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Protein

Neuronal acetylcholine receptor subunit alpha-7

Gene

CHRNA7

Organism
Gallus gallus (Chicken)
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-activated cation-selective channel activity Source: UniProtKB
  • acetylcholine binding Source: UniProtKB
  • acetylcholine receptor activity Source: UniProtKB
  • beta-amyloid binding Source: UniProtKB
  • chloride channel regulator activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • toxic substance binding Source: UniProtKB

GO - Biological processi

  • activation of MAPK activity Source: UniProtKB
  • calcium ion transport Source: UniProtKB
  • cellular calcium ion homeostasis Source: UniProtKB
  • cognition Source: UniProtKB
  • negative regulation of tumor necrosis factor production Source: UniProtKB
  • positive regulation of angiogenesis Source: UniProtKB
  • positive regulation of cell proliferation Source: UniProtKB
  • response to hypoxia Source: UniProtKB
  • response to nicotine Source: UniProtKB
  • signal transduction Source: UniProtKB
  • synaptic transmission, cholinergic Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Ligand-gated ion channel, Receptor

Keywords - Biological processi

Ion transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Neuronal acetylcholine receptor subunit alpha-7
Gene namesi
Name:CHRNA7
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 230207ExtracellularAdd
BLAST
Transmembranei231 – 25525HelicalAdd
BLAST
Transmembranei262 – 28019HelicalAdd
BLAST
Transmembranei296 – 31722HelicalAdd
BLAST
Topological domaini318 – 469152CytoplasmicAdd
BLAST
Transmembranei470 – 49021HelicalAdd
BLAST

GO - Cellular componenti

  • acetylcholine-gated channel complex Source: UniProtKB
  • axon Source: AgBase
  • cell junction Source: UniProtKB-KW
  • cytoplasm Source: AgBase
  • dendrite Source: AgBase
  • perikaryon Source: AgBase
  • plasma membrane Source: UniProtKB
  • postsynaptic membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi270 – 2701L → S or T: Suppresses inhibition by the open-channel blocker QX-222. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23231 PublicationAdd
BLAST
Chaini24 – 502479Neuronal acetylcholine receptor subunit alpha-7PRO_0000000370Add
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

PaxDbiP22770.

PTM databases

iPTMnetiP22770.
SwissPalmiP22770.

Expressioni

Developmental stagei

Alpha-7 transcripts transiently accumulate in the developing optic tectum between E5 and E16.

Interactioni

Subunit structurei

Forms a homooligomeric channel blocked by alpha-bungarotoxin. The structure is probably pentameric (By similarity).By similarity

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

IntActiP22770. 1 interaction.
STRINGi9031.ENSGALP00000006509.

Structurei

Secondary structure

1
502
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi215 – 2173Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KC4NMR-B201-219[»]
1KL8NMR-B201-219[»]
1OL3model-A/B/C/D/E24-230[»]
1OL4model-A/B24-230[»]
1OL8model-A/B24-230[»]
1OL9model-A/B24-230[»]
ProteinModelPortaliP22770.
SMRiP22770. Positions 227-261.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22770.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3645. Eukaryota.
ENOG410XQGR. LUCA.
HOGENOMiHOG000006756.
HOVERGENiHBG003756.
InParanoidiP22770.
PhylomeDBiP22770.

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.

P22770-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLRALMLWL LAAAGLVRES LQGEFQRKLY KELLKNYNPL ERPVANDSQP
60 70 80 90 100
LTVYFTLSLM QIMDVDEKNQ VLTTNIWLQM YWTDHYLQWN VSEYPGVKNV
110 120 130 140 150
RFPDGLIWKP DILLYNSADE RFDATFHTNV LVNSSGHCQY LPPGIFKSSC
160 170 180 190 200
YIDVRWFPFD VQKCNLKFGS WTYGGWSLDL QMQEADISGY ISNGEWDLVG
210 220 230 240 250
IPGKRTESFY ECCKEPYPDI TFTVTMRRRT LYYGLNLLIP CVLISALALL
260 270 280 290 300
VFLLPADSGE KISLGITVLL SLTVFMLLVA EIMPATSDSV PLIAQYFAST
310 320 330 340 350
MIIVGLSVVV TVIVLQYHHH DPDGGKMPKW TRVILLNWCA WFLRMKRPGE
360 370 380 390 400
DKVRPACQHK QRRCSLSSME MNTVSGQQCS NGNMLYIGFR GLDGVHCTPT
410 420 430 440 450
TDSGVICGRM TCSPTEEENL LHSGHPSEGD PDLAKILEEV RYIANRFRDQ
460 470 480 490 500
DEEEAICNEW KFAASVVDRL CLMAFSVFTI ICTIGILMSA PNFVEAVSKD

FA
Length:502
Mass (Da):56,947
Last modified:August 1, 1991 - v1
Checksum:i572325D4309AD2FD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68586 mRNA. Translation: CAA48576.1.
X52295 mRNA. Translation: CAA36543.1.
X68246 Genomic DNA. Translation: CAA48317.1.
PIRiJN0113.
UniGeneiGga.4000.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68586 mRNA. Translation: CAA48576.1.
X52295 mRNA. Translation: CAA36543.1.
X68246 Genomic DNA. Translation: CAA48317.1.
PIRiJN0113.
UniGeneiGga.4000.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KC4NMR-B201-219[»]
1KL8NMR-B201-219[»]
1OL3model-A/B/C/D/E24-230[»]
1OL4model-A/B24-230[»]
1OL8model-A/B24-230[»]
1OL9model-A/B24-230[»]
ProteinModelPortaliP22770.
SMRiP22770. Positions 227-261.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP22770. 1 interaction.
STRINGi9031.ENSGALP00000006509.

PTM databases

iPTMnetiP22770.
SwissPalmiP22770.

Proteomic databases

PaxDbiP22770.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG3645. Eukaryota.
ENOG410XQGR. LUCA.
HOGENOMiHOG000006756.
HOVERGENiHBG003756.
InParanoidiP22770.
PhylomeDBiP22770.

Miscellaneous databases

EvolutionaryTraceiP22770.
PROiP22770.

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...

Entry informationi

Entry nameiACHA7_CHICK
AccessioniPrimary (citable) accession number: P22770
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: July 6, 2016
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.