ACH4_DROME
ID ACH4_DROME Reviewed; 519 AA.
AC P25162; O18403; Q8IMW6; Q8SXP7; Q9VC71;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 3.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Acetylcholine receptor subunit beta-like 2;
DE AltName: Full=Nicotinic acetylcholine receptor beta 2;
DE Flags: Precursor;
GN Name=nAChRbeta2; Synonyms=Acr96Ac, AcrF, nAcRbeta-96, SBD; ORFNames=CG6798;
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] OF 20-519 (ISOFORM A), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S; TISSUE=Embryo;
RX PubMed=2121539; DOI=10.1016/0014-5793(90)81078-3;
RA Sawruk E., Udri C., Betz H., Schmitt B.;
RT "SBD, a novel structural subunit of the Drosophila nicotinic acetylcholine
RT receptor, shares its genomic localization with two alpha-subunits.";
RL FEBS Lett. 273:177-181(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-65.
RX PubMed=9109505; DOI=10.1046/j.1471-4159.1997.68051812.x;
RA Lansdell S.J., Schmitt B., Betz H., Sattelle D.B., Millar N.S.;
RT "Temperature-sensitive expression of Drosophila neuronal nicotinic
RT acetylcholine receptors.";
RL J. Neurochem. 68:1812-1819(1997).
RN [3]
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 [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP RNA EDITING OF POSITION 278.
RX PubMed=12907802; DOI=10.1126/science.1086763;
RA Hoopengardner B., Bhalla T., Staber C., Reenan R.;
RT "Nervous system targets of RNA editing identified by comparative
RT genomics.";
RL Science 301:832-836(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 {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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=P25162-1; Sequence=Displayed;
CC Name=B;
CC IsoId=P25162-2; Sequence=VSP_007411, VSP_007412;
CC -!- TISSUE SPECIFICITY: CNS in embryos. {ECO:0000269|PubMed:2121539}.
CC -!- DEVELOPMENTAL STAGE: Late embryonic and late pupal stages.
CC {ECO:0000269|PubMed:2121539}.
CC -!- RNA EDITING: Modified_positions=278 {ECO:0000269|PubMed:12907802};
CC Note=Partially edited.;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL90236.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X55676; CAA39211.1; -; mRNA.
DR EMBL; Y14678; CAA74994.1; -; mRNA.
DR EMBL; AE014297; AAF56304.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13998.1; -; Genomic_DNA.
DR EMBL; AY089498; AAL90236.1; ALT_FRAME; mRNA.
DR PIR; S12899; S12899.
DR RefSeq; NP_524483.1; NM_079759.4. [P25162-1]
DR RefSeq; NP_733002.1; NM_170147.3. [P25162-2]
DR AlphaFoldDB; P25162; -.
DR SMR; P25162; -.
DR BioGRID; 67846; 1.
DR STRING; 7227.FBpp0084061; -.
DR BindingDB; P25162; -.
DR ChEMBL; CHEMBL2366470; -.
DR DrugCentral; P25162; -.
DR GlyGen; P25162; 1 site.
DR PaxDb; P25162; -.
DR PRIDE; P25162; -.
DR EnsemblMetazoa; FBtr0084681; FBpp0084061; FBgn0004118. [P25162-1]
DR EnsemblMetazoa; FBtr0084682; FBpp0084062; FBgn0004118. [P25162-2]
DR GeneID; 42920; -.
DR KEGG; dme:Dmel_CG6798; -.
DR CTD; 42920; -.
DR FlyBase; FBgn0004118; nAChRbeta2.
DR VEuPathDB; VectorBase:FBgn0004118; -.
DR eggNOG; KOG3645; Eukaryota.
DR GeneTree; ENSGT00940000173136; -.
DR HOGENOM; CLU_018074_1_0_1; -.
DR InParanoid; P25162; -.
DR OMA; IWITVCV; -.
DR PhylomeDB; P25162; -.
DR Reactome; R-DME-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
DR BioGRID-ORCS; 42920; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 42920; -.
DR PRO; PR:P25162; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0004118; Expressed in brain and 8 other tissues.
DR ExpressionAtlas; P25162; baseline and differential.
DR Genevisible; P25162; 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; IEA:UniProtKB-SubCell.
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: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; 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 Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Ion channel; Ion transport; Ligand-gated ion channel; Membrane;
KW Postsynaptic cell membrane; Receptor; Reference proteome; RNA editing;
KW Signal; Synapse; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..519
FT /note="Acetylcholine receptor subunit beta-like 2"
FT /id="PRO_0000000302"
FT TOPO_DOM 19..244
FT /note="Extracellular"
FT TRANSMEM 245..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..462
FT /note="Cytoplasmic"
FT TRANSMEM 463..481
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 154..168
FT /evidence="ECO:0000250"
FT VAR_SEQ 279..304
FT /note="LCISILVSLTVFFLLLAEIIPPTSLA -> KMDPPNSMIKNLRVIPSFLWHV
FT ACFC (in isoform B)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_007411"
FT VAR_SEQ 305..519
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_007412"
FT VARIANT 278
FT /note="T -> A (in RNA edited version)"
FT CONFLICT 344
FT /note="P -> R (in Ref. 1; CAA39211)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 519 AA; 60140 MW; DDE67674529D2FCB CRC64;
MWHWSLLCVF LLVPLANSTA PISFEANPDT KRLYDDLLSN YNRLIRPVVN NTETLTVWLG
LKLSQLIEVN LKNQVMTTNL WVKQRWFDYK LRWDPEEYGG VEQLYVPSEH IWVPDIVLYN
NWDGNYEVTL MTKATLKYTG EVFWEPPAIY KSSCEMNVEY FPYDEQICFM KFGSWTYNGA
QVDLKHLDQI PGSNLVQVGI DLTEFYLSVE WDILEVPATK NEEYYPDTLE PFSDITFKLT
MRRKTLFYTV NLIVPCVALT FLTVLVFYLP SDSGEKVTLC ISILVSLTVF FLLLAEIIPP
TSLAVPLLGK YLLFTMILVS LSVWTTVCVL NIHFRSPSTH NMSPLVRKLF LHFMPKLMMM
RRTQYTLPDY DDSTPSNGYT NEIDVRDSIS DFPSEFKDSQ DGAYDNGMQN SVDSDNVIPR
NLTPEVLQAL RAVRFIAQHI KDADKDNEIV EDWKFVSMVL DRFFLWLFTL SCVFGTLAII
CQSPSLYDTR SPIDRQLSEI PLRKNNFMLP PDIVRQVLT
