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Q05941 (ACHA7_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neuronal acetylcholine receptor subunit alpha-7
Gene names
Name:Chrna7
Synonyms:Acra7
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length502 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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. The channel is blocked by alpha-bungarotoxin.

Subunit structure

Homopentamer. Interacts with RIC3; which is required for proper folding and assembly. Ref.5 Ref.6

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-7/CHRNA7 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 functionIonic channel
Ligand-gated ion channel
Receptor
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processcalcium ion transport

Inferred from mutant phenotype. Source: MGI

dopamine biosynthetic process

Inferred from expression pattern. Source: RGD

regulation of action potential in neuron

Inferred from direct assay. Source: RGD

synaptic transmission, cholinergic

Inferred from mutant phenotype. Source: RGD

   Cellular componentacetylcholine-gated channel complex

Inferred from direct assay. Source: RGD

asymmetric synapse

Inferred from direct assay. Source: RGD

axon

Inferred from direct assay. Source: RGD

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from direct assay. Source: RGD

dendritic shaft

Inferred from direct assay. Source: RGD

growth cone

Inferred from direct assay. Source: RGD

membrane raft

Inferred from direct assay. Source: RGD

neuronal cell body

Inferred from direct assay. Source: RGD

postsynaptic density

Inferred from direct assay. Source: RGD

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

presynaptic membrane

Inferred from direct assay. Source: RGD

   Molecular functionacetylcholine binding

Inferred from direct assay. Source: RGD

acetylcholine-activated cation-selective channel activity

Inferred from direct assay. Source: MGI

adenylate cyclase binding

Inferred from physical interaction. Source: RGD

drug binding

Inferred from direct assay. Source: RGD

protein kinase binding

Inferred from physical interaction. Source: RGD

receptor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

APPP050671EBI-79422,EBI-77613From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 By similarity
Chain23 – 502480Neuronal acetylcholine receptor subunit alpha-7
PRO_0000000369

Regions

Topological domain23 – 230208Extracellular Potential
Transmembrane231 – 25525Helical; Potential
Transmembrane262 – 28019Helical; Potential
Transmembrane296 – 31722Helical; Potential
Topological domain318 – 469152Cytoplasmic Potential
Transmembrane470 – 49021Helical; Potential

Amino acid modifications

Glycosylation461N-linked (GlcNAc...) Potential
Glycosylation901N-linked (GlcNAc...) Potential
Glycosylation1331N-linked (GlcNAc...) Potential
Disulfide bond150 ↔ 164 By similarity
Disulfide bond212 ↔ 213Associated with receptor activation By similarity

Experimental info

Mutagenesis4331L → A: Abolishes dependency on RIC3 for functional expression. Ref.5
Mutagenesis4351K → A: No effect on dependency on RIC3 for functional expression. Ref.5
Mutagenesis4401V → A: Impairs dependency on RIC3 for functional expression. Ref.5
Mutagenesis4451N → A: Slightly impairs dependency on RIC3 for functional expression. Ref.5
Mutagenesis4461R → A: Impairs dependency on RIC3 for functional expression. Ref.5
Mutagenesis4471F → A: Impairs dependency on RIC3 for functional expression. Ref.5
Mutagenesis4481R → A: Impairs dependency on RIC3 for functional expression. Ref.5
Sequence conflict4471F → N in AAB25224. Ref.1
Sequence conflict4691R → P in AAB25224. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q05941 [UniParc].

Last modified May 1, 2007. Version 2.
Checksum: 289A30498C7B9A58

FASTA50256,503
        10         20         30         40         50         60 
MCGGRGGIWL ALAAALLHVS LQGEFQRRLY KELVKNYNPL ERPVANDSQP LTVYFSLSLL 

        70         80         90        100        110        120 
QIMDVDEKNQ VLTTNIWLQM SWTDHYLQWN MSEYPGVKNV RFPDGQIWKP DILLYNSADE 

       130        140        150        160        170        180 
RFDATFHTNV LVNASGHCQY LPPGIFKSSC YIDVRWFPFD VQQCKLKFGS WSYGGWSLDL 

       190        200        210        220        230        240 
QMQEADISSY IPNGEWDLMG IPGKRNEKFY ECCKEPYPDV TYTVTMRRRT LYYGLNLLIP 

       250        260        270        280        290        300 
CVLISALALL VFLLPADSGE KISLGITVLL SLTVFMLLVA EIMPATSDSV PLIAQYFAST 

       310        320        330        340        350        360 
MIIVGLSVVV TVIVLRYHHH DPDGGKMPKW TRIILLNWCA WFLRMKRPGE DKVRPACQHK 

       370        380        390        400        410        420 
PRRCSLASVE LSAGAGPPTS NGNLLYIGFR GLEGMHCAPT PDSGVVCGRL ACSPTHDEHL 

       430        440        450        460        470        480 
MHGAHPSDGD PDLAKILEEV RYIANRFRCQ DESEVICSEW KFAACVVDRL CLMAFSVFTI 

       490        500 
ICTIGILMSA PNFVEAVSKD FA 

« Hide

References

[1]"Molecular cloning, functional properties, and distribution of rat brain alpha 7: a nicotinic cation channel highly permeable to calcium."
Seguela P., Wadiche J., Dineley-Miller K., Dani J.A., Patrick J.W.
J. Neurosci. 13:596-604(1993) [PubMed: 7678857] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]Boulter J.
Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Brain.
[3]Hartley M.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 363.
Strain: Sprague-Dawley.
Tissue: Brain.
[4]Groot-Kormelink P.J.
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Brain.
[5]"Dual role of the RIC-3 protein in trafficking of serotonin and nicotinic acetylcholine receptors."
Castillo M., Mulet J., Gutierrez L.M., Ortiz J.A., Castelan F., Gerber S., Sala S., Sala F., Criado M.
J. Biol. Chem. 280:27062-27068(2005) [PubMed: 15927954] [Abstract]
Cited for: INTERACTION WITH RIC3, MUTAGENESIS OF LEU-433; LYS-435; VAL-440; ASN-445; ARG-446; PHE-447 AND ARG-448.
[6]"RIC-3 enhances functional expression of multiple nicotinic acetylcholine receptor subtypes in mammalian cells."
Lansdell S.J., Gee V.J., Harkness P.C., Doward A.I., Baker E.R., Gibb A.J., Millar N.S.
Mol. Pharmacol. 68:1431-1438(2005) [PubMed: 16120769] [Abstract]
Cited for: INTERACTION WITH RIC3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S53987 mRNA. Translation: AAB25224.2.
L31619 mRNA. Translation: AAC33136.1.
AY574256 mRNA. Translation: AAS90352.1.
IPIIPI00607154.
PIRT01378.
RefSeqNP_036964.3. NM_012832.3.
UniGeneRn.9698.

3D structure databases

ProteinModelPortalQ05941.
SMRQ05941. Positions 227-261.
ModBaseSearch...

Protein-protein interaction databases

IntActQ05941. 1 interaction.
STRINGQ05941.

PTM databases

PhosphoSiteQ05941.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID25302.
KEGGrno:25302.
UCSCAY671974. rat.

Organism-specific databases

CTD1139.
RGD2348. Chrna7.

Phylogenomic databases

eggNOGroNOG14608.
HOVERGENHBG003756.

Gene expression databases

ArrayExpressQ05941.
GenevestigatorQ05941.
GermOnlineENSRNOG00000010853. Rattus norvegicus.

Family and domain databases

InterProIPR006202. Neur_chan_lig-bd.
IPR006201. Neur_channel.
IPR006029. Neurotrans-gated_channel_TM.
IPR018000. Neurotransmitter_ion_chnl_CS.
IPR002394. Nicotinic_acetylcholine_rcpt.
[Graphical view]
Gene3DG3DSA:2.70.170.10. Neur_chan_lig_bd. 1 hit.
KOK04809.
PANTHERPTHR18945. Neur_channel. 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

NextBio606083.

Entry information

Entry nameACHA7_RAT
AccessionPrimary (citable) accession number: Q05941
Secondary accession number(s): Q53YK2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: May 1, 2007
Last modified: January 25, 2012
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families