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P09690 (ACHB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. 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

Names and origin

Protein namesRecommended name:
Acetylcholine receptor subunit beta
Gene names
Name:Chrnb1
Synonyms:Acrb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length501 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 electronic annotation. Source: Ensembl

muscle contraction

Inferred from electronic annotation. Source: Ensembl

muscle fiber development

Inferred from electronic annotation. Source: Ensembl

neurological system process

Inferred from electronic annotation. Source: Ensembl

neuromuscular synaptic transmission

Inferred from electronic annotation. Source: Ensembl

postsynaptic membrane organization

Inferred from electronic annotation. Source: Ensembl

regulation of membrane potential

Inferred from genetic interaction PubMed 2383398PubMed 8798466. Source: MGI

synaptic transmission, cholinergic

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentacetylcholine-gated channel complex

Inferred from direct assay PubMed 8798466. Source: MGI

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from direct assay PubMed 12388596. Source: MGI

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionacetylcholine binding

Inferred from mutant phenotype PubMed 8872460. Source: UniProtKB

acetylcholine receptor activity

Inferred from electronic annotation. Source: Ensembl

acetylcholine-activated cation-selective channel activity

Inferred from genetic interaction PubMed 8798466. Source: MGI

protein binding

Inferred from physical interaction PubMed 8798466. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323
Chain24 – 501478Acetylcholine receptor subunit beta
PRO_0000000316

Regions

Topological domain24 – 244221Extracellular Potential
Transmembrane245 – 26925Helical; Potential
Transmembrane277 – 29519Helical; Potential
Transmembrane311 – 33222Helical; Potential
Topological domain333 – 469137Cytoplasmic Potential
Transmembrane470 – 48819Helical; Potential

Amino acid modifications

Modified residue3901Phosphotyrosine; by Tyr-kinases By similarity
Glycosylation1641N-linked (GlcNAc...) Potential
Disulfide bond151 ↔ 165 By similarity

Sequences

Sequence LengthMass (Da)Tools
P09690 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 787BDDA90EBB0EF2

FASTA50156,931
        10         20         30         40         50         60 
MALGALLLLL GVLGTPLAPG ARGSEAEGQL IKKLFSNYDS SVRPAREVGD RVGVSIGLTL 

        70         80         90        100        110        120 
AQLISLNEKD EEMSTKVYLD LEWTDYRLSW DPAEHDGIDS LRITAESVWL PDVVLLNNND 

       130        140        150        160        170        180 
GNFDVALDIN VVVSFEGSVR WQPPGLYRSS CSIQVTYFPF DWQNCTMVFS SYSYDSSEVS 

       190        200        210        220        230        240 
LKTGLDPEGE ERQEVYIHEG TFIENGQWEI IHKPSRLIQL PGDQRGGKEG HHEEVIFYLI 

       250        260        270        280        290        300 
IRRKPLFYLV NVIAPCILIT LLAIFVFYLP PDAGEKMGLS IFALLTLTVF LLLLADKVPE 

       310        320        330        340        350        360 
TSLAVPIIIK YLMFTMVLVT FSVILSVVVL NLHHRSPHTH QMPFWVRQIF IHKLPPYLGL 

       370        380        390        400        410        420 
KRPKPERDQL PEPHHSLSPR SGWGRGTDEY FIRKPPSDFL FPKLNRFQPE SSAPDLRRFI 

       430        440        450        460        470        480 
DGPTRAVGLP QELREVISSI SYMARQLQEQ EDHDALKEDW QFVAMVVDRL FLWTFIVFTS 

       490        500 
VGTLVIFLDA TYHLPPPEPF P 

« Hide

References

« Hide 'large scale' references
[1]"A universal oligonucleotide probe for acetylcholine receptor genes. Selection and sequencing of cDNA clones for the mouse muscle beta subunit."
Buonanno A., Mudd J., Shah V., Merlie J.P.
J. Biol. Chem. 261:16451-16458(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Isolation and characterization of the beta and epsilon subunit genes of mouse muscle acetylcholine receptor."
Buonanno A., Mudd J., Merlie J.P.
J. Biol. Chem. 264:7611-7616(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Eye.
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M14537 mRNA. Translation: AAA37154.1.
J04699 Genomic DNA. Translation: AAA37156.1.
AK087554 mRNA. Translation: BAC39924.1.
AL603707 Genomic DNA. Translation: CAI51959.1.
CCDSCCDS24910.1.
PIRA25338. A33358.
RefSeqNP_033731.3. NM_009601.4.
UniGeneMm.86425.

3D structure databases

ProteinModelPortalP09690.
SMRP09690. Positions 24-341, 435-500.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid197935. 1 interaction.
IntActP09690. 4 interactions.
MINTMINT-2983098.

Chemistry

BindingDBP09690.
ChEMBLCHEMBL3038460.
GuidetoPHARMACOLOGY471.

PTM databases

PhosphoSiteP09690.

Proteomic databases

PRIDEP09690.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000045971; ENSMUSP00000047270; ENSMUSG00000041189.
GeneID11443.
KEGGmmu:11443.
UCSCuc007jrq.2. mouse.

Organism-specific databases

CTD1140.
MGIMGI:87890. Chrnb1.

Phylogenomic databases

eggNOGNOG243276.
GeneTreeENSGT00750000117375.
HOGENOMHOG000006757.
HOVERGENHBG003756.
InParanoidQ5F292.
KOK04812.
OMAFIDGPNR.
OrthoDBEOG70ZZN7.
PhylomeDBP09690.
TreeFamTF315605.

Gene expression databases

BgeeP09690.
GenevestigatorP09690.

Family and domain databases

Gene3D1.20.120.370. 2 hits.
2.70.170.10. 1 hit.
InterProIPR027361. 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]
PANTHERPTHR18945. PTHR18945. 1 hit.
PfamPF02931. Neur_chan_LBD. 1 hit.
PF02932. Neur_chan_memb. 1 hit.
[Graphical view]
PRINTSPR00254. NICOTINICR.
PR00252. NRIONCHANNEL.
SUPFAMSSF63712. SSF63712. 1 hit.
SSF90112. SSF90112. 1 hit.
TIGRFAMsTIGR00860. LIC. 1 hit.
PROSITEPS00236. NEUROTR_ION_CHANNEL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio278748.
PROP09690.
SOURCESearch...

Entry information

Entry nameACHB_MOUSE
AccessionPrimary (citable) accession number: P09690
Secondary accession number(s): Q5F292
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: July 9, 2014
This is version 133 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot