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Protein

Neuronal acetylcholine receptor subunit alpha-3

Gene

Chrna3

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

GO - Molecular functioni

  • acetylcholine binding Source: RGD
  • acetylcholine-gated cation-selective channel activity Source: RGD
  • acetylcholine receptor activity Source: RGD
  • drug binding Source: RGD
  • protein heterodimerization activity Source: RGD
  • serotonin-gated cation-selective channel activity Source: GO_Central

GO - Biological processi

  • acetylcholine receptor signaling pathway Source: ARUK-UCL
  • heart development Source: RGD
  • protein heterooligomerization Source: RGD
  • response to acetylcholine Source: ARUK-UCL
  • response to drug Source: RGD
  • response to inorganic substance Source: RGD
  • response to nicotine Source: RGD

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
Synonyms:Acra3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2345. Chrna3.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini26 – 234ExtracellularAdd BLAST209
Transmembranei235 – 259HelicalAdd BLAST25
Transmembranei267 – 285HelicalAdd BLAST19
Transmembranei301 – 322HelicalAdd BLAST22
Topological domaini323 – 471CytoplasmicAdd BLAST149
Transmembranei472 – 491HelicalAdd BLAST20

GO - Cellular componenti

  • acetylcholine-gated channel complex Source: RGD
  • cell junction Source: UniProtKB-KW
  • dendrite Source: RGD
  • membrane Source: RGD
  • neuronal cell body Source: RGD
  • plasma membrane raft Source: ARUK-UCL
  • postsynaptic density Source: RGD
  • postsynaptic membrane Source: UniProtKB-SubCell

Keywords - Cellular componenti

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

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3818.
GuidetoPHARMACOLOGYi464.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Sequence analysisAdd BLAST25
ChainiPRO_000000034826 – 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 residuei407PhosphoserineCombined sources1
Modified residuei410PhosphoserineCombined sources1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP04757.
PRIDEiP04757.

PTM databases

iPTMnetiP04757.
PhosphoSitePlusiP04757.

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 (PubMed:15609996, PubMed:15929983).By similarity2 Publications

GO - Molecular functioni

  • protein heterodimerization activity Source: RGD

Protein-protein interaction databases

IntActiP04757. 1 interactor.
STRINGi10116.ENSRNOP00000019307.

Chemistry databases

BindingDBiP04757.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OLFmodel-A/C28-235[»]
1OLJmodel-A/C28-235[»]
ProteinModelPortaliP04757.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3645. Eukaryota.
ENOG410XQGR. LUCA.
HOGENOMiHOG000006756.
HOVERGENiHBG003756.
InParanoidiP04757.
PhylomeDBiP04757.

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.

P04757-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGVVLLPPPL SMLMLVLMLL PAASASEAEH 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
TRPTSGEGDT PKTRTFYGAE LSNLNCFSRA DSKSCKEGYP CQDGTCGYCH
410 420 430 440 450
HRRVKISNFS ANLTRSSSSE SVNAVLSLSA LSPEIKEAIQ SVKYIAENMK
460 470 480 490
AQNVAKEIQD DWKYVAMVID RIFLWVFILV CILGTAGLFL QPLMARDDT
Length:499
Mass (Da):56,998
Last modified:August 13, 1987 - v1
Checksum:iD66C491E832B9C34
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03440 mRNA. Translation: CAA27170.1.
L31621 mRNA. Translation: AAA41673.1.
U04961 Unassigned DNA. Translation: AAA18001.1.
PIRiA24572.
A53733.
UniGeneiRn.10996.

Genome annotation databases

UCSCiRGD:2345. 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 nameiACHA3_RAT
AccessioniPrimary (citable) accession number: P04757
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: July 5, 2017
This is version 143 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families