Skip Header

Contribute Send feedback
Read comments (?) or add your own

P02711 (ACHA_TORMA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 103. 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetylcholine receptor subunit alpha
Gene names
Name:CHRNA1
OrganismTorpedo marmorata (Marbled electric ray)
Taxonomic identifier7788 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Chondrichthyes › Elasmobranchii › Squalea › Hypnosqualea › Pristiorajea › Batoidea › Torpediniformes › Torpedinoidei › Torpedinidae › Torpedo

Protein attributes

Sequence length461 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.

Subunit structure

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

Subcellular location

Cell junction › synapse › postsynaptic 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-1/CHRNA1 sub-subfamily. [View classification]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424
Chain25 – 461437Acetylcholine receptor subunit alpha
PRO_0000000311

Regions

Topological domain25 – 234210Extracellular
Transmembrane235 – 25925Helical
Transmembrane267 – 28519Helical
Transmembrane301 – 32020Helical
Topological domain321 – 432112Cytoplasmic
Transmembrane433 – 45119Helical

Amino acid modifications

Glycosylation1651N-linked (GlcNAc...) Potential
Disulfide bond152 ↔ 166
Disulfide bond216 ↔ 217Associated with receptor activation

Experimental info

Sequence conflict3471V → L in AAA96704. Ref.3
Sequence conflict4481S → C in AAA96704. Ref.3

Secondary structure

1 .............................................. 461
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02711 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 5354B3F8451D4F8C

FASTA46152,795
        10         20         30         40         50         60 
MILCSYWHVG LVLLLFSCCG LVLGSEHETR LVANLLENYN KVIRPVEHHT HFVDITVGLQ 

        70         80         90        100        110        120 
LIQLINVDEV NQIVETNVRL RQQWIDVRLR WNPADYGGIK KIRLPSDDVW LPDLVLYNNA 

       130        140        150        160        170        180 
DGDFAIVHMT KLLLDYTGKI MWTPPAIFKS YCEIIVTHFP FDQQNCTMKL GIWTYDGTKV 

       190        200        210        220        230        240 
SISPESDRPD LSTFMESGEW VMKDYRGWKH WVYYTCCPDT PYLDITYHFI MQRIPLYFVV 

       250        260        270        280        290        300 
NVIIPCLLFS FLTVLVFYLP TDSGEKMTLS ISVLLSLTVF LLVIVELIPS TSSAVPLIGK 

       310        320        330        340        350        360 
YMLFTMIFVI SSIIVTVVVI NTHHRSPSTH TMPQWVRKIF INTIPNVMFF STMKRASKEK 

       370        380        390        400        410        420 
QENKIFADDI DISDISGKQV TGEVIFQTPL IKNPDVKSAI EGVKYIAEHM KSDEESSNAA 

       430        440        450        460 
EEWKYVAMVI DHILLCVFML ICIIGTVSVF AGRLIELSQE G

« Hide

References

[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: 6183641] [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: 6572962] [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: 6549423] [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: 6327147] [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: 12827192] [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: 12160749] [Abstract]
Cited for: STRUCTURE BY NMR OF 206-228 IN COMPLEX WITH ALPHA-BUNGAROTOXIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J00963 mRNA. No translation available.
M25893 mRNA. Translation: AAA96704.1.
M14807 mRNA. Translation: AAA49273.1.
PIRA93440.
I50548.
I50549.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1L4WNMR-B206-226[»]
1LJZNMR-B206-226[»]
1OEDelectron microscopy4.00A/D235-461[»]
2BG9electron microscopy4.00A/D25-461[»]
ProteinModelPortalP02711.
SMRP02711. Positions 25-339, 427-461.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG003756.

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.
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...

Entry information

Entry nameACHA_TORMA
AccessionPrimary (citable) accession number: P02711
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 25, 2012
This is version 103 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents