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Protein

Neuronal acetylcholine receptor subunit alpha-3

Gene

Chrna3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.By similarity

GO - Molecular functioni

GO - Biological processi

  • activation of transmembrane receptor protein tyrosine kinase activity Source: MGI
  • behavioral response to nicotine Source: MGI
  • excitatory postsynaptic potential Source: MGI
  • locomotory behavior Source: MGI
  • nervous system development Source: MGI
  • regulation of acetylcholine secretion, neurotransmission Source: MGI
  • regulation of dendrite morphogenesis Source: MGI
  • regulation of membrane potential Source: MGI
  • regulation of muscle contraction Source: MGI
  • regulation of smooth muscle contraction Source: MGI
  • signal transduction Source: MGI
  • synaptic transmission, cholinergic Source: MGI
  • synaptic transmission involved in micturition Source: MGI

Keywordsi

Molecular functionIon channel, Ligand-gated ion channel, Receptor
Biological processIon transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Neuronal acetylcholine receptor subunit alpha-3
Gene namesi
Name:Chrna3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:87887. Chrna3.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini26 – 234ExtracellularSequence analysisAdd BLAST209
Transmembranei235 – 259HelicalSequence analysisAdd BLAST25
Transmembranei267 – 285HelicalSequence analysisAdd BLAST19
Transmembranei301 – 322HelicalSequence analysisAdd BLAST22
Topological domaini323 – 471CytoplasmicSequence analysisAdd BLAST149
Transmembranei472 – 491HelicalSequence analysisAdd BLAST20

Keywords - Cellular componenti

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

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3350222.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Sequence analysisAdd BLAST25
ChainiPRO_000000034726 – 499Neuronal acetylcholine receptor subunit alpha-3Add BLAST474

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi49N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi153 ↔ 167By similarity
Glycosylationi166N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi217 ↔ 218Associated with receptor activationBy similarity
Modified residuei407PhosphoserineBy similarity1
Modified residuei410PhosphoserineBy similarity1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ8R4G9.
PaxDbiQ8R4G9.
PRIDEiQ8R4G9.

PTM databases

PhosphoSitePlusiQ8R4G9.

Interactioni

Subunit structurei

Neuronal AChR is composed of two different types of subunits: alpha and beta. Alpha-3 subunit can be combined to beta-2 or beta-4 to give rise to functional receptors. Interacts with RIC3; which is required for proper folding and assembly. Interacts with LYPD6. The heteropentamer alpha-3-beta-2 interacts with alpha-conotoxins ImI, ImII, PnIA, GID and MII. The heteropentamer alpha-3-beta-4 interacts with the alpha-conotoxin ImI.By similarity

Protein-protein interaction databases

BioGridi225944. 2 interactors.
STRINGi10090.ENSMUSP00000034851.

Structurei

3D structure databases

ProteinModelPortaliQ8R4G9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3645. Eukaryota.
ENOG410XQGR. LUCA.
HOVERGENiHBG003756.
InParanoidiQ8R4G9.
KOiK04805.
PhylomeDBiQ8R4G9.

Family and domain databases

Gene3Di1.20.58.390. 1 hit.
2.70.170.10. 1 hit.
InterProiView protein in InterPro
IPR006202. Neur_chan_lig-bd.
IPR036734. Neur_chan_lig-bd_sf.
IPR006201. Neur_channel.
IPR036719. Neuro-gated_channel_TM_sf.
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.

Q8R4G9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGVVLPPPPL SMLMLVLMLL PVASASEAEH RLFQYLFEDY NEIIRPVANV
60 70 80 90 100
SHPVIIQFEV SMSQLVKVDE VNQIMETNLW LKQIWNDYKL KWKPSDYQGV
110 120 130 140 150
EFMRVPAEKI WKPDIVLYNN ADGDFQVDDK TKALLKYTGE VTWIPPAIFK
160 170 180 190 200
SSCKIDVTYF PFDYQNCTMK FGSWSYDKAK IDLVLIGSSM NLKDYWESGE
210 220 230 240 250
WAIIKAPGYK HEIKYNCCEE IYQDITYSLY IRRLPLFYTI NLIIPCLLIS
260 270 280 290 300
FLTVLVFYLP SDCGEKVTLC ISVLLSLTVF LLVITETIPS TSLVIPLIGE
310 320 330 340 350
YLLFTMIFVT LSIVITVFVL NVHYRTPTTH TMPTWVKAVF LNLLPRVMFM
360 370 380 390 400
TRPTSTEEDA PKTRNFYGAE LSNLNCFSRA DSKSCKEGYP CQDGTCGYCH
410 420 430 440 450
HRRVKISNFS ANLTRSSSSE SVDAVLSLSA LSPEIKEAIQ SVKYIAENMK
460 470 480 490
AQNVAKEIQD DWKYVAMVID RIFLWVFILV CILGTAGLFL QPLMARDDT
Length:499
Mass (Da):57,110
Last modified:June 1, 2002 - v1
Checksum:i721650E3F38D00FD
GO

Sequence cautioni

The sequence BAC37909 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF472588 mRNA. Translation: AAL84757.1.
AY574262 mRNA. Translation: AAS90358.1.
AK051730 mRNA. Translation: BAC34740.1.
AK053497 mRNA. Translation: BAC35404.1.
AK080415 mRNA. Translation: BAC37909.1. Different initiation.
RefSeqiNP_660111.2. NM_145129.2.
UniGeneiMm.63569.

Genome annotation databases

GeneIDi110834.
KEGGimmu:110834.
UCSCiuc009pry.1. mouse.

Similar proteinsi

Entry informationi

Entry nameiACHA3_MOUSE
AccessioniPrimary (citable) accession number: Q8R4G9
Secondary accession number(s): Q8BV44
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: June 1, 2002
Last modified: October 25, 2017
This is version 132 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families