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P04757 (ACHA3_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neuronal acetylcholine receptor subunit alpha-3
Gene names
Name:Chrna3
Synonyms:Acra3
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length499 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Subunit structure

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 By similarity.

Subcellular location

Cell junctionsynapsepostsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-3/CHRNA3 sub-subfamily. [View classification]

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentCell junction
Cell membrane
Membrane
Postsynaptic cell membrane
Synapse
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionIon channel
Ligand-gated ion channel
Receptor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processheart development

Inferred from expression pattern PubMed 15549397. Source: RGD

protein heterooligomerization

Inferred from direct assay PubMed 16129735. Source: RGD

response to drug

Inferred from direct assay PubMed 15896488. Source: RGD

response to inorganic substance

Inferred from expression pattern PubMed 15212813. Source: RGD

response to nicotine

Inferred from expression pattern PubMed 17105949. Source: RGD

   Cellular_componentacetylcholine-gated channel complex

Inferred from direct assay PubMed 16129735. Source: RGD

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

neuronal cell body

Inferred from direct assay PubMed 11297818. Source: RGD

postsynaptic density

Inferred from direct assay PubMed 14989600. Source: RGD

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionacetylcholine binding

Inferred from direct assay PubMed 11297818PubMed 15016836. Source: RGD

acetylcholine receptor activity

Inferred from direct assay Ref.2. Source: RGD

acetylcholine-activated cation-selective channel activity

Inferred from mutant phenotype PubMed 11297818. Source: RGD

drug binding

Inferred from direct assay PubMed 15016836PubMed 16129735. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 499474Neuronal acetylcholine receptor subunit alpha-3
PRO_0000000348

Regions

Topological domain26 – 234209Extracellular
Transmembrane235 – 25925Helical
Transmembrane267 – 28519Helical
Transmembrane301 – 32222Helical
Topological domain323 – 471149Cytoplasmic
Transmembrane472 – 49120Helical

Amino acid modifications

Glycosylation491N-linked (GlcNAc...) Potential
Glycosylation1661N-linked (GlcNAc...) Potential
Disulfide bond153 ↔ 167 By similarity
Disulfide bond217 ↔ 218Associated with receptor activation By similarity

Sequences

Sequence LengthMass (Da)Tools
P04757 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: D66C491E832B9C34

FASTA49956,998
        10         20         30         40         50         60 
MGVVLLPPPL SMLMLVLMLL PAASASEAEH RLFQYLFEDY NEIIRPVANV SHPVIIQFEV 

        70         80         90        100        110        120 
SMSQLVKVDE VNQIMETNLW LKQIWNDYKL KWKPSDYQGV EFMRVPAEKI WKPDIVLYNN 

       130        140        150        160        170        180 
ADGDFQVDDK TKALLKYTGE VTWIPPAIFK SSCKIDVTYF PFDYQNCTMK FGSWSYDKAK 

       190        200        210        220        230        240 
IDLVLIGSSM NLKDYWESGE WAIIKAPGYK HEIKYNCCEE IYQDITYSLY IRRLPLFYTI 

       250        260        270        280        290        300 
NLIIPCLLIS FLTVLVFYLP SDCGEKVTLC ISVLLSLTVF LLVITETIPS TSLVIPLIGE 

       310        320        330        340        350        360 
YLLFTMIFVT LSIVITVFVL NVHYRTPTTH TMPTWVKAVF LNLLPRVMFM TRPTSGEGDT 

       370        380        390        400        410        420 
PKTRTFYGAE LSNLNCFSRA DSKSCKEGYP CQDGTCGYCH HRRVKISNFS ANLTRSSSSE 

       430        440        450        460        470        480 
SVNAVLSLSA LSPEIKEAIQ SVKYIAENMK AQNVAKEIQD DWKYVAMVID RIFLWVFILV 

       490 
CILGTAGLFL QPLMARDDT 

« Hide

References

[1]"Isolation of a cDNA clone coding for a possible neural nicotinic acetylcholine receptor alpha-subunit."
Boulter J., Evans K., Goldman D.J., Martin G., Treco D., Heinemann S.F., Patrick J.
Nature 319:368-374(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Functional expression of two neuronal nicotinic acetylcholine receptors from cDNA clones identifies a gene family."
Boulter J., Connolly J.G., Deneris E.S., Goldman D.J., Heinemann S.F., Patrick J.
Proc. Natl. Acad. Sci. U.S.A. 84:7763-7767(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Characterization of an acetylcholine receptor alpha 3 gene promoter and its activation by the POU domain factor SCIP/Tst-1."
Yang X., McDonough J., Fyodorov D., Morris M., Wang F., Deneris E.S.
J. Biol. Chem. 269:10252-10264(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03440 mRNA. Translation: CAA27170.1.
L31621 mRNA. Translation: AAA41673.1.
U04961 Unassigned DNA. Translation: AAA18001.1.
IPIIPI00198781.
PIRA24572.
A53733.
UniGeneRn.10996.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OLFmodel-A/C28-235[»]
1OLJmodel-A/C28-235[»]
ProteinModelPortalP04757.
SMRP04757. Positions 235-326.
ModBaseSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000019307.

PTM databases

PhosphoSiteP04757.

Proteomic databases

PRIDEP04757.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:2345. rat.

Organism-specific databases

RGD2345. Chrna3.

Phylogenomic databases

eggNOGNOG290206.
HOGENOMHOG000006756.
HOVERGENHBG003756.
InParanoidP04757.
OrthoDBEOG45B1FG.

Gene expression databases

ArrayExpressP04757.
GenevestigatorP04757.
GermOnlineENSRNOG00000013829. Rattus norvegicus.

Family and domain databases

Gene3D1.20.120.370. 2 hits.
2.70.170.10. 1 hit.
InterProIPR027361. Acetylcholine_rcpt_TM.
IPR006202. Neur_chan_lig-bd.
IPR006201. Neur_channel.
IPR006029. Neurotrans-gated_channel_TM.
IPR018000. Neurotransmitter_ion_chnl_CS.
IPR002394. Nicotinic_acetylcholine_rcpt.
[Graphical view]
PANTHERPTHR18945. PTHR18945. 1 hit.
PfamPF02931. Neur_chan_LBD. 1 hit.
PF02932. Neur_chan_memb. 1 hit.
[Graphical view]
PRINTSPR00254. NICOTINICR.
PR00252. NRIONCHANNEL.
SUPFAMSSF90112. Neu_channel_TM. 1 hit.
SSF63712. Neur_chan_LBD. 1 hit.
TIGRFAMsTIGR00860. LIC. 1 hit.
PROSITEPS00236. NEUROTR_ION_CHANNEL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP04757.
ChEMBLCHEMBL3818.

Entry information

Entry nameACHA3_RAT
AccessionPrimary (citable) accession number: P04757
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: May 29, 2013
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families