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P04758 (ACHB_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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

Names and origin

Protein namesRecommended name:
Acetylcholine receptor subunit beta
Gene names
Name:CHRNB1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length505 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 (in immature muscle) or epsilon (in mature muscle) chains.

Subcellular location

Cell junctionsynapsepostsynaptic 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]

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentCell junction
Cell membrane
Membrane
Postsynaptic cell membrane
Synapse
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionIon channel
Ligand-gated ion channel
Receptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbehavioral response to nicotine

Inferred from sequence or structural similarity. Source: UniProtKB

cation transport

Inferred from sequence or structural similarity. Source: UniProtKB

muscle contraction

Inferred from sequence or structural similarity. Source: UniProtKB

muscle fiber development

Inferred from sequence or structural similarity. Source: UniProtKB

neuromuscular synaptic transmission

Inferred from sequence or structural similarity. Source: UniProtKB

postsynaptic membrane organization

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of membrane potential

Inferred from electronic annotation. Source: Compara

signal transduction

Inferred from sequence or structural similarity. Source: UniProtKB

synaptic transmission, cholinergic

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentacetylcholine-gated channel complex

Inferred from sequence or structural similarity. Source: UniProtKB

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

synapse

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionacetylcholine binding

Inferred from electronic annotation. Source: Compara

acetylcholine receptor activity

Inferred from electronic annotation. Source: Compara

acetylcholine-activated cation-selective channel activity

Inferred from electronic annotation. Source: Compara

channel activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424
Chain25 – 505481Acetylcholine receptor subunit beta
PRO_0000000314

Regions

Topological domain25 – 245221Extracellular Potential
Transmembrane246 – 27025Helical; Potential
Transmembrane278 – 29518Helical; Potential
Transmembrane312 – 33322Helical; Potential
Topological domain334 – 473140Cytoplasmic Potential
Transmembrane474 – 49219Helical; Potential

Amino acid modifications

Modified residue3941Phosphotyrosine; by Tyr-kinases By similarity
Glycosylation1651N-linked (GlcNAc...) Potential
Disulfide bond152 ↔ 166 By similarity

Sequences

Sequence LengthMass (Da)Tools
P04758 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: B003D552A6701ECC

FASTA50557,352
        10         20         30         40         50         60 
MTPGALLLLL LGVLGAHLAP GARGSEAEGR LREKLFSGYD STVRPAREVG DRVWVSIGLT 

        70         80         90        100        110        120 
LAQLISLNEK DEEMSTKVYL DLEWTDYRLS WDPEEHEGID SLRISAESVW LPDVVLLNNN 

       130        140        150        160        170        180 
DGNFDVALDI NVVVSSDGSM RWQPPGIYRS SCSIQVTYFP FDWQNCTMVF SSYSYDSSEV 

       190        200        210        220        230        240 
SLQTGLSPEG QERQEVYIHE GTFIENGQWE IIHKPSRLIQ PSVDPRGGGE GRREEVTFYL 

       250        260        270        280        290        300 
IIRRKPLFYL VNVIAPCILI TLLAIFVFYL PPDAGEKMGL SIFALLTLTV FLLLLADKVP 

       310        320        330        340        350        360 
ETSLSVPIII KYLMFTMVLV TFSVILSVVV LNLHHRSPHT HQMPLWVRQI FIHKLPLYLG 

       370        380        390        400        410        420 
LKRPKPERDQ MQEPPSIAPR DSPGSGWGRG TDEYFIRKPP NDFLFPKPNR FQPELSAPDL 

       430        440        450        460        470        480 
RRFIDGPNRA VGLPPELREV VSSISYIARQ LQEQEDHDVL KEDWQFVAMV VDRLFLWTFI 

       490        500 
IFTSVGTLVI FLDATYHLPP ADPFP 

« Hide

References

« Hide 'large scale' references
[1]"Primary structure of beta subunit precursor of calf muscle acetylcholine receptor deduced from cDNA sequence."
Tanabe T., Noda M., Furutani Y., Takai T., Takahashi H., Tanaka K., Hirose T., Inayama S., Numa S.
Eur. J. Biochem. 144:11-17(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Thymus.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X00962 mRNA. Translation: CAA25475.1.
BC147876 mRNA. Translation: AAI47877.1.
IPIIPI00691448.
PIRS07227.
RefSeqNP_776941.1. NM_174516.2.
UniGeneBt.5107.

3D structure databases

ProteinModelPortalP04758.
SMRP04758. Positions 25-342.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000025624; ENSBTAP00000025624; ENSBTAG00000019242.
GeneID282179.
KEGGbta:282179.

Organism-specific databases

CTD1140.

Phylogenomic databases

eggNOGNOG243276.
GeneTreeENSGT00620000087691.
HOGENOMHOG000006757.
HOVERGENHBG003756.
InParanoidP04758.
KOK04812.
OMAFIDGPNR.
OrthoDBEOG4DFPNC.

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

NextBio20806008.

Entry information

Entry nameACHB_BOVIN
AccessionPrimary (citable) accession number: P04758
Secondary accession number(s): A6QL86
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: April 3, 2013
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families