ACHA9_CHICK
ID ACHA9_CHICK Reviewed; 484 AA.
AC Q9PTS8;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Neuronal acetylcholine receptor subunit alpha-9;
DE AltName: Full=Nicotinic acetylcholine receptor subunit alpha-9;
DE Short=NACHR alpha-9;
DE Flags: Precursor;
GN Name=CHRNA9;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Cochlea;
RX PubMed=10700617; DOI=10.1016/s0006-8993(00)01947-8;
RA Hiel H., Luebke A.E., Fuchs P.A.;
RT "Cloning and expression of the alpha9 nicotinic acetylcholine receptor
RT subunit in cochlear hair cells of the chick.";
RL Brain Res. 858:215-225(2000).
CC -!- FUNCTION: Ionotropic receptor that may play a role in the modulation of
CC auditory stimuli. Agonist binding induces a conformation change that
CC leads to the opening of an ion-conducting channel across the plasma
CC membrane. The channel is permeable to a range of divalent cations
CC including calcium, the influx of which may activate a potassium current
CC which hyperpolarizes the cell membrane. {ECO:0000250|UniProtKB:P43144}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000305}; Multi-
CC pass membrane protein {ECO:0000305}. Cell membrane
CC {ECO:0000250|UniProtKB:P43144}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P43144}.
CC -!- TISSUE SPECIFICITY: Expressed in hair cells of the cochlea (at protein
CC level). Expressed in hair cells of the cochlea.
CC {ECO:0000269|PubMed:10700617}.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-9/CHRNA9 sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; AF082192; AAF24618.1; -; mRNA.
DR RefSeq; NP_990091.1; NM_204760.1.
DR AlphaFoldDB; Q9PTS8; -.
DR SMR; Q9PTS8; -.
DR ComplexPortal; CPX-225; Neuronal nicotinic acetylcholine receptor complex, alpha9-alpha10.
DR ComplexPortal; CPX-229; Neuronal nicotinic acetylcholine receptor complex, alpha9.
DR STRING; 9031.ENSGALP00000023037; -.
DR PaxDb; Q9PTS8; -.
DR Ensembl; ENSGALT00000023080; ENSGALP00000023037; ENSGALG00000014268.
DR GeneID; 395522; -.
DR KEGG; gga:395522; -.
DR CTD; 55584; -.
DR VEuPathDB; HostDB:geneid_395522; -.
DR eggNOG; KOG3645; Eukaryota.
DR GeneTree; ENSGT00940000156077; -.
DR HOGENOM; CLU_018074_0_0_1; -.
DR InParanoid; Q9PTS8; -.
DR OMA; ICIINER; -.
DR OrthoDB; 845098at2759; -.
DR PhylomeDB; Q9PTS8; -.
DR TreeFam; TF315605; -.
DR Reactome; R-GGA-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
DR PRO; PR:Q9PTS8; -.
DR Proteomes; UP000000539; Chromosome 4.
DR Bgee; ENSGALG00000014268; Expressed in granulocyte and 2 other tissues.
DR ExpressionAtlas; Q9PTS8; baseline and differential.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; IC:ComplexPortal.
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:0005262; F:calcium channel activity; IEA:UniProtKB-KW.
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:0051899; P:membrane depolarization; IDA:ComplexPortal.
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:0007165; P:signal transduction; IBA:GO_Central.
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 1: Evidence at protein level;
KW Calcium; Calcium channel; Calcium transport; Cell membrane; Disulfide bond;
KW Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
KW Membrane; Postsynaptic cell membrane; Receptor; Reference proteome; Signal;
KW Synapse; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..484
FT /note="Neuronal acetylcholine receptor subunit alpha-9"
FT /id="PRO_0000000373"
FT TOPO_DOM 28..240
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..462
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 463..483
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 364..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 157..171
FT /evidence="ECO:0000250|UniProtKB:Q9UGM1"
FT DISULFID 221..222
FT /evidence="ECO:0000250|UniProtKB:Q9UGM1"
SQ SEQUENCE 484 AA; 55286 MW; 06B831ED8447FDE3 CRC64;
MKRNNLSSFY VSLWLLFTAT MLQAVESAKG KYAQMLFNEL FEDYSNALRP VEDTDKVLNV
TLQITLSQIK DMDERNQILT AYLWIRQSWY DAYLKWDKDK YDGLDSIRIP SNLVWRPDIV
LYNKADDDFS EPVNTNVVLR YDGKITWDAP AITKSSCVVD VSYFPFDSQQ CNLTFGSWTY
NGNQVDIINS LDSGDLSDFV EDVEWEIHGM PAVKNVITYG CCSEPYPDVT FTLILKRKSS
FYIFNLLLPC ILISFLAPLG FYLPADSGEK VSLGVTVLLA LTVFQLMVAE IMPPSENVPL
IGKYYIATMT MITASTALTI IIMNVHHCGS EAKPVPQWAR VVILDYMSKI FFVYDVGENC
TSPRREKEQE HRLEGGDMCR GGDGKSHLSS RNDDSDLKEN LNGNWNKSFG VHGENVRENV
NCCSCYKMLI KNIEYIANCV RDHKANRAKG IEWKKVAKVM DRFFMWIFFI MVFFMSVLII
GKAA
