P45963; -. DR SMR; P45963; -. DR FunCoup; P45963; 57. DR STRING; 6239.T09A5.3.1; -. DR GlyCosmos; P45963; 2 sites, No reported glycans. DR iPTMnet; P45963; -. DR PaxDb; 6239-T09A5.3.1; -. DR EnsemblMetazoa; T09A5.3.1; T09A5.3.1; WBGene00000046. DR GeneID; 174262; -. DR KEGG; cel:CELE_T09A5.3; -. DR UCSC; T09A5.3; c. elegans. DR AGR; WB:WBGene00000046; -. DR CTD; 174262; -. DR WormBase; T09A5.3; CE28078; WBGene00000046; acr-7. DR eggNOG; KOG3646; Eukaryota. DR HOGENOM; CLU_018074_0_3_1; -. DR InParanoid; P45963; -. DR OMA; DGVINWI; -. DR OrthoDB; 5975154at2759; -. DR PhylomeDB; P45963; -. DR Reactome; R-CEL-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors. DR PRO; PR:P45963; -. DR Proteomes; UP000001940; Chromosome II. DR Bgee; WBGene00000046; Expressed in pharyngeal muscle cell (C elegans) and 3 other cell types or tissues. DR GO; GO:0005892; C:acetylcholine-gated channel complex; IBA:GO_Central. DR GO; GO:0043005; C:neuron projection; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; 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:0005230; F:extracellular ligand-gated monoatomic ion channel activity; IEA:InterPro. 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:0006816; P:calcium ion transport; IBA:GO_Central. DR GO; GO:0060079; P:excitatory postsynaptic potential; IEA:GOC. DR GO; GO:0034220; P:monoatomic ion transmembrane transport; IBA:GO_Central. DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central. DR GO; GO:0007271; P:synaptic transmission, cholinergic; IBA:GO_Central. DR CDD; cd18997; LGIC_ECD_nAChR; 1. DR CDD; cd19051; LGIC_TM_cation; 1. DR FunFam; 2.70.170.10:FF:000016; Nicotinic acetylcholine receptor subunit; 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; 2. 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 NCBIfam; TIGR00860; LIC; 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; 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; Disulfide bond; Glycoprotein; Ion channel; Ion transport; KW Ligand-gated ion channel; Membrane; Postsynaptic cell membrane; Receptor; KW Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix; KW Transport. FT SIGNAL 1..27 FT /evidence="ECO:0000255" FT CHAIN 28..538 FT /note="Acetylcholine receptor subunit alpha-type acr-7" FT /id="PRO_0000000400" FT TOPO_DOM 28..250 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 251..271 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 280..300 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 313..333 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 334..513 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 514..534 FT /note="Helical" FT /evidence="ECO:0000255" FT CARBOHYD 41 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 101 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:17761667" FT DISULFID 160..174 FT /evidence="ECO:0000250" FT DISULFID 229..230 FT /note="Associated with receptor activation" FT /evidence="ECO:0000250" SQ SEQUENCE 538 AA; 62823 MW; A33C6514FF64F56C CRC64; MMVQSIQIVL PVALFFLIVF NGFTVEGSKK EAQLYRDLLT NYSYLVRPVR NPKKALTVTM KVFIQQVLLV DAKHQMIEVN AWLKYIWTDF RLRWNPLDYE NITSVRFQGE DQIWQPDILL YNRYIEDEQE SFDITYKTNA VAYSDGVINW IPPGIFKLSC KMDITLFPFD EQICFMKFGS WTYHGFALDL RLDVVKGQEP SADLSTYITN GEWHLLSAPA RREEKFYKCC KEPYPTVKFY LHLRRRTFYY VFNVVLPTLL VSFMSLLAFC LPATDLSEKI GLQTTILLSV CFFLTILSEM TPTTSEAVPL LGVFFSALTF IVAMSTTFTI LVLNIRYRQI TNHYLSPMFR SIFLECLPWL MMMKRPDHKF RRGSSYRDSS ADQCVQCAKN AELKSILRGT DNQQQIETNT FYPFPTETLS LNRKVGDGLF IQRRCQIHEE ARSEKFTHGM LACEKSLREN GSELANILVT ILKMYEVMVS QVERIRKRIA LKRKRKDIQD EWKFAAQAVD RFCLIIFTIV FIICCFIFVA IPPIKILD //