ID   ACHN2_CARAU             Reviewed;         462 AA.
AC   P13908;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Neuronal acetylcholine receptor subunit non-alpha-2;
DE   AltName: Full=GFN-alpha-2;
DE   Flags: Precursor;
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=2465296; DOI=10.1083/jcb.108.2.637;
RA   Cauley K., Agranoff B.W., Goldman D.;
RT   "Identification of a novel nicotinic acetylcholine receptor structural
RT   subunit expressed in goldfish retina.";
RL   J. Cell Biol. 108:637-645(1989).
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 beta.
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC       protein. Cell membrane; Multi-pass membrane protein.
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; X14786; CAA32888.1; -; mRNA.
DR   PIR; S06893; S06893.
DR   AlphaFoldDB; P13908; -.
DR   SMR; P13908; -.
DR   Ensembl; ENSCART00000082105; ENSCARP00000076292; ENSCARG00000035457.
DR   Proteomes; UP000515129; Genome assembly.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IEA:InterPro.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
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; 2.
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..30
FT   CHAIN           31..462
FT                   /note="Neuronal acetylcholine receptor subunit non-alpha-2"
FT                   /id="PRO_0000000393"
FT   TOPO_DOM        31..234
FT                   /note="Extracellular"
FT   TRANSMEM        235..259
FT                   /note="Helical"
FT   TRANSMEM        267..284
FT                   /note="Helical"
FT   TRANSMEM        301..322
FT                   /note="Helical"
FT   TOPO_DOM        323..428
FT                   /note="Cytoplasmic"
FT   TRANSMEM        429..446
FT                   /note="Helical"
FT   REGION          362..384
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        362..378
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        168
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        155..169
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   462 AA;  53195 MW;  306DBDD9E683F3F6 CRC64;
     MTLAVIGLFT LFTSIIAITP AREFVSLAER EDALLRELFQ GYQRWVRPVQ HANHSVKVRF
     GLKISQLVDV DEKNQLMTTN VWLWQEWLDY KLRWNPENYG GITSIRVPSE SIWLPDIVLY
     ENADGRFEGS LMTKAIVRYN GMITWTPPAS YKSACTMDVT FFPFDRQNCS MKFGSWTYDG
     NMVKLVLINQ QVDRSDFFDN GEWEILSATG VKGSRQDSHL SYPYITYSFI LKRLPLFYTL
     FLIIPCLGLS FLTVLVFYLP SDEGEKVSLS TSVLVSLTVF LLVIEEIIPS SSKVIPLIGE
     YLLFIMIFVT LSIIVTIFVI NVHHRSSATY HPMSPWVRSL FLQRLPHLLC MRGNTDRYHY
     PELEPHSPDL KPRNKKGPPG PEGEGQALIN LLEQATNSVR YISRHIKKEH FIREVVQDWK
     FVAQVLDRIF LWTFLTVSVL GTILIFTPAL KMFLRTPPPP SP