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ACH1_DROME
ID   ACH1_DROME              Reviewed;         567 AA.
AC   P09478; Q9VC74;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   09-MAY-2003, sequence version 2.
DT   03-AUG-2022, entry version 191.
DE   RecName: Full=Acetylcholine receptor subunit alpha-like 1;
DE   AltName: Full=Nicotinic acetylcholine receptor alpha 1;
DE   Flags: Precursor;
GN   Name=nAChRalpha1; Synonyms=Acr96Aa, AcrB, als, nAcRalpha-96Aa;
GN   ORFNames=CG5610;
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.
RC   STRAIN=Oregon-R;
RX   PubMed=2840281; DOI=10.1002/j.1460-2075.1988.tb02854.x;
RA   Bossy B., Ballivet M., Spierer P.;
RT   "Conservation of neural nicotinic acetylcholine receptors from Drosophila
RT   to vertebrate central nervous systems.";
RL   EMBO J. 7:611-618(1988).
RN   [2]
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   [3]
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:2840281}.
CC   -!- DEVELOPMENTAL STAGE: Late embryonic, late pupal and second instar
CC       larvae stages. {ECO:0000269|PubMed:2840281}.
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; X07194; CAA30172.1; -; mRNA.
DR   EMBL; AE014297; AAF56301.2; -; Genomic_DNA.
DR   PIR; S00381; ACFFA1.
DR   RefSeq; NP_001262917.1; NM_001275988.2.
DR   RefSeq; NP_524481.2; NM_079757.4.
DR   AlphaFoldDB; P09478; -.
DR   SMR; P09478; -.
DR   BioGRID; 67844; 1.
DR   STRING; 7227.FBpp0084003; -.
DR   ChEMBL; CHEMBL3350223; -.
DR   GlyGen; P09478; 2 sites.
DR   PaxDb; P09478; -.
DR   PRIDE; P09478; -.
DR   EnsemblMetazoa; FBtr0084619; FBpp0084003; FBgn0000036.
DR   EnsemblMetazoa; FBtr0334916; FBpp0306936; FBgn0000036.
DR   GeneID; 42918; -.
DR   KEGG; dme:Dmel_CG5610; -.
DR   CTD; 42918; -.
DR   FlyBase; FBgn0000036; nAChRalpha1.
DR   VEuPathDB; VectorBase:FBgn0000036; -.
DR   eggNOG; KOG3645; Eukaryota.
DR   GeneTree; ENSGT00940000171907; -.
DR   HOGENOM; CLU_018074_1_0_1; -.
DR   InParanoid; P09478; -.
DR   OMA; QHAKNKD; -.
DR   OrthoDB; 381858at2759; -.
DR   PhylomeDB; P09478; -.
DR   Reactome; R-DME-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
DR   BioGRID-ORCS; 42918; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 42918; -.
DR   PRO; PR:P09478; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0000036; Expressed in central nervous system and 6 other tissues.
DR   ExpressionAtlas; P09478; baseline and differential.
DR   Genevisible; P09478; DM.
DR   GO; GO:0005892; C:acetylcholine-gated channel complex; IDA:FlyBase.
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:0022848; F:acetylcholine-gated cation-selective channel activity; IEA:InterPro.
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:0098655; P:cation transmembrane transport; IDA:FlyBase.
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:0017085; P:response to insecticide; IMP:FlyBase.
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; 2.
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   CHAIN           22..567
FT                   /note="Acetylcholine receptor subunit alpha-like 1"
FT                   /id="PRO_0000000298"
FT   TOPO_DOM        22..240
FT                   /note="Extracellular"
FT   TRANSMEM        241..264
FT                   /note="Helical"
FT   TRANSMEM        272..290
FT                   /note="Helical"
FT   TRANSMEM        306..325
FT                   /note="Helical"
FT   TOPO_DOM        326..513
FT                   /note="Cytoplasmic"
FT   TRANSMEM        514..532
FT                   /note="Helical"
FT   CARBOHYD        45
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        233
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        149..163
FT                   /evidence="ECO:0000250"
FT   DISULFID        222..223
FT                   /note="Associated with receptor activation"
FT                   /evidence="ECO:0000250"
FT   VARIANT         538
FT                   /note="Y -> H"
FT   CONFLICT        108
FT                   /note="L -> H (in Ref. 1; CAA30172)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   567 AA;  64019 MW;  08E1F721FB2A92AC CRC64;
     MGSVLFAAVF IALHFATGGL ANPDAKRLYD DLLSNYNRLI RPVGNNSDRL TVKMGLRLSQ
     LIDVNLKNQI MTTNVWVEQE WNDYKLKWNP DDYGGVDTLH VPSEHIWLPD IVLYNNADGN
     YEVTIMTKAI LHHTGKVVWK PPAIYKSFCE IDVEYFPFDE QTCFMKFGSW TYDGYMVDLR
     HLKQTADSDN IEVGIDLQDY YISVEWDIMR VPAVRNEKFY SCCEEPYLDI VFNLTLRRKT
     LFYTVNLIIP CVGISFLSVL VFYLPSDSGE KISLCISILL SLTVFFLLLA EIIPPTSLTV
     PLLGKYLLFT MMLVTLSVVV TIAVLNVNFR SPVTHRMAPW VQRLFIQILP KLLCIERPKK
     EEPEEDQPPE VLTDVYHLPP DVDKFVNYDS KRFSGDYGIP ALPASHRFDL AAAGGISAHC
     FAEPPLPSSL PLPGADDDLF SPSGLNGDIS PGCCPAAAAA AAADLSPTFE KPYAREMEKT
     IEGSRFIAQH VKNKDKFESV EEDWKYVAMV LDRMFLWIFA IACVVGTALI ILQAPSLYDQ
     SQPIDILYSK IAKKKFELLK MGSENTL
 
 
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