ID   ACR2_CAEEL              Reviewed;         575 AA.
AC   P48182;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   02-SEP-2026, entry version 175.
DE   RecName: Full=Acetylcholine receptor subunit beta-type acr-2;
DE   Flags: Precursor;
GN   Name=acr-2; ORFNames=K11G12.2;
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], FUNCTION, AND INTERACTION WITH NICOTINIC
RP   ACETYLCHOLINE RECEPTOR.
RC   STRAIN=Bristol N2;
RX   PubMed=8581398;
RA   Squire M.D., Tornoe C.A., Baylis H.A., Fleming J.T., Barnard E.A.,
RA   Sattelle D.B.;
RT   "Molecular cloning and functional co-expression of a Caenorhabditis elegans
RT   nicotinic acetylcholine receptor subunit (acr-2).";
RL   Recept. Channels 3:107-115(1995).
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   FUNCTION, INTERACTION WITH NICOTINIC ACETYLCHOLINE RECEPTOR, TISSUE
RP   SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP   VAL-309.
RX   PubMed=20027209; DOI=10.1371/journal.pbio.1000265;
RA   Jospin M., Qi Y.B., Stawicki T.M., Boulin T., Schuske K.R., Horvitz H.R.,
RA   Bessereau J.L., Jorgensen E.M., Jin Y.;
RT   "A neuronal acetylcholine receptor regulates the balance of muscle
RT   excitation and inhibition in Caenorhabditis elegans.";
RL   PLoS Biol. 7:E1000265-E1000265(2009).
RN   [4]
RP   FUNCTION, AND MUTAGENESIS OF VAL-309.
RX   PubMed=23658528; DOI=10.1371/journal.pgen.1003472;
RA   Stawicki T.M., Takayanagi-Kiya S., Zhou K., Jin Y.;
RT   "Neuropeptides function in a homeostatic manner to modulate excitation-
RT   inhibition imbalance in C. elegans.";
RL   PLoS Genet. 9:E1003472-E1003472(2013).
RN   [5]
RP   FUNCTION.
RX   PubMed=27782882; DOI=10.7554/elife.21734;
RA   Takayanagi-Kiya S., Zhou K., Jin Y.;
RT   "Release-dependent feedback inhibition by a presynaptically localized
RT   ligand-gated anion channel.";
RL   Elife 5:21734-21749(2016).
CC   -!- FUNCTION: Non-alpha subunit of nicotinic acetylcholine receptor (nAChR)
CC       (PubMed:20027209, PubMed:8581398). Acts in cholinergic motoneurons to
CC       regulate presynaptic neurotransmitter release, thereby ensuring normal
CC       level of excitation of cholinergic motoneurons during locomotion
CC       (PubMed:20027209, PubMed:23658528, PubMed:27782882).
CC       {ECO:0000269|PubMed:20027209, ECO:0000269|PubMed:23658528,
CC       ECO:0000269|PubMed:8581398}.
CC   -!- SUBUNIT: Component of nicotinic acetylcholine receptor. In cholinergic
CC       motoneurons, composed of 2 non-alpha subunits acr-2 and acr-3, and 3
CC       alpha subunits unc-38, unc-63 and acr-12. {ECO:0000269|PubMed:20027209,
CC       ECO:0000269|PubMed:8581398}.
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC       {ECO:0000250|UniProtKB:Q23022}; Multi-pass membrane protein
CC       {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q23022}; Multi-pass
CC       membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in cholinergic ventral cord
CC       motoneurons of the VA, VB, DA and DB classes but not AS and VC classes.
CC       Expressed in PVQ and DVC neurons in the tail.
CC       {ECO:0000269|PubMed:20027209}.
CC   -!- DEVELOPMENTAL STAGE: Expressed from L1 larval stage through adults.
CC       {ECO:0000269|PubMed:20027209}.
CC   -!- DISRUPTION PHENOTYPE: Locomotion is slower. Moderately resistant to
CC       paralysis induced by acetylcholine esterase inhibitor aldicarb but
CC       sensitivity to acetylcholine agonist levamisole is normal. Reduced both
CC       cholinergic and GABAergic motoneuron activities characterized by a
CC       reduction in miniature postsynaptic currents in muscles.
CC       {ECO:0000269|PubMed:20027209}.
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; X86403; CAA60157.1; -; mRNA.
DR   EMBL; FO081325; CCD70794.1; -; Genomic_DNA.
DR   PIR; S57648; S57648.
DR   RefSeq; NP_509128.1; NM_076727.9.
DR   AlphaFoldDB; P48182; -.
DR   SMR; P48182; -.
DR   FunCoup; P48182; 49.
DR   STRING; 6239.K11G12.2.1; -.
DR   TCDB; 1.A.9.1.13; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
DR   TCDB; 1.A.9.1.2; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
DR   GlyCosmos; P48182; 4 sites, No reported glycans.
DR   PaxDb; 6239-K11G12.2.1; -.
DR   EnsemblMetazoa; K11G12.2.1; K11G12.2.1; WBGene00000042.
DR   GeneID; 180936; -.
DR   KEGG; cel:CELE_K11G12.2; -.
DR   UCSC; K11G12.2; c. elegans.
DR   AGR; WB:WBGene00000042; -.
DR   CTD; 180936; -.
DR   WormBase; K11G12.2; CE07380; WBGene00000042; acr-2.
DR   eggNOG; KOG3645; Eukaryota.
DR   HOGENOM; CLU_018074_1_0_1; -.
DR   InParanoid; P48182; -.
DR   OMA; SHKMPTW; -.
DR   OrthoDB; 5975154at2759; -.
DR   PhylomeDB; P48182; -.
DR   Reactome; R-CEL-629587; Highly sodium permeable postsynaptic acetylcholine nicotinic receptors.
DR   Reactome; R-CEL-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
DR   Reactome; R-CEL-629597; Highly calcium permeable nicotinic acetylcholine receptors.
DR   Reactome; R-CEL-6798695; Neutrophil degranulation.
DR   PRO; PR:P48182; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00000042; Expressed in larva 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; IDA:WormBase.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
DR   GO; GO:0022848; F:acetylcholine-gated monoatomic cation-selective channel activity; IDA:WormBase.
DR   GO; GO:0005231; F:excitatory extracellular ligand-gated monoatomic ion channel activity; IDA:WormBase.
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:0098703; P:calcium ion import across plasma membrane; IDA:WormBase.
DR   GO; GO:0006816; P:calcium ion transport; IBA:GO_Central.
DR   GO; GO:0034220; P:monoatomic ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:UniProtKB.
DR   GO; GO:0045727; P:positive regulation of translation; IDA:UniProtKB.
DR   GO; GO:0010468; P:regulation of gene expression; IMP:UniProtKB.
DR   GO; GO:0040012; P:regulation of locomotion; IMP:UniProtKB.
DR   GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR   GO; GO:0006937; P:regulation of muscle contraction; IMP:UniProtKB.
DR   GO; GO:0007271; P:synaptic transmission, cholinergic; IBA:GO_Central.
DR   GO; GO:0055085; P:transmembrane transport; IDA:WormBase.
DR   CDD; cd19032; LGIC_ECD_nAChR_proto_beta-like; 1.
DR   CDD; cd19064; LGIC_TM_nAChR; 1.
DR   FunFam; 1.20.58.390:FF:000035; Acetylcholine receptor subunit beta-like 1; 1.
DR   FunFam; 2.70.170.10:FF:000023; Acetylcholine receptor subunit beta-like 1; 1.
DR   FunFam; 1.20.58.390:FF:000086; Acetylcholine receptor subunit beta-type acr-2; 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   InterPro; IPR002394; Nicotinic_acetylcholine_rcpt.
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; PR00254; NICOTINICR.
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..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..575
FT                   /note="Acetylcholine receptor subunit beta-type acr-2"
FT                   /id="PRO_0000000398"
FT   TOPO_DOM        21..270
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        271..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        299..319
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        331..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        352..527
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        528..548
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          31..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..50
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        41
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        42
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        131
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        185..199
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         309
FT                   /note="V->M: In n2420; constitutively active. Spontaneous
FT                   convulsions and shrinking behavior in response to touch.
FT                   Convulsions are suppressed in an unc-74, unc-50, unc-38 or
FT                   unc-63 mutant background. Enhanced neurotransmitter release
FT                   by cholinergic motoneurons and reduced neurotransmitter
FT                   release by GABAergic motoneurons. Increases neuropeptide
FT                   flp-18 expression in cholinergic B-type motor neurons.
FT                   Increases sensitivity to paralysis induced by acetylcholine
FT                   esterase inhibitor aldicarb or acetylcholine agonist
FT                   levamisole in L3-L4 larvae and adults."
FT                   /evidence="ECO:0000269|PubMed:20027209,
FT                   ECO:0000269|PubMed:23658528"
SQ   SEQUENCE   575 AA;  65595 MW;  7EB24296100EEB05 CRC64;
     MKKTVKILLI LITVFLKVHC NGGHDDEAAD FLSHTNIDDP NNSSDPNKNS DQGDTMGEDE
     DRLVIDLFRE YNFLIRPVKN VSSPPVVVDF GVAMILLINV DEKNQILQTN VWLTMKWNDF
     QLAWNPAEYG NISNLHVPSD RVWLPDIVLF NNADGNYEVS FKSNVFVDHH GDVTWVPPAM
     FKSSCRIDVE WFPFDEQCCT LVFGSWTYNS EEVRLHWYNN IQAVQLHDYS YSGIWDVIDV
     PGQLVHKPDL KENKMVFNVV IRRKTLFYTV ILIIPTVLMA FLSVMAFYLP VDSGEKVSLT
     ISLLLALVVF LLLVSKILPP TSNIPLMGKY LLLAFVLNIT AVVGTVVIVN IYFRSALSHK
     MPTWVRKVFL EFLPHLLVMK RPERIPIFNG YFVEEYCASE IFDASLVMPS MTATMLPFLQ
     VTTNLKAASS TSSGQSSEHH ENCSKWKKRL SIRMSKRRAP RARLDDDSED IIDDTNGNHV
     DSLQEKISKE MKTTVEAIAY IAEHMKREMS LKKMRDDWKY VAMVLDRLIL LIFFGVTLGG
     TLGIICSAPH VFDFVDQEAI ISKLNAKYLP SDMYS
//