ACH3_DROME
ID ACH3_DROME Reviewed; 521 AA.
AC P04755; Q9VZC3;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Acetylcholine receptor subunit beta-like 1;
DE AltName: Full=Nicotinic acetylcholine receptor beta 1;
DE Flags: Precursor;
GN Name=nAChRbeta1; Synonyms=Acr64B, AcrD, ard, nAcRbeta-64B;
GN ORFNames=CG11348;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16453690; DOI=10.1002/j.1460-2075.1986.tb04389.x;
RA Hermans-Borgmeyer I., Zopf D., Ryseck R.-P., Hovemann B., Betz H.,
RA Gundelfinger E.D.;
RT "Primary structure of a developmentally regulated nicotinic acetylcholine
RT receptor protein from Drosophila.";
RL EMBO J. 5:1503-1508(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3136037; DOI=10.1016/0014-5793(88)81230-4;
RA Sawruk E., Hermans-Borgmeyer I., Betz H., Gundelfinger E.D.;
RT "Characterization of an invertebrate nicotinic acetylcholine receptor gene:
RT the ard gene of Drosophila melanogaster.";
RL FEBS Lett. 235:40-46(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2832736; DOI=10.1128/mcb.8.2.778-785.1988;
RA Wadsworth S.C., Rosenthal L.S., Kammermeyer K.L., Potter M.B., Nelson D.J.;
RT "Expression of a Drosophila melanogaster acetylcholine receptor-related
RT gene in the central nervous system.";
RL Mol. Cell. Biol. 8:778-785(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
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 -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC protein. Cell membrane {ECO:0000250}; Multi-pass membrane protein
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: CNS in embryos. {ECO:0000269|PubMed:16453690}.
CC -!- DEVELOPMENTAL STAGE: Late embryonic and late pupal stages.
CC {ECO:0000269|PubMed:16453690}.
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; X04016; CAA27641.1; -; mRNA.
DR EMBL; X07956; CAA30778.1; -; Genomic_DNA.
DR EMBL; X07957; CAA30778.1; JOINED; Genomic_DNA.
DR EMBL; X07958; CAA30778.1; JOINED; Genomic_DNA.
DR EMBL; M20316; AAA28311.1; -; mRNA.
DR EMBL; AE014296; AAF47900.1; -; Genomic_DNA.
DR PIR; S03012; ACFFNN.
DR RefSeq; NP_523927.2; NM_079203.3.
DR AlphaFoldDB; P04755; -.
DR SMR; P04755; -.
DR BioGRID; 64020; 1.
DR STRING; 7227.FBpp0073155; -.
DR ChEMBL; CHEMBL3350223; -.
DR GlyGen; P04755; 1 site.
DR PaxDb; P04755; -.
DR DNASU; 38545; -.
DR GeneID; 38545; -.
DR KEGG; dme:Dmel_CG11348; -.
DR CTD; 38545; -.
DR FlyBase; FBgn0000038; nAChRbeta1.
DR VEuPathDB; VectorBase:FBgn0000038; -.
DR eggNOG; KOG3645; Eukaryota.
DR HOGENOM; CLU_018074_1_0_1; -.
DR InParanoid; P04755; -.
DR PhylomeDB; P04755; -.
DR Reactome; R-DME-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
DR BioGRID-ORCS; 38545; 0 hits in 3 CRISPR screens.
DR ChiTaRS; nAChRbeta1; fly.
DR GenomeRNAi; 38545; -.
DR PRO; PR:P04755; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR ExpressionAtlas; P04755; baseline and differential.
DR Genevisible; P04755; DM.
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; IDA:FlyBase.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; 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 GO; GO:0007271; P:synaptic transmission, cholinergic; IEP:FlyBase.
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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..521
FT /note="Acetylcholine receptor subunit beta-like 1"
FT /id="PRO_0000000301"
FT TOPO_DOM 25..235
FT /note="Extracellular"
FT TRANSMEM 236..260
FT /note="Helical"
FT TRANSMEM 268..286
FT /note="Helical"
FT TRANSMEM 302..323
FT /note="Helical"
FT TOPO_DOM 324..481
FT /note="Cytoplasmic"
FT TRANSMEM 482..500
FT /note="Helical"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 152..166
FT /evidence="ECO:0000250"
FT VARIANT 73
FT /note="V -> I"
FT CONFLICT 383..384
FT /note="EL -> DV (in Ref. 3; AAA28311)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 521 AA; 59902 MW; FF9BA2ABC0C3AA62 CRC64;
MESSCKSWLL CSILVLVAFS LVSASEDEER LVRDLFRGYN KLIRPVQNMT QKVGVRFGLA
FVQLINVNEK NQVMKSNVWL RLVWYDYQLQ WDEADYGGIG VLRLPPDKVW KPDIVLFNNA
DGNYEVRYKS NVLIYPTGEV LWVPPAIYQS SCTIDVTYFP FDQQTCIMKF GSWTFNGDQV
SLALYNNKNF VDLSDYWKSG TWDIIEVPAY LNVYEGDSNH PTETDITFYI IIRRKTLFYT
VNLILPTVLI SFLCVLVFYL PAEAGEKVTL GISILLSLVV FLLLVSKILP PTSLVLPLIA
KYLLFTFIMN TVSILVTVII INWNFRGPRT HRMPMYIRSI FLHYLPAFLF MKRPRKTRLR
WMMEMPGMSM PAHPHPSYGS PAELPKHISA IGGKQSKMEV MELSDLHHPN CKINRKVNSG
GELGLGDGCR RESESSDSIL LSPEASKATE AVEFIAEHLR NEDLYIQTRE DWKYVAMVID
RLQLYIFFIV TTAGTVGILM DAPHIFEYVD QDRIIEIYRG K
