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Protein

Neuronal acetylcholine receptor subunit alpha-7

Gene

Chrna7

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. The channel is blocked by alpha-bungarotoxin.

GO - Molecular functioni

  • acetylcholine-activated cation-selective channel activity Source: MGI
  • acetylcholine binding Source: RGD
  • adenylate cyclase binding Source: RGD
  • ATPase binding Source: RGD
  • drug binding Source: RGD
  • protein kinase binding Source: RGD
  • scaffold protein binding Source: RGD

GO - Biological processi

  • calcium ion transport Source: MGI
  • cation transmembrane transport Source: GOC
  • dopamine biosynthetic process Source: RGD
  • neuronal action potential Source: RGD
  • regulation of membrane potential Source: MGI
  • synaptic transmission, cholinergic Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Ligand-gated ion channel, Receptor

Keywords - Biological processi

Ion transport, Transport

Enzyme and pathway databases

ReactomeiR-RNO-629594. Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.

Names & Taxonomyi

Protein namesi
Recommended name:
Neuronal acetylcholine receptor subunit alpha-7
Gene namesi
Name:Chrna7
Synonyms:Acra7
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2348. Chrna7.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 230208ExtracellularSequence analysisAdd
BLAST
Transmembranei231 – 25525HelicalSequence analysisAdd
BLAST
Transmembranei262 – 28019HelicalSequence analysisAdd
BLAST
Transmembranei296 – 31722HelicalSequence analysisAdd
BLAST
Topological domaini318 – 469152CytoplasmicSequence analysisAdd
BLAST
Transmembranei470 – 49021HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • acetylcholine-gated channel complex Source: RGD
  • asymmetric synapse Source: RGD
  • axon Source: RGD
  • cell junction Source: UniProtKB-KW
  • cytoplasm Source: RGD
  • dendrite Source: RGD
  • dendritic shaft Source: RGD
  • dendritic spine Source: RGD
  • growth cone Source: RGD
  • membrane raft Source: RGD
  • neuronal cell body Source: RGD
  • plasma membrane Source: RGD
  • postsynaptic density Source: RGD
  • postsynaptic membrane Source: UniProtKB-SubCell
  • presynaptic membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi433 – 4331L → A: Abolishes dependency on RIC3 for functional expression. 1 Publication
Mutagenesisi435 – 4351K → A: No effect on dependency on RIC3 for functional expression. 1 Publication
Mutagenesisi440 – 4401V → A: Impairs dependency on RIC3 for functional expression. 1 Publication
Mutagenesisi445 – 4451N → A: Slightly impairs dependency on RIC3 for functional expression. 1 Publication
Mutagenesisi446 – 4461R → A: Impairs dependency on RIC3 for functional expression. 1 Publication
Mutagenesisi447 – 4471F → A: Impairs dependency on RIC3 for functional expression. 1 Publication
Mutagenesisi448 – 4481R → A: Impairs dependency on RIC3 for functional expression. 1 Publication

Chemistry

ChEMBLiCHEMBL2094110.
GuidetoPHARMACOLOGYi468.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222By similarityAdd
BLAST
Chaini23 – 502480Neuronal acetylcholine receptor subunit alpha-7PRO_0000000369Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi46 – 461N-linked (GlcNAc...)Sequence analysis
Glycosylationi90 – 901N-linked (GlcNAc...)Sequence analysis
Glycosylationi133 – 1331N-linked (GlcNAc...)Sequence analysis
Disulfide bondi150 ↔ 164By similarity
Disulfide bondi212 ↔ 213Associated with receptor activationBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ05941.

PTM databases

iPTMnetiQ05941.
PhosphoSiteiQ05941.
SwissPalmiQ05941.

Interactioni

Subunit structurei

Homopentamer. Interacts with RIC3; which is required for proper folding and assembly.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P606154EBI-79422,EBI-7516391From a different organism.

GO - Molecular functioni

  • adenylate cyclase binding Source: RGD
  • ATPase binding Source: RGD
  • protein kinase binding Source: RGD
  • scaffold protein binding Source: RGD

Protein-protein interaction databases

IntActiQ05941. 3 interactions.
STRINGi10116.ENSRNOP00000045255.

Chemistry

BindingDBiQ05941.

Structurei

3D structure databases

ProteinModelPortaliQ05941.
SMRiQ05941. Positions 227-261.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3645. Eukaryota.
ENOG410XQGR. LUCA.
HOGENOMiHOG000006756.
HOVERGENiHBG003756.
InParanoidiQ05941.
KOiK04809.
OMAiQGGVWLA.
OrthoDBiEOG72JWGV.
PhylomeDBiQ05941.

Family and domain databases

Gene3Di1.20.120.370. 2 hits.
2.70.170.10. 1 hit.
InterProiIPR027361. 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]
PANTHERiPTHR18945. PTHR18945. 3 hits.
PfamiPF02931. Neur_chan_LBD. 1 hit.
PF02932. Neur_chan_memb. 1 hit.
[Graphical view]
PRINTSiPR00254. NICOTINICR.
PR00252. NRIONCHANNEL.
SUPFAMiSSF63712. SSF63712. 1 hit.
SSF90112. SSF90112. 1 hit.
TIGRFAMsiTIGR00860. LIC. 1 hit.
PROSITEiPS00236. NEUROTR_ION_CHANNEL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q05941-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCGGRGGIWL ALAAALLHVS LQGEFQRRLY KELVKNYNPL ERPVANDSQP
60 70 80 90 100
LTVYFSLSLL QIMDVDEKNQ VLTTNIWLQM SWTDHYLQWN MSEYPGVKNV
110 120 130 140 150
RFPDGQIWKP DILLYNSADE RFDATFHTNV LVNASGHCQY LPPGIFKSSC
160 170 180 190 200
YIDVRWFPFD VQQCKLKFGS WSYGGWSLDL QMQEADISSY IPNGEWDLMG
210 220 230 240 250
IPGKRNEKFY ECCKEPYPDV TYTVTMRRRT LYYGLNLLIP CVLISALALL
260 270 280 290 300
VFLLPADSGE KISLGITVLL SLTVFMLLVA EIMPATSDSV PLIAQYFAST
310 320 330 340 350
MIIVGLSVVV TVIVLRYHHH DPDGGKMPKW TRIILLNWCA WFLRMKRPGE
360 370 380 390 400
DKVRPACQHK PRRCSLASVE LSAGAGPPTS NGNLLYIGFR GLEGMHCAPT
410 420 430 440 450
PDSGVVCGRL ACSPTHDEHL MHGAHPSDGD PDLAKILEEV RYIANRFRCQ
460 470 480 490 500
DESEVICSEW KFAACVVDRL CLMAFSVFTI ICTIGILMSA PNFVEAVSKD

FA
Length:502
Mass (Da):56,503
Last modified:May 1, 2007 - v2
Checksum:i289A30498C7B9A58
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti447 – 4471F → N in AAB25224 (PubMed:7678857).Curated
Sequence conflicti469 – 4691R → P in AAB25224 (PubMed:7678857).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S53987 mRNA. Translation: AAB25224.2.
L31619 mRNA. Translation: AAC33136.1.
AY574256 mRNA. Translation: AAS90352.1.
PIRiT01378.
RefSeqiNP_036964.3. NM_012832.3.
UniGeneiRn.9698.

Genome annotation databases

GeneIDi25302.
KEGGirno:25302.
UCSCiRGD:2348. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S53987 mRNA. Translation: AAB25224.2.
L31619 mRNA. Translation: AAC33136.1.
AY574256 mRNA. Translation: AAS90352.1.
PIRiT01378.
RefSeqiNP_036964.3. NM_012832.3.
UniGeneiRn.9698.

3D structure databases

ProteinModelPortaliQ05941.
SMRiQ05941. Positions 227-261.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ05941. 3 interactions.
STRINGi10116.ENSRNOP00000045255.

Chemistry

BindingDBiQ05941.
ChEMBLiCHEMBL2094110.
GuidetoPHARMACOLOGYi468.

PTM databases

iPTMnetiQ05941.
PhosphoSiteiQ05941.
SwissPalmiQ05941.

Proteomic databases

PaxDbiQ05941.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25302.
KEGGirno:25302.
UCSCiRGD:2348. rat.

Organism-specific databases

CTDi1139.
RGDi2348. Chrna7.

Phylogenomic databases

eggNOGiKOG3645. Eukaryota.
ENOG410XQGR. LUCA.
HOGENOMiHOG000006756.
HOVERGENiHBG003756.
InParanoidiQ05941.
KOiK04809.
OMAiQGGVWLA.
OrthoDBiEOG72JWGV.
PhylomeDBiQ05941.

Enzyme and pathway databases

ReactomeiR-RNO-629594. Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.

Miscellaneous databases

NextBioi606083.
PROiQ05941.

Family and domain databases

Gene3Di1.20.120.370. 2 hits.
2.70.170.10. 1 hit.
InterProiIPR027361. 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]
PANTHERiPTHR18945. PTHR18945. 3 hits.
PfamiPF02931. Neur_chan_LBD. 1 hit.
PF02932. Neur_chan_memb. 1 hit.
[Graphical view]
PRINTSiPR00254. NICOTINICR.
PR00252. NRIONCHANNEL.
SUPFAMiSSF63712. SSF63712. 1 hit.
SSF90112. SSF90112. 1 hit.
TIGRFAMsiTIGR00860. LIC. 1 hit.
PROSITEiPS00236. NEUROTR_ION_CHANNEL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RIC3.

Entry informationi

Entry nameiACHA7_RAT
AccessioniPrimary (citable) accession number: Q05941
Secondary accession number(s): Q53YK2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: May 1, 2007
Last modified: May 11, 2016
This is version 134 of the entry and version 2 of the sequence. [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

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.