ID   ACH91_ONCMY             Reviewed;         572 AA.
AC   Q8JFN7;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Neuronal acetylcholine receptor subunit alpha-9-I;
DE   AltName: Full=Nicotinic acetylcholine receptor subunit alpha-9-I;
DE            Short=NACHR alpha-9-I;
DE   Flags: Precursor;
GN   Name=nachra9;
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Saccule;
RX   PubMed=15283971; DOI=10.1016/j.neuroscience.2004.05.037;
RA   Drescher D.G., Ramakrishnan N.A., Drescher M.J., Chun W., Wang X.,
RA   Myers S.F., Green G.E., Sadrazodi K., Karadaghy A.A., Poopat N.,
RA   Karpenko A.N., Khan K.M., Hatfield J.S.;
RT   "Cloning and characterization of alpha9 subunits of the nicotinic
RT   acetylcholine receptor expressed by saccular hair cells of the rainbow
RT   trout (Oncorhynchus mykiss).";
RL   Neuroscience 127:737-752(2004).
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000305}; Multi-
CC       pass membrane protein {ECO:0000305}. Cell membrane {ECO:0000305};
CC       Multi-pass membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in the liver, olfactory mucosa, pituitary
CC       gland, hair cells of the saccule and spleen.
CC       {ECO:0000269|PubMed:15283971}.
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; AY037940; AAK72491.1; -; mRNA.
DR   RefSeq; NP_001117911.1; NM_001124439.1.
DR   AlphaFoldDB; Q8JFN7; -.
DR   SMR; Q8JFN7; -.
DR   GeneID; 100136152; -.
DR   KEGG; omy:100136152; -.
DR   CTD; 662452; -.
DR   OrthoDB; 845098at2759; -.
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; 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   Signal; Synapse; Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..572
FT                   /note="Neuronal acetylcholine receptor subunit alpha-9-I"
FT                   /id="PRO_0000000374"
FT   TOPO_DOM        20..232
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        233..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        263..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        297..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        318..550
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        551..571
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          405..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..438
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        51
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        149..163
FT                   /evidence="ECO:0000250"
FT   DISULFID        213..214
FT                   /note="Associated with receptor activation"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   572 AA;  65590 MW;  EB27F30AC97AA352 CRC64;
     MKTVVLLTWI SCWIDVCTSA QGRYAQKLLN DLMENYSSAL RPVEDTDKTL NVTLQITLSQ
     IKDMDERNQV LTTYLWIRQT WFDAYLKWDK EEYDGLEVIR IPSNLVWRPD IVLYNKADEE
     ASGPADTNVV LRYNGEITWD MPAITKSSCV VDVSYFPFDW QWCNLTFGSW TYNGNQVDIA
     MGMDSGDLSD FVENVEWECH GMPAVRNVIM YGCCSDPYPD ITYTLHLKRR SLFYIFNLLL
     PCFLISFLAP LGFYLPADSG EKVSLGVTVL LALTVFQLMV AESMPPSESV PYIGKYYIAT
     MTMITASTSL TIFIMNIHFC GAEAKPVPHW AKVLIIDYMS KILFVYEVGE NCTTPESERT
     PLYSEEPMSG NSALARNHYH DDLYHDGGCY QDDCHRLRPY QYGNGHLQNH HSTHQNHLDN
     CRYANGGHRD DHYSNRSNQN HHSNRSQTSK GEGGEEKREP LRHYHHIGRE ELDYQAPPPG
     NLQNGGLNEP LPYPKEKHLN PASAPACSCP CPHHKQVVYN IQYIANCFRE QRATCAKGAE
     WKKVAKVMDR FFMWIFFIMV FLMSILIIGK AT