ID   ACHA3_CARAU             Reviewed;         512 AA.
AC   P18845;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Neuronal acetylcholine receptor subunit alpha-3;
DE   AltName: Full=GF-alpha-3;
DE   Flags: Precursor;
GN   Name=chrna3;
OS   Carassius auratus (Goldfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Carassius.
OX   NCBI_TaxID=7957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Retina;
RX   PubMed=2402459; DOI=10.1093/nar/18.17.5293;
RA   Hieber V.C., Bouchey J.E., Agranoff B.W., Goldman D.;
RT   "Nucleotide and deduced amino acid sequence of the goldfish neural
RT   nicotinic acetylcholine receptor alpha-3 subunit.";
RL   Nucleic Acids Res. 18:5293-5293(1990).
RN   [2]
RP   TISSUE SPECIFICITY.
RX   PubMed=2303867; DOI=10.1523/jneurosci.10-02-00670.1990;
RA   Cauley K., Agranoff B.W., Goldman D.;
RT   "Multiple nicotinic acetylcholine receptor genes are expressed in goldfish
RT   retina and tectum.";
RL   J. Neurosci. 10:670-683(1990).
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   -!- SUBUNIT: Neuronal AChR seems to be composed of two different type of
CC       subunits: alpha and non-alpha (beta).
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC       protein. Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in retina and brain.
CC       {ECO:0000269|PubMed:2303867}.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC       Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-3/CHRNA3 sub-
CC       subfamily. {ECO:0000305}.
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DR   EMBL; X54051; CAA37985.1; -; mRNA.
DR   PIR; S11230; B37014.
DR   AlphaFoldDB; P18845; -.
DR   SMR; P18845; -.
DR   Ensembl; ENSCART00000041987; ENSCARP00000040207; ENSCARG00000017362.
DR   Proteomes; UP000515129; Genome assembly.
DR   GO; GO:0005892; C:acetylcholine-gated channel complex; ISS:UniProtKB.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015464; F:acetylcholine receptor activity; ISS:UniProtKB.
DR   GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; ISS:UniProtKB.
DR   GO; GO:0035095; P:behavioral response to nicotine; ISS:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; ISS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; ISS:UniProtKB.
DR   GO; GO:0060084; P:synaptic transmission involved in micturition; ISS:UniProtKB.
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..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..512
FT                   /note="Neuronal acetylcholine receptor subunit alpha-3"
FT                   /id="PRO_0000000350"
FT   TOPO_DOM        24..232
FT                   /note="Extracellular"
FT   TRANSMEM        233..257
FT                   /note="Helical"
FT   TRANSMEM        265..283
FT                   /note="Helical"
FT   TRANSMEM        299..320
FT                   /note="Helical"
FT   TOPO_DOM        321..485
FT                   /note="Cytoplasmic"
FT   TRANSMEM        486..505
FT                   /note="Helical"
FT   REGION          356..389
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        47
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        164
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        151..165
FT                   /evidence="ECO:0000250"
FT   DISULFID        215..216
FT                   /note="Associated with receptor activation"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   512 AA;  58096 MW;  8D2F63E37ECE9077 CRC64;
     MNSASRITLF FLLTVLITQE CLSSKGEDRL FRRLFRRYNQ FIRPVENVSD PVTVEFEVSI
     SQLVKVDEVN QIMETNLWLR HIWNDYKLKW LPAEFDGIEF IRVPSNKIWR PDIVLYNNAV
     GDFLVEDKTK ALLKYDGTIT WVPPAIFKSS CPMDITYFPF DYQNCSMKFG SWTYDKAKID
     LVLIGSKVNL KDFWESGEWE IIDAPGYKHD IKYNCCEEIY PDITYSFYIR RLPLFYTINL
     IIPCLLISFL TILVFYLPSD CGEKVTLCIS VLLSLTVFLL VITETIPSTS LVIPLIGEYL
     LFTMIFVTLS IVITVFVLNV HYRTPMTHTM PSWVRTVFLR ALPRVMLMRR PIDLSESSGK
     GGGEIAGSSG TGGGRGAEGK KMKSSASQQG AMNSLEFGEG KAALEGKKGG CPCHPIKEAI
     EGDCGKVSRQ LTPQAINTVV TFSVVSPEIK QAIESVKYIA ENMRSRNKAK EVEDDWKYVA
     MVIDRIFLWV FVLVCVLGTL GLFLQPLIGF FS