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Neuronal acetylcholine receptor subunit alpha-9 (Nicotinic acetylcholine receptor subunit alpha-9) (NACHR alpha-9)

 ACHA9_RAT               Reviewed;         479 AA.
P43144; Q6PW49;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
21-JUN-2005, sequence version 2.
22-NOV-2017, entry version 149.
RecName: Full=Neuronal acetylcholine receptor subunit alpha-9;
AltName: Full=Nicotinic acetylcholine receptor subunit alpha-9;
Short=NACHR alpha-9;
Flags: Precursor;
Name=Chrna9; Synonyms=Acra9;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
TISSUE=Olfactory epithelium;
PubMed=7954834; DOI=10.1016/0092-8674(94)90555-X;
Elgoyhen A.B., Johnson D.S., Boulter J., Vetter D.E., Heinemann S.F.;
"Alpha 9: an acetylcholine receptor with novel pharmacological
properties expressed in rat cochlear hair cells.";
Cell 79:705-715(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Brain;
Groot-Kormelink P.J.;
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
[3]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10713500; DOI=10.1016/S0378-5955(99)00214-2;
Katz E., Verbitsky M., Rothlin C.V., Vetter D.E., Heinemann S.F.,
Elgoyhen A.B.;
"High calcium permeability and calcium block of the alpha9 nicotinic
acetylcholine receptor.";
Hear. Res. 141:117-128(2000).
[4]
FUNCTION.
PubMed=11044723; DOI=10.1016/S0028-3908(00)00124-6;
Verbitsky M., Rothlin C.V., Katz E., Elgoyhen A.B.;
"Mixed nicotinic-muscarinic properties of the alpha9 nicotinic
cholinergic receptor.";
Neuropharmacology 39:2515-2524(2000).
[5]
INTERACTION WITH CHRNA10, SUBUNIT, TISSUE SPECIFICITY, FUNCTION, AND
SUBCELLULAR LOCATION.
PubMed=11248107; DOI=10.1073/pnas.051622798;
Elgoyhen A.B., Vetter D.E., Katz E., Rothlin C.V., Heinemann S.F.,
Boulter J.;
"Alpha10: a determinant of nicotinic cholinergic receptor function in
mammalian vestibular and cochlear mechanosensory hair cells.";
Proc. Natl. Acad. Sci. U.S.A. 98:3501-3506(2001).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CHRNA10.
PubMed=12117536; DOI=10.1016/S0378-5955(02)00380-5;
Weisstaub N., Vetter D.E., Elgoyhen A.B., Katz E.;
"The alpha9alpha10 nicotinic acetylcholine receptor is permeable to
and is modulated by divalent cations.";
Hear. Res. 167:122-135(2002).
[7]
TISSUE SPECIFICITY.
PubMed=12401316; DOI=10.1016/S0306-4522(02)00274-9;
Lips K.S., Pfeil U., Kummer W.;
"Coexpression of alpha 9 and alpha 10 nicotinic acetylcholine
receptors in rat dorsal root ganglion neurons.";
Neuroscience 115:1-5(2002).
[8]
FUNCTION, AND INTERACTION WITH CHRNA10.
PubMed=14742688; DOI=10.1124/mol.65.2.453;
Baker E.R., Zwart R., Sher E., Millar N.S.;
"Pharmacological properties of alpha 9 alpha 10 nicotinic
acetylcholine receptors revealed by heterologous expression of subunit
chimeras.";
Mol. Pharmacol. 65:453-460(2004).
[9]
SITE THR-86, AND MUTAGENESIS OF SER-36; SER-44; ALA-54; THR-86;
ARG-101; SER-147 AND SER-166.
PubMed=22774872; DOI=10.1111/j.1471-4159.2012.07867.x;
Azam L., McIntosh J.M.;
"Molecular basis for the differential sensitivity of rat and human
alpha9alpha10 nAChRs to alpha-conotoxin RgIA.";
J. Neurochem. 122:1137-1144(2012).
[10]
MUTAGENESIS OF TRP-176.
PubMed=18295795; DOI=10.1016/j.jmb.2008.01.082;
Ellison M., Feng Z.P., Park A.J., Zhang X., Olivera B.M.,
McIntosh J.M., Norton R.S.;
"Alpha-RgIA, a novel conotoxin that blocks the alpha9alpha10 nAChR:
structure and identification of key receptor-binding residues.";
J. Mol. Biol. 377:1216-1227(2008).
[11]
SITE ASP-146, MUTAGENESIS OF THR-86 AND ASP-146, AND SUBUNIT.
PubMed=25740413; DOI=10.1124/mol.114.096511;
Azam L., Papakyriakou A., Zouridakis M., Giastas P., Tzartos S.J.,
McIntosh J.M.;
"Molecular interaction of alpha-conotoxin RgIA with the rat
alpha9alpha10 nicotinic acetylcholine receptor.";
Mol. Pharmacol. 87:855-864(2015).
[12]
ERRATUM.
PubMed=27559150; DOI=10.1124/mol.114.096511err;
Azam L., Papakyriakou A., Zouridakis M., Giastas P., Tzartos S.J.,
McIntosh J.M.;
"Corrections to 'Molecular interaction of alpha-conotoxin RgIA with
the rat alpha9alpha10 nicotinic acetylcholine receptor'.";
Mol. Pharmacol. 90:415-417(2016).
-!- FUNCTION: Ionotropic receptor with a probable role in the
modulation of auditory stimuli. Agonist binding induces a
conformation change that leads to the opening of an ion-conducting
channel across the plasma membrane. The channel is permeable to a
range of divalent cations including calcium, the influx of which
may activate a potassium current which hyperpolarizes the cell
membrane. In the ear, this leads to a reduction in basilar
membrane motion, altering the activity of auditory nerve fibers
and reducing the range of dynamic hearing. This may protect
against acoustic trauma. May also regulate keratinocyte adhesion.
{ECO:0000269|PubMed:10713500, ECO:0000269|PubMed:11044723,
ECO:0000269|PubMed:11248107, ECO:0000269|PubMed:12117536,
ECO:0000269|PubMed:14742688, ECO:0000269|PubMed:7954834,
ECO:0000305}.
-!- SUBUNIT: Can form homo- or heterooligomeric channels in
conjunction with CHRNA10. The native outer hair cell receptor may
be composed of CHRNA9-CHRNA10 heterooligomers. Interacts with the
alpha-conotoxin RgIA (PubMed:25740413).
{ECO:0000269|PubMed:11248107, ECO:0000269|PubMed:12117536,
ECO:0000269|PubMed:14742688, ECO:0000269|PubMed:25740413,
ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Cell membrane {ECO:0000269|PubMed:10713500,
ECO:0000269|PubMed:11248107, ECO:0000269|PubMed:12117536,
ECO:0000269|PubMed:7954834}; Multi-pass membrane protein
{ECO:0000305}.
-!- TISSUE SPECIFICITY: Detected in the nasal epithelium, in the outer
hair cells of the cochlea, in the pars tuberalis of the
hypophysis, and in the developing muscle of the tongue. Also
expressed in the neurons of dorsal root ganglia.
{ECO:0000269|PubMed:11248107, ECO:0000269|PubMed:12401316,
ECO:0000269|PubMed:7954834}.
-!- MISCELLANEOUS: The heterooligomeric receptor composed of CHRNA9
and CHRNA10 has an atypical pharmacological profile, binding
several non-nicotinic ligands including strychnine (a glycine
receptor antagonist) and atropine (a muscarinic acetylcholine
receptor antagonist). {ECO:0000269|PubMed:7954834}.
-!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9)
family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-
9/CHRNA9 sub-subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U12336; AAA56720.1; -; mRNA.
EMBL; AY574257; AAS90353.1; -; mRNA.
PIR; A55382; A55382.
RefSeq; NP_075219.1; NM_022930.1.
UniGene; Rn.54463; -.
ProteinModelPortal; P43144; -.
MINT; MINT-4996733; -.
STRING; 10116.ENSRNOP00000003382; -.
BindingDB; P43144; -.
ChEMBL; CHEMBL2585; -.
GuidetoPHARMACOLOGY; 469; -.
PhosphoSitePlus; P43144; -.
PaxDb; P43144; -.
PRIDE; P43144; -.
DNASU; 65024; -.
Ensembl; ENSRNOT00000003382; ENSRNOP00000003382; ENSRNOG00000002484.
GeneID; 65024; -.
KEGG; rno:65024; -.
UCSC; RGD:621534; rat.
CTD; 55584; -.
RGD; 621534; Chrna9.
eggNOG; KOG3645; Eukaryota.
eggNOG; ENOG410XQGR; LUCA.
GeneTree; ENSGT00790000122957; -.
HOGENOM; HOG000006756; -.
HOVERGEN; HBG003756; -.
InParanoid; P43144; -.
KO; K04810; -.
OMA; ATKNVIM; -.
OrthoDB; EOG091G0R20; -.
PhylomeDB; P43144; -.
TreeFam; TF315605; -.
Reactome; R-RNO-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
PRO; PR:P43144; -.
Proteomes; UP000002494; Chromosome 14.
Bgee; ENSRNOG00000002484; -.
Genevisible; P43144; RN.
GO; GO:0005892; C:acetylcholine-gated channel complex; IDA:RGD.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IDA:RGD.
GO; GO:0005262; F:calcium channel activity; IEA:UniProtKB-KW.
GO; GO:0006812; P:cation transport; ISO:RGD.
GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; ISO:RGD.
GO; GO:0042472; P:inner ear morphogenesis; ISO:RGD.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:RGD.
GO; GO:0007605; P:sensory perception of sound; IEP:RGD.
Gene3D; 1.20.58.390; -; 1.
Gene3D; 2.70.170.10; -; 1.
InterPro; IPR006202; Neur_chan_lig-bd.
InterPro; IPR036734; Neur_chan_lig-bd_sf.
InterPro; IPR006201; Neur_channel.
InterPro; IPR036719; Neuro-gated_channel_TM_sf.
InterPro; IPR006029; Neurotrans-gated_channel_TM.
InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
InterPro; IPR002394; Nicotinic_acetylcholine_rcpt.
PANTHER; PTHR18945; PTHR18945; 1.
Pfam; PF02931; Neur_chan_LBD; 1.
Pfam; PF02932; Neur_chan_memb; 1.
PRINTS; PR00254; NICOTINICR.
PRINTS; PR00252; NRIONCHANNEL.
SUPFAM; SSF63712; SSF63712; 1.
SUPFAM; SSF90112; SSF90112; 1.
TIGRFAMs; TIGR00860; LIC; 1.
PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
1: Evidence at protein level;
Calcium; Calcium channel; Calcium transport; Cell junction;
Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
Ion channel; Ion transport; Ligand-gated ion channel; Membrane;
Postsynaptic cell membrane; Receptor; Reference proteome; Signal;
Synapse; Transmembrane; Transmembrane helix; Transport.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 479 Neuronal acetylcholine receptor subunit
alpha-9.
/FTId=PRO_0000000372.
TOPO_DOM 26 237 Extracellular. {ECO:0000255}.
TRANSMEM 238 262 Helical. {ECO:0000255}.
TRANSMEM 269 287 Helical. {ECO:0000255}.
TRANSMEM 302 323 Helical. {ECO:0000255}.
TOPO_DOM 324 457 Cytoplasmic. {ECO:0000255}.
TRANSMEM 458 476 Helical. {ECO:0000255}.
SITE 86 86 Key residue important for potent
inhibition of the CHRNA9-CHRNA10 receptor
by the alpha-conotoxin RgIA (AC P0C1D0).
{ECO:0000269|PubMed:22774872}.
SITE 146 146 Key residue important for potent
inhibition of the CHRNA9-CHRNA10 receptor
by the alpha-conotoxin RgIA (AC P0C1D0).
{ECO:0000269|PubMed:25740413}.
CARBOHYD 57 57 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 170 170 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 155 169 {ECO:0000250|UniProtKB:Q9UGM1}.
DISULFID 219 220 {ECO:0000250|UniProtKB:Q9UGM1}.
MUTAGEN 36 36 S->N: No significant change in potency of
inhibition of the CHRNA9-CHRNA10 receptor
by the alpha-conotoxin RgIA.
{ECO:0000269|PubMed:22774872}.
MUTAGEN 44 44 S->N: No significant change in potency of
inhibition of the CHRNA9-CHRNA10
receptorby the alpha-conotoxin RgIA.
{ECO:0000269|PubMed:22774872}.
MUTAGEN 54 54 A->K: No significant change in potency of
inhibition of the CHRNA9-CHRNA10
receptorby the alpha-conotoxin RgIA.
{ECO:0000269|PubMed:22774872}.
MUTAGEN 86 86 T->E: The CHRNA9-CHRNA10 receptor is 20-
fold less potently inhibited by the
alpha-conotoxin RgIA.
{ECO:0000269|PubMed:25740413}.
MUTAGEN 86 86 T->I: The CHRNA9-CHRNA10 receptor is
1700-fold less potently inhibited by the
alpha-conotoxin RgIA.
{ECO:0000269|PubMed:22774872,
ECO:0000269|PubMed:25740413}.
MUTAGEN 101 101 R->G: No significant change in potency of
inhibition of the CHRNA9-CHRNA10 receptor
by the alpha-conotoxin RgIA.
{ECO:0000269|PubMed:22774872}.
MUTAGEN 146 146 D->L: Complete loss of inhibition of the
CHRNA9-CHRNA10 receptor by the alpha-
conotoxin RgIA.
{ECO:0000269|PubMed:25740413}.
MUTAGEN 147 147 S->A: No significant change in potency of
inhibition of the CHRNA9-CHRNA10 receptor
by the alpha-conotoxin RgIA.
{ECO:0000269|PubMed:22774872}.
MUTAGEN 166 166 S->N: No significant change in potency of
inhibition of the CHRNA9-CHRNA10 receptor
by the alpha-conotoxin RgIA.
{ECO:0000269|PubMed:22774872}.
MUTAGEN 176 176 W->T: The CHRNA9-CHRNA10 receptor is 8.5-
fold less potently inhibited by the
alpha-conotoxin RgIA.
{ECO:0000269|PubMed:18295795}.
CONFLICT 425 425 T -> A (in Ref. 1; AAA56720).
{ECO:0000305}.
SEQUENCE 479 AA; 54526 MW; CBB3E15E9DF68837 CRC64;
MNRPHSCLSF CWMYFAASGI RAVETANGKY AQKLFSDLFE DYSSALRPVE DTDAVLNVTL
QVTLSQIKDM DERNQILTAY LWIRQTWHDA YLTWDRDQYD RLDSIRIPSD LVWRPDIVLY
NKADDESSEP VNTNVVLRYD GLITWDSPAI TKSSCVVDVT YFPFDSQQCN LTFGSWTYNG
NQVDIFNALD SGDLSDFIED VEWEVHGMPA VKNVISYGCC SEPYPDVTFT LLLKRRSSFY
IVNLLIPCVL ISFLAPLSFY LPAASGEKVS LGVTILLAMT VFQLMVAEIM PASENVPLIG
KYYIATMALI TASTALTIMV MNIHFCGAEA RPVPHWAKVV ILKYMSRILF VYDVGESCLS
PRHSQEPEQV TKVYSKLPES NLKTSRNKDL SRKKEVRKLL KNDLGYQGGI PQNTDSYCAR
YEALTKNIEY IAKCLKDHKA TNSKGSEWKK VAKVIDRFFM WIFFAMVFVM TVLIIARAD


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