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P02712 (ACHB_TORCA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Acetylcholine receptor subunit beta
Gene names
Name:CHRNB1
OrganismTorpedo californica (Pacific electric ray)
Taxonomic identifier7787 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Chondrichthyes › Elasmobranchii › Batoidea › Torpediniformes › Torpedinidae › Torpedo

Protein attributes

Sequence length493 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. Beta-1/CHRNB1 sub-subfamily. [View classification]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.2
Chain25 – 493469Acetylcholine receptor subunit beta
PRO_0000000319

Regions

Topological domain25 – 240216Extracellular Potential
Transmembrane241 – 26525Helical; Potential
Transmembrane273 – 29119Helical; Potential
Transmembrane307 – 32822Helical; Potential
Topological domain329 – 461133Cytoplasmic Potential
Transmembrane462 – 48019Helical; Potential

Amino acid modifications

Modified residue3791Phosphotyrosine; by Tyr-kinases Ref.4
Glycosylation1651N-linked (GlcNAc...) Ref.3
Disulfide bond152 ↔ 166 Ref.3

Natural variations

Natural variant31N → D in a second clone.
Natural variant111L → V in a second clone.

Experimental info

Sequence conflict751T → R AA sequence Ref.2

Secondary structure

1 ........................................... 493
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02712 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 4E145192584D8F5F

FASTA49356,156
        10         20         30         40         50         60 
MENVRRMALG LVVMMALALS GVGASVMEDT LLSVLFETYN PKVRPAQTVG DKVTVRVGLT 

        70         80         90        100        110        120 
LTNLLILNEK IEEMTTNVFL NLAWTDYRLQ WDPAAYEGIK DLRIPSSDVW QPDIVLMNNN 

       130        140        150        160        170        180 
DGSFEITLHV NVLVQHTGAV SWQPSAIYRS SCTIKVMYFP FDWQNCTMVF KSYTYDTSEV 

       190        200        210        220        230        240 
TLQHALDAKG EREVKEIVIN KDAFTENGQW SIEHKPSRKN WRSDDPSYED VTFYLIIQRK 

       250        260        270        280        290        300 
PLFYIVYTII PCILISILAI LVFYLPPDAG EKMSLSISAL LAVTVFLLLL ADKVPETSLS 

       310        320        330        340        350        360 
VPIIIRYLMF IMILVAFSVI LSVVVLNLHH RSPNTHTMPN WIRQIFIETL PPFLWIQRPV 

       370        380        390        400        410        420 
TTPSPDSKPT IISRANDEYF IRKPAGDFVC PVDNARVAVQ PERLFSEMKW HLNGLTQPVT 

       430        440        450        460        470        480 
LPQDLKEAVE AIKYIAEQLE SASEFDDLKK DWQYVAMVAD RLFLYVFFVI CSIGTFSIFL 

       490 
DASHNVPPDN PFA

« Hide

References

[1]"Primary structures of beta- and delta-subunit precursors of Torpedo californica acetylcholine receptor deduced from cDNA sequences."
Noda M., Takahashi H., Tanabe T., Toyosato M., Kikyotani S., Hirose T., Asai M., Takashima H., Inayama S., Miyata T., Numa S.
Nature 301:251-255(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Acetylcholine receptor: complex of homologous subunits."
Raftery M.A., Hunkapiller M.W., Strader C.D., Hood L.E.
Science 208:1454-1457(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-78.
[3]"Assessment of the number of free cysteines and isolation and identification of cystine-containing peptides from acetylcholine receptor."
Kellaris K.V., Ware D.K., Smith S., Kyte J.
Biochemistry 28:3469-3482(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 126-147, GLYCOSYLATION AT ASN-165, DISULFIDE BOND.
[4]"Determination of the tyrosine phosphorylation sites of the nicotinic acetylcholine receptor."
Wagner K., Edson K., Heginbotham L., Post M., Huganir R.L., Czernik A.J.
J. Biol. Chem. 266:23784-23789(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-379.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J00964 mRNA. Translation: AAA49274.1.
PIRACRYB1. A93294.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LK1model-G26-241[»]
1OEDelectron microscopy4.00B241-490[»]
1OLKmodel-E23-241[»]
ProteinModelPortalP02712.
SMRP02712. Positions 25-493.
ModBaseSearch...

PTM databases

GlycoSuiteDBP02712.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG003756.

Family and domain databases

Gene3D2.70.170.10. 1 hit.
InterProIPR006202. Neur_chan_lig-bd.
IPR006201. Neur_channel.
IPR006029. Neurotrans-gated_channel_TM.
IPR018000. Neurotransmitter_ion_chnl_CS.
IPR002394. Nicotinic_acetylcholine_rcpt.
[Graphical view]
PANTHERPTHR18945. PTHR18945. 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

BindingDBP02712.
ChEMBLCHEMBL3803.
EvolutionaryTraceP02712.

Entry information

Entry nameACHB_TORCA
AccessionPrimary (citable) accession number: P02712
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 3, 2013
This is version 102 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

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