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Protein

Acetylcholine receptor subunit alpha

Gene

CHRNA1

Organism
Torpedo marmorata (Marbled electric ray)
Status
Reviewed-Annotation score: Annotation score: 4 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

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:
Acetylcholine receptor subunit alpha
Gene namesi
Name:CHRNA1
OrganismiTorpedo marmorata (Marbled electric ray)
Taxonomic identifieri7788 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataChondrichthyesElasmobranchiiBatoideaTorpediniformesTorpedinidaeTorpedo

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 234210ExtracellularAdd
BLAST
Transmembranei235 – 25925HelicalAdd
BLAST
Transmembranei267 – 28519HelicalAdd
BLAST
Transmembranei301 – 32020HelicalAdd
BLAST
Topological domaini321 – 432112CytoplasmicAdd
BLAST
Transmembranei433 – 45119HelicalAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Add
BLAST
Chaini25 – 461437Acetylcholine receptor subunit alphaPRO_0000000311Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi152 ↔ 166
Glycosylationi165 – 1651N-linked (GlcNAc...)Sequence analysis
Disulfide bondi216 ↔ 217Associated with receptor activation

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Pentamer of two alpha chains, and one each of the beta, delta, and gamma chains.1 Publication

Structurei

Secondary structure

1
461
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi210 – 2156Combined sources
Beta strandi218 – 2203Combined sources
Beta strandi222 – 2254Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L4WNMR-B206-226[»]
1LJZNMR-B206-226[»]
1OEDelectron microscopy4.00A/D235-461[»]
2BG9electron microscopy4.00A/D25-461[»]
4AQ5electron microscopy6.20A/D1-461[»]
4AQ9electron microscopy6.20A/D1-461[»]
4BOGelectron microscopy50.002/A/D/F/I/K/N/P/S/U/X/Z1-461[»]
4BOIelectron microscopy41.00A/D1-461[»]
4BONelectron microscopy40.00A/D1-461[»]
4BOOelectron microscopy42.00A/D1-461[»]
4BORelectron microscopy42.00A/D1-461[»]
4BOTelectron microscopy42.00A/D1-461[»]
ProteinModelPortaliP02711.
SMRiP02711. Positions 25-339, 427-461.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02711.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG003756.

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. 1 hit.
PfamiPF02931. Neur_chan_LBD. 1 hit.
PF02932. Neur_chan_memb. 2 hits.
[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.

P02711-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MILCSYWHVG LVLLLFSCCG LVLGSEHETR LVANLLENYN KVIRPVEHHT
60 70 80 90 100
HFVDITVGLQ LIQLINVDEV NQIVETNVRL RQQWIDVRLR WNPADYGGIK
110 120 130 140 150
KIRLPSDDVW LPDLVLYNNA DGDFAIVHMT KLLLDYTGKI MWTPPAIFKS
160 170 180 190 200
YCEIIVTHFP FDQQNCTMKL GIWTYDGTKV SISPESDRPD LSTFMESGEW
210 220 230 240 250
VMKDYRGWKH WVYYTCCPDT PYLDITYHFI MQRIPLYFVV NVIIPCLLFS
260 270 280 290 300
FLTVLVFYLP TDSGEKMTLS ISVLLSLTVF LLVIVELIPS TSSAVPLIGK
310 320 330 340 350
YMLFTMIFVI SSIIVTVVVI NTHHRSPSTH TMPQWVRKIF INTIPNVMFF
360 370 380 390 400
STMKRASKEK QENKIFADDI DISDISGKQV TGEVIFQTPL IKNPDVKSAI
410 420 430 440 450
EGVKYIAEHM KSDEESSNAA EEWKYVAMVI DHILLCVFML ICIIGTVSVF
460
AGRLIELSQE G
Length:461
Mass (Da):52,795
Last modified:July 21, 1986 - v1
Checksum:i5354B3F8451D4F8C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti347 – 3471V → L in AAA96704 (PubMed:6549423).Curated
Sequence conflicti448 – 4481S → C in AAA96704 (PubMed:6549423).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00963 mRNA. No translation available.
M25893 mRNA. Translation: AAA96704.1.
M14807 mRNA. Translation: AAA49273.1.
PIRiA93440.
I50548.
I50549.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00963 mRNA. No translation available.
M25893 mRNA. Translation: AAA96704.1.
M14807 mRNA. Translation: AAA49273.1.
PIRiA93440.
I50548.
I50549.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L4WNMR-B206-226[»]
1LJZNMR-B206-226[»]
1OEDelectron microscopy4.00A/D235-461[»]
2BG9electron microscopy4.00A/D25-461[»]
4AQ5electron microscopy6.20A/D1-461[»]
4AQ9electron microscopy6.20A/D1-461[»]
4BOGelectron microscopy50.002/A/D/F/I/K/N/P/S/U/X/Z1-461[»]
4BOIelectron microscopy41.00A/D1-461[»]
4BONelectron microscopy40.00A/D1-461[»]
4BOOelectron microscopy42.00A/D1-461[»]
4BORelectron microscopy42.00A/D1-461[»]
4BOTelectron microscopy42.00A/D1-461[»]
ProteinModelPortaliP02711.
SMRiP02711. Positions 25-339, 427-461.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG003756.

Miscellaneous databases

EvolutionaryTraceiP02711.

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. 1 hit.
PfamiPF02931. Neur_chan_LBD. 1 hit.
PF02932. Neur_chan_memb. 2 hits.
[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. "The molecular cloning and characterisation of cDNA coding for the alpha subunit of the acetylcholine receptor."
    Sumikawa K., Houghton M., Smith J.C., Bell L., Richards B.M., Barnard E.A.
    Nucleic Acids Res. 10:5809-5822(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-335 AND 341-411.
  2. "Complete mRNA coding sequence of the acetylcholine binding alpha-subunit of Torpedo marmorata acetylcholine receptor: a model for the transmembrane organization of the polypeptide chain."
    Devillers-Thiery A., Giraudat J., Bentaboulet M., Changeux J.-P.
    Proc. Natl. Acad. Sci. U.S.A. 80:2067-2071(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Molecular genetics of Torpedo marmorata acetylcholine receptor."
    Devillers-Thiery A., Giraudat J., Bentaboulet M., Klarsfeld A., Changeux J.-P.
    Adv. Exp. Med. Biol. 181:17-29(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Acetylcholine and GABA receptors: subunits of central and peripheral receptors and their encoding nucleic acids."
    Barnard E.A., Beeson D., Bilbe G., Brown D.A., Constanti A., Conti-Tronconi B.M., Dolly J.O., Dunn S.M.J., Mehraban F., Richards B.M., Smart T.G.
    Cold Spring Harb. Symp. Quant. Biol. 48:109-124(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-79.
  5. "Structure and gating mechanism of the acetylcholine receptor pore."
    Miyazawa A., Fujiyoshi Y., Unwin N.
    Nature 423:949-955(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.0 ANGSTROMS) OF 235-461.
  6. "The mechanism for acetylcholine receptor inhibition by alpha-neurotoxins and species-specific resistance to alpha-bungarotoxin revealed by NMR."
    Samson A.O., Scherf T., Eisenstein M., Chill J.H., Anglister J.
    Neuron 35:319-332(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 206-228 IN COMPLEX WITH ALPHA-BUNGAROTOXIN.

Entry informationi

Entry nameiACHA_TORMA
AccessioniPrimary (citable) accession number: P02711
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 14, 2015
This is version 121 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

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.