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Neuronal acetylcholine receptor subunit alpha-10 (Nicotinic acetylcholine receptor subunit alpha-10) (NACHR alpha-10)

 ACH10_RAT               Reviewed;         447 AA.
Q9JLB5;
21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
30-AUG-2017, entry version 119.
RecName: Full=Neuronal acetylcholine receptor subunit alpha-10;
AltName: Full=Nicotinic acetylcholine receptor subunit alpha-10;
Short=NACHR alpha-10;
Flags: Precursor;
Name=Chrna10;
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, INTERACTION WITH CHRNA9, TISSUE
SPECIFICITY, AND DEVELOPMENTAL STAGE.
STRAIN=Sprague-Dawley;
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).
[2]
FUNCTION, AND INTERACTION WITH CHRNA9.
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).
[3]
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).
[4]
DEVELOPMENTAL STAGE.
PubMed=15356192; DOI=10.1523/JNEUROSCI.2102-04.2004;
Katz E., Elgoyhen A.B., Gomez-Casati M.E., Knipper M., Vetter D.E.,
Fuchs P.A., Glowatzki E.;
"Developmental regulation of nicotinic synapses on cochlear inner hair
cells.";
J. Neurosci. 24:7814-7820(2004).
[5]
FUNCTION, AND INTERACTION WITH CHRNA9.
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).
[6]
SITE HIS-31, AND SUBUNIT.
PubMed=26395518; DOI=10.1038/srep14261;
Xu S., Zhang T., Kompella S.N., Yan M., Lu A., Wang Y., Shao X.,
Chi C., Adams D.J., Ding J., Wang C.;
"Conotoxin alphaD-GeXXA utilizes a novel strategy to antagonize
nicotinic acetylcholine receptors.";
Sci. Rep. 5:14261-14268(2015).
[7]
MUTAGENESIS OF GLU-221 AND PRO-224, 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).
[8]
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 may induce an
extensive change in conformation that affects all subunits and
leads to 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.
{ECO:0000269|PubMed:11248107, ECO:0000269|PubMed:12117536,
ECO:0000269|PubMed:14742688}.
-!- SUBUNIT: Forms heterooligomeric channels in conjunction with
CHRNA9. The native outer hair cell receptor may be composed of
CHRNA9-CHRNA10 heterooligomers. Interacts with the conotoxin GeXXA
(PubMed:26395518). Interacts with the alpha-conotoxin RgIA
(PubMed:25740413). {ECO:0000269|PubMed:25740413,
ECO:0000269|PubMed:26395518}.
-!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Cell membrane {ECO:0000305}; Multi-pass membrane protein
{ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed in the outer hair cells of the
cochlea and the neurons of dorsal root ganglia.
{ECO:0000269|PubMed:11248107, ECO:0000269|PubMed:12401316}.
-!- DEVELOPMENTAL STAGE: Expression in the inner hair cells of the ear
is lost at the onset of hearing, around P12. This correlates with
a loss of sensitivity of these cells to cholinergic stimuli.
{ECO:0000269|PubMed:11248107, ECO:0000269|PubMed:15356192}.
-!- 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).
-!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9)
family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-
10/CHRNA10 sub-subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF196344; AAF27624.1; -; mRNA.
RefSeq; NP_072161.1; NM_022639.1.
RefSeq; XP_017445156.1; XM_017589667.1.
UniGene; Rn.48767; -.
ProteinModelPortal; Q9JLB5; -.
SMR; Q9JLB5; -.
STRING; 10116.ENSRNOP00000027506; -.
BindingDB; Q9JLB5; -.
ChEMBL; CHEMBL3461; -.
GuidetoPHARMACOLOGY; 470; -.
PaxDb; Q9JLB5; -.
PRIDE; Q9JLB5; -.
Ensembl; ENSRNOT00000027507; ENSRNOP00000027506; ENSRNOG00000020293.
GeneID; 64574; -.
KEGG; rno:64574; -.
UCSC; RGD:620142; rat.
CTD; 57053; -.
RGD; 620142; Chrna10.
eggNOG; KOG3645; Eukaryota.
eggNOG; ENOG410XQGR; LUCA.
GeneTree; ENSGT00790000122957; -.
HOGENOM; HOG000006756; -.
HOVERGEN; HBG003756; -.
InParanoid; Q9JLB5; -.
KO; K04811; -.
OMA; AQRCHED; -.
OrthoDB; EOG091G0R20; -.
PhylomeDB; Q9JLB5; -.
TreeFam; TF315605; -.
PRO; PR:Q9JLB5; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000020293; -.
Genevisible; Q9JLB5; RN.
GO; GO:0005892; C:acetylcholine-gated channel complex; IMP:RGD.
GO; GO:0030424; C:axon; IDA:RGD.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0043204; C:perikaryon; IDA:RGD.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IMP:RGD.
GO; GO:0005262; F:calcium channel activity; IEA:UniProtKB-KW.
GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; IEA:Ensembl.
GO; GO:0042472; P:inner ear morphogenesis; IEA:Ensembl.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
GO; GO:0007271; P:synaptic transmission, cholinergic; TAS:RGD.
Gene3D; 2.70.170.10; -; 1.
InterPro; IPR006202; Neur_chan_lig-bd.
InterPro; IPR006201; Neur_channel.
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 24 {ECO:0000255}.
CHAIN 25 447 Neuronal acetylcholine receptor subunit
alpha-10.
/FTId=PRO_0000000377.
TOPO_DOM 25 237 Extracellular. {ECO:0000255}.
TRANSMEM 238 258 Helical. {ECO:0000255}.
TRANSMEM 268 288 Helical. {ECO:0000255}.
TRANSMEM 302 322 Helical. {ECO:0000255}.
TOPO_DOM 323 425 Cytoplasmic. {ECO:0000255}.
TRANSMEM 426 446 Helical. {ECO:0000255}.
SITE 31 31 Involved in the interaction with the
conotoxin GeXXA.
{ECO:0000269|PubMed:26395518}.
CARBOHYD 40 40 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 56 56 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 154 168 {ECO:0000250}.
DISULFID 218 219 Associated with receptor activation.
{ECO:0000250}.
MUTAGEN 221 221 E->Q: CHRNA9-CHRNA10 receptor is 25-fold
less potently inhibited by the alpha-
conotoxin RgIA.
{ECO:0000269|PubMed:25740413}.
MUTAGEN 224 224 P->Q: CHRNA9-CHRNA10 receptor is 300-fold
less potently inhibited by the alpha-
conotoxin RgIA.
{ECO:0000269|PubMed:25740413}.
SEQUENCE 447 AA; 49820 MW; EEE49D93490B698F CRC64;
MGTRSHYLDL GFLLLLFLPA ECLGAEGRLA HKLFRDLFAN YTSALRPVAD TDQTLNVTLE
VTLSQIIDMD ERNQVLTLYL WIRQEWTDAY LHWDPKAYGD LDAIRIPSRL VWRPDIVLYN
KADTQPPASA STNVVVRHDG AVRWDAPAIT RSSCRVDVSA FPFDAQRCGL TFGSWTHGGH
QLDVRPRGTS ASLADFVENV EWRVLGMPAR RRVLTYGCCS EPYPDVTFTL LLRRRAAAYV
CNLLLPCVFI SLLAPLAFHL PADSGEKVSL GVTVLLALTV FQLILAESMP PAESVPLIGK
YYMATMTMVT FSTALTILIM NLHYCGPNAH PVPAWARVLL LGHLAKGLCV RERGEPCGQS
KPLESAPSLQ PPPASPAGPC HEPRCLCHQE ALLHHIASIA STFRSHRAAQ RRHEDWKRLA
RVMDRFFLGI FFCMALVMSL IVLVQAL


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