ACH8_CAEEL
ID ACH8_CAEEL Reviewed; 474 AA.
AC Q9U298;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Neuronal acetylcholine receptor subunit eat-2;
DE AltName: Full=Abnormal pharyngeal pumping eat-2;
DE Flags: Precursor;
GN Name=eat-2 {ECO:0000312|WormBase:Y48B6A.4};
GN ORFNames=Y48B6A.4 {ECO:0000312|WormBase:Y48B6A.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:15020415};
RX PubMed=15020415; DOI=10.1534/genetics.166.1.161;
RA McKay J.P., Raizen D.M., Gottschalk A., Schafer W.R., Avery L.;
RT "eat-2 and eat-18 are required for nicotinic neurotransmission in the
RT Caenorhabditis elegans pharynx.";
RL Genetics 166:161-169(2004).
RN [2] {ECO:0000312|EMBL:CAB54450.1}
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] {ECO:0000305}
RP FUNCTION.
RX PubMed=8462849; DOI=10.1093/genetics/133.4.897;
RA Avery L.;
RT "The genetics of feeding in Caenorhabditis elegans.";
RL Genetics 133:897-917(1993).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=8601480; DOI=10.1093/genetics/141.4.1365;
RA Raizen D.M., Lee R.Y.N., Avery L.;
RT "Interacting genes required for pharyngeal excitation by motor neuron MC in
RT Caenorhabditis elegans.";
RL Genetics 141:1365-1382(1995).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=9789046; DOI=10.1073/pnas.95.22.13091;
RA Lakowski B., Hekimi S.;
RT "The genetics of caloric restriction in Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:13091-13096(1998).
RN [6] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15141086; DOI=10.1073/pnas.0400848101;
RA Huang C., Xiong C., Kornfeld K.;
RT "Measurements of age-related changes of physiological processes that
RT predict lifespan of Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:8084-8089(2004).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28853436; DOI=10.1038/ncomms16083;
RA Tiku V., Jain C., Raz Y., Nakamura S., Heestand B., Liu W., Spaeth M.,
RA Suchiman H.E.D., Mueller R.U., Slagboom P.E., Partridge L., Antebi A.;
RT "Small nucleoli are a cellular hallmark of longevity.";
RL Nat. Commun. 8:16083-16083(2016).
RN [8]
RP FUNCTION.
RX PubMed=30965033; DOI=10.1016/j.devcel.2019.03.010;
RA Kumar S., Egan B.M., Kocsisova Z., Schneider D.L., Murphy J.T., Diwan A.,
RA Kornfeld K.;
RT "Lifespan extension in C. elegans caused by bacterial colonization of the
RT intestine and subsequent activation of an innate immune response.";
RL Dev. Cell 49:100-117(2019).
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). Nicotinic acetylcholine receptor in the MC pharyngeal
CC motor neuron involved in pharyngeal pumping (PubMed:15020415,
CC PubMed:8601480). Has a role in the determination of life span possibly
CC via calorific restriction which affects growth rate, although this is
CC independent of metabolic activity (PubMed:8462849, PubMed:9789046,
CC PubMed:15141086, PubMed:28853436, PubMed:30965033). Plays a role in the
CC defense against the accumulation of ingested live pathogenic bacteria
CC in the intestine (PubMed:30965033). {ECO:0000250|UniProtKB:P22770,
CC ECO:0000269|PubMed:15020415, ECO:0000269|PubMed:15141086,
CC ECO:0000269|PubMed:28853436, ECO:0000269|PubMed:30965033,
CC ECO:0000269|PubMed:8462849, ECO:0000269|PubMed:8601480,
CC ECO:0000269|PubMed:9789046}.
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
CC {ECO:0000269|PubMed:15020415}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15020415}. Cell membrane
CC {ECO:0000269|PubMed:15020415}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15020415}. Note=MC motor neuron.
CC {ECO:0000269|PubMed:15020415}.
CC -!- TISSUE SPECIFICITY: Expressed in pharyngeal muscle.
CC {ECO:0000269|PubMed:15020415}.
CC -!- DISRUPTION PHENOTYPE: Worms exhibit a lack of MC neurotransmission
CC possibly explaining the observed reduction in pharyngeal pumping rate
CC (PubMed:15020415). Mutants show differences in their pharyngeal
CC responses to nicotine (PubMed:15020415). A variety of mutants show an
CC increase in lifespan ranging from 29-57% longer than wild-type
CC (PubMed:15141086, PubMed:28853436). Extended self-fertile reproductive
CC span, fast body movement, and a longer pharyngeal pumping span
CC (PubMed:15141086). The strongest allele (ad1113) shows retarded growth
CC (PubMed:15141086). Animals generally have smaller nucleoli
CC (PubMed:28853436). Double knockout with ncl-1 reduces the increased
CC longevity and suppresses the reduced nucleoli size phenotype of the
CC eat-2 single mutant, and reduces the increased ribosomal protein
CC synthesis in the ncl-1 single mutant (e1942) (PubMed:28853436).
CC {ECO:0000269|PubMed:15020415, ECO:0000269|PubMed:15141086,
CC ECO:0000269|PubMed:28853436}.
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; BX284602; CAB54450.1; -; Genomic_DNA.
DR PIR; T27006; T27006.
DR RefSeq; NP_496959.1; NM_064558.3.
DR AlphaFoldDB; Q9U298; -.
DR SMR; Q9U298; -.
DR STRING; 6239.Y48B6A.4; -.
DR TCDB; 1.A.9.1.17; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
DR PaxDb; Q9U298; -.
DR EnsemblMetazoa; Y48B6A.4.1; Y48B6A.4.1; WBGene00001133.
DR GeneID; 175072; -.
DR KEGG; cel:CELE_Y48B6A.4; -.
DR UCSC; Y48B6A.4; c. elegans.
DR CTD; 175072; -.
DR WormBase; Y48B6A.4; CE22119; WBGene00001133; eat-2.
DR eggNOG; KOG3646; Eukaryota.
DR HOGENOM; CLU_018074_1_0_1; -.
DR InParanoid; Q9U298; -.
DR OMA; FNSANEH; -.
DR OrthoDB; 845098at2759; -.
DR PhylomeDB; Q9U298; -.
DR Reactome; R-CEL-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
DR PRO; PR:Q9U298; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00001133; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; IMP:UniProtKB.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0031594; C:neuromuscular junction; IDA:WormBase.
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; IMP: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:0001508; P:action potential; IMP:WormBase.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0030536; P:larval feeding behavior; IMP:UniProtKB.
DR GO; GO:0048609; P:multicellular organismal reproductive process; IMP:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:UniProtKB.
DR GO; GO:0043050; P:pharyngeal pumping; IMP:UniProtKB.
DR GO; GO:1904000; P:positive regulation of eating behavior; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0090326; P:positive regulation of locomotion involved in locomotory behavior; IMP:UniProtKB.
DR GO; GO:0061063; P:positive regulation of nematode larval development; IMP:UniProtKB.
DR GO; GO:0060378; P:regulation of brood size; IMP:UniProtKB.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP:WormBase.
DR GO; GO:0043051; P:regulation of pharyngeal pumping; IMP:WormBase.
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 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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..474
FT /note="Neuronal acetylcholine receptor subunit eat-2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000306253"
FT TOPO_DOM 22..237
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..440
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 359..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 149..163
FT /evidence="ECO:0000250|UniProtKB:P22770"
SQ SEQUENCE 474 AA; 55042 MW; AAAA3786CEAEB02F CRC64;
MTLKIAFFTL ILLVSIERVY SSDEEYRLLK DLREGYDPVE RPVADHRKPV NVKLRLILQQ
LVDVDERNQV ITLVVWNQYT WNDYKLRWSP EEYGNITTLQ IPHGTLWKPD ILLFNSANEH
FDASFPVHMV VSSNGDVLFA PPGIVSFSCS LSMTWFPYDQ QVCYLKFGSW TYGKKLDLQI
DDSDLPDGHK MDLQYYIPNG EFDLLATPAF RKSTTFLDET YVELYFHMHL KRRTMYYGLN
WIVPSILISL SNILGFTMPP ECGEKITLQI TNFLSVMVFL AMVSEVAPPT SESIPIIAAF
FSLSIVILGL SICASLIIVN IFFRHPKTHR MGDWTRYVFL EWLPWFLLMS RPEHTFCRPR
REEEKNDEEA GGDGTKLLEN QQHQPRPRLL VNSQLVMDST VPYLEEIIGY LKVFKAKLDD
DEEEEEEILN WRFMAMVIDR LSLFLFTGLI FGTTALIFAF CPNLFTDSPI VDIE
