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Protein

Neuronal acetylcholine receptor subunit alpha-10

Gene

Chrna10

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

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).

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei31Involved in the interaction with the conotoxin GeXXA1 Publication1

GO - Molecular functioni

  • acetylcholine-gated cation-selective channel activity Source: RGD
  • calcium channel activity Source: UniProtKB-KW

GO - Biological processi

Keywordsi

Molecular functionCalcium channel, Ion channel, Ligand-gated ion channel, Receptor
Biological processCalcium transport, Ion transport, Transport
LigandCalcium

Names & Taxonomyi

Protein namesi
Recommended name:
Neuronal acetylcholine receptor subunit alpha-10
Alternative name(s):
Nicotinic acetylcholine receptor subunit alpha-10
Short name:
NACHR alpha-10
Gene namesi
Name:Chrna10
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi620142. Chrna10.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini25 – 237ExtracellularSequence analysisAdd BLAST213
Transmembranei238 – 258HelicalSequence analysisAdd BLAST21
Transmembranei268 – 288HelicalSequence analysisAdd BLAST21
Transmembranei302 – 322HelicalSequence analysisAdd BLAST21
Topological domaini323 – 425CytoplasmicSequence analysisAdd BLAST103
Transmembranei426 – 446HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

  • acetylcholine-gated channel complex Source: RGD
  • axon Source: RGD
  • cell junction Source: UniProtKB-KW
  • perikaryon Source: RGD
  • postsynaptic membrane Source: UniProtKB-SubCell

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi221E → Q: CHRNA9-CHRNA10 receptor is 25-fold less potently inhibited by the alpha-conotoxin RgIA. 1 Publication1
Mutagenesisi224P → Q: CHRNA9-CHRNA10 receptor is 300-fold less potently inhibited by the alpha-conotoxin RgIA. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL3461.
GuidetoPHARMACOLOGYi470.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
ChainiPRO_000000037725 – 447Neuronal acetylcholine receptor subunit alpha-10Add BLAST423

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi40N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi56N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi154 ↔ 168By similarity
Disulfide bondi218 ↔ 219Associated with receptor activationBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9JLB5.
PRIDEiQ9JLB5.

Expressioni

Tissue specificityi

Expressed in the outer hair cells of the cochlea and the neurons of dorsal root ganglia.2 Publications

Developmental stagei

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.2 Publications

Gene expression databases

GenevisibleiQ9JLB5. RN.

Interactioni

Subunit structurei

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).2 Publications

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000027506.

Chemistry databases

BindingDBiQ9JLB5.

Structurei

3D structure databases

ProteinModelPortaliQ9JLB5.
SMRiQ9JLB5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3645. Eukaryota.
ENOG410XQGR. LUCA.
GeneTreeiENSGT00790000122957.
HOGENOMiHOG000006756.
HOVERGENiHBG003756.
InParanoidiQ9JLB5.
KOiK04811.
OMAiAQRCHED.
OrthoDBiEOG091G0R20.
PhylomeDBiQ9JLB5.
TreeFamiTF315605.

Family and domain databases

Gene3Di2.70.170.10. 1 hit.
InterProiView protein in InterPro
IPR006202. Neur_chan_lig-bd.
IPR006201. Neur_channel.
IPR006029. Neurotrans-gated_channel_TM.
IPR018000. Neurotransmitter_ion_chnl_CS.
IPR002394. Nicotinic_acetylcholine_rcpt.
PANTHERiPTHR18945. PTHR18945. 1 hit.
PfamiView protein in Pfam
PF02931. Neur_chan_LBD. 1 hit.
PF02932. Neur_chan_memb. 1 hit.
PRINTSiPR00254. NICOTINICR.
PR00252. NRIONCHANNEL.
SUPFAMiSSF63712. SSF63712. 1 hit.
SSF90112. SSF90112. 1 hit.
TIGRFAMsiTIGR00860. LIC. 1 hit.
PROSITEiView protein in PROSITE
PS00236. NEUROTR_ION_CHANNEL. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9JLB5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGTRSHYLDL GFLLLLFLPA ECLGAEGRLA HKLFRDLFAN YTSALRPVAD
60 70 80 90 100
TDQTLNVTLE VTLSQIIDMD ERNQVLTLYL WIRQEWTDAY LHWDPKAYGD
110 120 130 140 150
LDAIRIPSRL VWRPDIVLYN KADTQPPASA STNVVVRHDG AVRWDAPAIT
160 170 180 190 200
RSSCRVDVSA FPFDAQRCGL TFGSWTHGGH QLDVRPRGTS ASLADFVENV
210 220 230 240 250
EWRVLGMPAR RRVLTYGCCS EPYPDVTFTL LLRRRAAAYV CNLLLPCVFI
260 270 280 290 300
SLLAPLAFHL PADSGEKVSL GVTVLLALTV FQLILAESMP PAESVPLIGK
310 320 330 340 350
YYMATMTMVT FSTALTILIM NLHYCGPNAH PVPAWARVLL LGHLAKGLCV
360 370 380 390 400
RERGEPCGQS KPLESAPSLQ PPPASPAGPC HEPRCLCHQE ALLHHIASIA
410 420 430 440
STFRSHRAAQ RRHEDWKRLA RVMDRFFLGI FFCMALVMSL IVLVQAL
Length:447
Mass (Da):49,820
Last modified:October 1, 2000 - v1
Checksum:iEEE49D93490B698F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF196344 mRNA. Translation: AAF27624.1.
RefSeqiNP_072161.1. NM_022639.1.
XP_017445156.1. XM_017589667.1.
UniGeneiRn.48767.

Genome annotation databases

EnsembliENSRNOT00000027507; ENSRNOP00000027506; ENSRNOG00000020293.
GeneIDi64574.
KEGGirno:64574.
UCSCiRGD:620142. rat.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiACH10_RAT
AccessioniPrimary (citable) accession number: Q9JLB5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: October 1, 2000
Last modified: May 10, 2017
This is version 118 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families