ACR7_CAEEL
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 03-AUG-2022, entry version 153.
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}.
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DR EMBL; AF187012; AAG35182.1; -; mRNA.
DR EMBL; Z36753; CAA85338.2; -; Genomic_DNA.
DR PIR; T24724; T24724.
DR RefSeq; NP_495647.1; NM_063246.4.
DR AlphaFoldDB; P45963; -.
DR SMR; P45963; -.
DR STRING; 6239.T09A5.3; -.
DR iPTMnet; P45963; -.
DR PaxDb; P45963; -.
DR PRIDE; P45963; -.
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 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; 845098at2759; -.
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 tissues.
DR GO; GO:0070161; C:anchoring junction; 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:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
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; 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; -; 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 PANTHER; PTHR18945; PTHR18945; 1.
DR Pfam; PF02931; Neur_chan_LBD; 1.
DR Pfam; PF02932; Neur_chan_memb; 1.
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; 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
