ID   ACH8_CAEBR              Reviewed;         481 AA.
AC   Q60S81; A8XZ53;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 3.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Neuronal acetylcholine receptor subunit eat-2;
DE   Flags: Precursor;
GN   Name=eat-2 {ECO:0000250|UniProtKB:Q9U298}; ORFNames=CBG21000;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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       Nicotinic acetylcholine receptor in the MC pharyngeal motor neuron
CC       involved in pharyngeal pumping. Has a role in the determination of life
CC       span possibly via calorific restriction which affects growth rate,
CC       although this is independent of metabolic activity (By similarity).
CC       {ECO:0000250|UniProtKB:P22770, ECO:0000250|UniProtKB:Q9U298}.
CC   -!- SUBUNIT: Neuronal AChR seems to be composed of two different type of
CC       subunits: alpha and beta. {ECO:0000250|UniProtKB:P22770}.
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250}; Multi-
CC       pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}. Note=MC motor neuron.
CC       {ECO:0000250|UniProtKB:Q9U298}.
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; HE600928; CAP37920.1; -; Genomic_DNA.
DR   RefSeq; XP_002631787.1; XM_002631741.1.
DR   AlphaFoldDB; Q60S81; -.
DR   SMR; Q60S81; -.
DR   STRING; 6238.CBG21000; -.
DR   EnsemblMetazoa; CBG21000.1; CBG21000.1; WBGene00039891.
DR   GeneID; 8573786; -.
DR   KEGG; cbr:CBG_21000; -.
DR   CTD; 8573786; -.
DR   WormBase; CBG21000; CBP37967; WBGene00039891; Cbr-eat-2.
DR   eggNOG; KOG3646; Eukaryota.
DR   HOGENOM; CLU_018074_1_0_1; -.
DR   InParanoid; Q60S81; -.
DR   OrthoDB; 845098at2759; -.
DR   Proteomes; UP000008549; Chromosome II.
DR   GO; GO:0005892; C:acetylcholine-gated channel complex; ISS:UniProtKB.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
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; ISS:UniProtKB.
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:0008340; P:determination of adult lifespan; ISS:UniProtKB.
DR   GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0048609; P:multicellular organismal reproductive process; ISS:UniProtKB.
DR   GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR   GO; GO:0007274; P:neuromuscular synaptic transmission; ISS:UniProtKB.
DR   GO; GO:0043050; P:pharyngeal pumping; ISS:UniProtKB.
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   3: Inferred from homology;
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..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..481
FT                   /note="Neuronal acetylcholine receptor subunit eat-2"
FT                   /id="PRO_0000306252"
FT   TOPO_DOM        20..235
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        236..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        264..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        292..312
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        313..443
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        444..464
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          356..384
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        93
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        147..161
FT                   /evidence="ECO:0000250|UniProtKB:P22770"
SQ   SEQUENCE   481 AA;  56046 MW;  BA266277A5DE975D CRC64;
     MFLLLQILYI LLFLNLADTS DDEYRLLKDL REGYDPMERP VSDHMKPVNV KLRLILQQLV
     DVDEKNQVIT LVVWTQYTWN DYKMKWSPEE YGNITSLQIP FGTLWKPDIL LFNSANEHFD
     SSFPVNMVVS NDGNVLFAPP GIMQFSCSLS MTWFPYDEQV CYLKFGSWTY GKKLDLRIDD
     ADLPEGHKMD LQYYVPNGEF DLISTPAFRK STTFLDETYV ELYFHMHLKR RTMYYGLNWI
     IPSILISLSN ILGFTMPVEC GEKVTLQITN FLSIMVFLAM VSEVAPPTSE SIPIIAAFFS
     FAIVILGVSI CVSLITVNIF YRHPKMHRMG DWTRYIFLEW LPWFLLMSRP DHVFRKPKRE
     KKKEEEEDEE SNAGGKEEES ELISQKQQRP RLLVNSQIVM DSTIPYLEEV IGYLKVFKAK
     LDDDEEEEEE ILNWRFMAMV IDRASLFLFT GLIFGTTFVI FAACPNLFSA DQIIETEPVI
     T