ACH10_RAT
ID ACH10_RAT Reviewed; 447 AA.
AC Q9JLB5;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Neuronal acetylcholine receptor subunit alpha-10;
DE AltName: Full=Nicotinic acetylcholine receptor subunit alpha-10;
DE Short=NACHR alpha-10;
DE Flags: Precursor;
GN Name=Chrna10;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH CHRNA9, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Sprague-Dawley;
RX PubMed=11248107; DOI=10.1073/pnas.051622798;
RA Elgoyhen A.B., Vetter D.E., Katz E., Rothlin C.V., Heinemann S.F.,
RA Boulter J.;
RT "Alpha10: a determinant of nicotinic cholinergic receptor function in
RT mammalian vestibular and cochlear mechanosensory hair cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3501-3506(2001).
RN [2]
RP FUNCTION, AND INTERACTION WITH CHRNA9.
RX PubMed=12117536; DOI=10.1016/s0378-5955(02)00380-5;
RA Weisstaub N., Vetter D.E., Elgoyhen A.B., Katz E.;
RT "The alpha9alpha10 nicotinic acetylcholine receptor is permeable to and is
RT modulated by divalent cations.";
RL Hear. Res. 167:122-135(2002).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=12401316; DOI=10.1016/s0306-4522(02)00274-9;
RA Lips K.S., Pfeil U., Kummer W.;
RT "Coexpression of alpha 9 and alpha 10 nicotinic acetylcholine receptors in
RT rat dorsal root ganglion neurons.";
RL Neuroscience 115:1-5(2002).
RN [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=15356192; DOI=10.1523/jneurosci.2102-04.2004;
RA Katz E., Elgoyhen A.B., Gomez-Casati M.E., Knipper M., Vetter D.E.,
RA Fuchs P.A., Glowatzki E.;
RT "Developmental regulation of nicotinic synapses on cochlear inner hair
RT cells.";
RL J. Neurosci. 24:7814-7820(2004).
RN [5]
RP FUNCTION, AND INTERACTION WITH CHRNA9.
RX PubMed=14742688; DOI=10.1124/mol.65.2.453;
RA Baker E.R., Zwart R., Sher E., Millar N.S.;
RT "Pharmacological properties of alpha 9 alpha 10 nicotinic acetylcholine
RT receptors revealed by heterologous expression of subunit chimeras.";
RL Mol. Pharmacol. 65:453-460(2004).
RN [6]
RP SITE HIS-31, AND SUBUNIT.
RX PubMed=26395518; DOI=10.1038/srep14261;
RA Xu S., Zhang T., Kompella S.N., Yan M., Lu A., Wang Y., Shao X., Chi C.,
RA Adams D.J., Ding J., Wang C.;
RT "Conotoxin alphaD-GeXXA utilizes a novel strategy to antagonize nicotinic
RT acetylcholine receptors.";
RL Sci. Rep. 5:14261-14268(2015).
RN [7]
RP MUTAGENESIS OF GLU-221 AND PRO-224, AND SUBUNIT.
RX PubMed=25740413; DOI=10.1124/mol.114.096511;
RA Azam L., Papakyriakou A., Zouridakis M., Giastas P., Tzartos S.J.,
RA McIntosh J.M.;
RT "Molecular interaction of alpha-conotoxin RgIA with the rat alpha9alpha10
RT nicotinic acetylcholine receptor.";
RL Mol. Pharmacol. 87:855-864(2015).
RN [8]
RP ERRATUM OF PUBMED:25740413.
RX PubMed=27559150; DOI=10.1124/mol.114.096511err;
RA Azam L., Papakyriakou A., Zouridakis M., Giastas P., Tzartos S.J.,
RA McIntosh J.M.;
RT "Corrections to 'Molecular interaction of alpha-conotoxin RgIA with the rat
RT alpha9alpha10 nicotinic acetylcholine receptor'.";
RL Mol. Pharmacol. 90:415-417(2016).
CC -!- FUNCTION: Ionotropic receptor with a probable role in the modulation of
CC auditory stimuli. Agonist binding may induce an extensive change in
CC conformation that affects all subunits and leads to opening of an ion-
CC conducting channel across the plasma membrane. The channel is permeable
CC to a range of divalent cations including calcium, the influx of which
CC may activate a potassium current which hyperpolarizes the cell
CC membrane. In the ear, this leads to a reduction in basilar membrane
CC motion, altering the activity of auditory nerve fibers and reducing the
CC range of dynamic hearing. This may protect against acoustic trauma.
CC {ECO:0000269|PubMed:11248107, ECO:0000269|PubMed:12117536,
CC ECO:0000269|PubMed:14742688}.
CC -!- SUBUNIT: Forms heterooligomeric channels in conjunction with CHRNA9.
CC The native outer hair cell receptor may be composed of CHRNA9-CHRNA10
CC heterooligomers. Interacts with the conotoxin GeXXA (PubMed:26395518).
CC Interacts with the alpha-conotoxin RgIA (PubMed:25740413).
CC {ECO:0000269|PubMed:25740413, ECO:0000269|PubMed:26395518}.
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 outer hair cells of the cochlea
CC and the neurons of dorsal root ganglia. {ECO:0000269|PubMed:11248107,
CC ECO:0000269|PubMed:12401316}.
CC -!- DEVELOPMENTAL STAGE: Expression in the inner hair cells of the ear is
CC lost at the onset of hearing, around P12. This correlates with a loss
CC of sensitivity of these cells to cholinergic stimuli.
CC {ECO:0000269|PubMed:11248107, ECO:0000269|PubMed:15356192}.
CC -!- MISCELLANEOUS: The heterooligomeric receptor composed of CHRNA9 and
CC CHRNA10 has an atypical pharmacological profile, binding several non-
CC nicotinic ligands including strychnine (a glycine receptor antagonist)
CC and atropine (a muscarinic acetylcholine receptor antagonist).
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-10/CHRNA10 sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; AF196344; AAF27624.1; -; mRNA.
DR RefSeq; NP_072161.1; NM_022639.1.
DR RefSeq; XP_017445156.1; XM_017589667.1.
DR AlphaFoldDB; Q9JLB5; -.
DR SMR; Q9JLB5; -.
DR ComplexPortal; CPX-224; Neuronal nicotinic acetylcholine receptor complex, alpha9-alpha10.
DR STRING; 10116.ENSRNOP00000027506; -.
DR BindingDB; Q9JLB5; -.
DR ChEMBL; CHEMBL3461; -.
DR DrugCentral; Q9JLB5; -.
DR GuidetoPHARMACOLOGY; 470; -.
DR GlyGen; Q9JLB5; 2 sites.
DR PaxDb; Q9JLB5; -.
DR PRIDE; Q9JLB5; -.
DR Ensembl; ENSRNOT00000027507; ENSRNOP00000027506; ENSRNOG00000020293.
DR GeneID; 64574; -.
DR KEGG; rno:64574; -.
DR UCSC; RGD:620142; rat.
DR CTD; 57053; -.
DR RGD; 620142; Chrna10.
DR eggNOG; KOG3645; Eukaryota.
DR GeneTree; ENSGT00940000160721; -.
DR HOGENOM; CLU_018074_0_0_1; -.
DR InParanoid; Q9JLB5; -.
DR OMA; QSNYMMS; -.
DR OrthoDB; 845098at2759; -.
DR PhylomeDB; Q9JLB5; -.
DR TreeFam; TF315605; -.
DR PRO; PR:Q9JLB5; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020293; Expressed in spleen.
DR Genevisible; Q9JLB5; RN.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; IC:ComplexPortal.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0098981; C:cholinergic synapse; IDA:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; IDA:SynGO.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; ISO:RGD.
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; IDA:SynGO.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; ISO:RGD.
DR GO; GO:0042472; P:inner ear morphogenesis; ISO:RGD.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0051899; P:membrane depolarization; IDA:ComplexPortal.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:RGD.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:RGD.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0010996; P:response to auditory stimulus; IDA:ComplexPortal.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; ISO:RGD.
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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..447
FT /note="Neuronal acetylcholine receptor subunit alpha-10"
FT /id="PRO_0000000377"
FT TOPO_DOM 25..237
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..425
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT SITE 31
FT /note="Involved in the interaction with the conotoxin
FT GeXXA"
FT /evidence="ECO:0000269|PubMed:26395518"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 154..168
FT /evidence="ECO:0000250"
FT DISULFID 218..219
FT /note="Associated with receptor activation"
FT /evidence="ECO:0000250"
FT MUTAGEN 221
FT /note="E->Q: CHRNA9-CHRNA10 receptor is 25-fold less
FT potently inhibited by the alpha-conotoxin RgIA."
FT /evidence="ECO:0000269|PubMed:25740413"
FT MUTAGEN 224
FT /note="P->Q: CHRNA9-CHRNA10 receptor is 300-fold less
FT potently inhibited by the alpha-conotoxin RgIA."
FT /evidence="ECO:0000269|PubMed:25740413"
SQ 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
