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P09690

- ACHB_MOUSE

UniProt

P09690 - ACHB_MOUSE

Protein

Acetylcholine receptor subunit beta

Gene

Chrnb1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    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

    1. acetylcholine-activated cation-selective channel activity Source: MGI
    2. acetylcholine binding Source: UniProtKB
    3. acetylcholine receptor activity Source: Ensembl
    4. protein binding Source: MGI

    GO - Biological processi

    1. behavioral response to nicotine Source: Ensembl
    2. muscle contraction Source: Ensembl
    3. muscle fiber development Source: Ensembl
    4. neurological system process Source: Ensembl
    5. neuromuscular synaptic transmission Source: Ensembl
    6. postsynaptic membrane organization Source: Ensembl
    7. regulation of membrane potential Source: MGI
    8. synaptic transmission, cholinergic Source: Ensembl

    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 beta
    Gene namesi
    Name:Chrnb1
    Synonyms:Acrb
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:87890. Chrnb1.

    Subcellular locationi

    GO - Cellular componenti

    1. acetylcholine-gated channel complex Source: MGI
    2. cell junction Source: UniProtKB-KW
    3. plasma membrane Source: MGI
    4. postsynaptic membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Add
    BLAST
    Chaini24 – 501478Acetylcholine receptor subunit betaPRO_0000000316Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi151 ↔ 165By similarity
    Glycosylationi164 – 1641N-linked (GlcNAc...)Sequence Analysis
    Modified residuei390 – 3901Phosphotyrosine; by Tyr-kinasesBy similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PRIDEiP09690.

    PTM databases

    PhosphoSiteiP09690.

    Expressioni

    Gene expression databases

    BgeeiP09690.
    GenevestigatoriP09690.

    Interactioni

    Subunit structurei

    Pentamer of two alpha chains, and one each of the beta, delta, and gamma (in immature muscle) or epsilon (in mature muscle) chains.

    Protein-protein interaction databases

    BioGridi197935. 1 interaction.
    IntActiP09690. 4 interactions.
    MINTiMINT-2983098.

    Structurei

    3D structure databases

    ProteinModelPortaliP09690.
    SMRiP09690. Positions 24-341, 435-500.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini24 – 244221ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini333 – 469137CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei245 – 26925HelicalSequence AnalysisAdd
    BLAST
    Transmembranei277 – 29519HelicalSequence AnalysisAdd
    BLAST
    Transmembranei311 – 33222HelicalSequence AnalysisAdd
    BLAST
    Transmembranei470 – 48819HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG243276.
    GeneTreeiENSGT00750000117375.
    HOGENOMiHOG000006757.
    HOVERGENiHBG003756.
    InParanoidiQ5F292.
    KOiK04812.
    OMAiFIDGPNR.
    OrthoDBiEOG70ZZN7.
    PhylomeDBiP09690.
    TreeFamiTF315605.

    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. 1 hit.
    [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.

    P09690-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALGALLLLL GVLGTPLAPG ARGSEAEGQL IKKLFSNYDS SVRPAREVGD    50
    RVGVSIGLTL AQLISLNEKD EEMSTKVYLD LEWTDYRLSW DPAEHDGIDS 100
    LRITAESVWL PDVVLLNNND GNFDVALDIN VVVSFEGSVR WQPPGLYRSS 150
    CSIQVTYFPF DWQNCTMVFS SYSYDSSEVS LKTGLDPEGE ERQEVYIHEG 200
    TFIENGQWEI IHKPSRLIQL PGDQRGGKEG HHEEVIFYLI IRRKPLFYLV 250
    NVIAPCILIT LLAIFVFYLP PDAGEKMGLS IFALLTLTVF LLLLADKVPE 300
    TSLAVPIIIK YLMFTMVLVT FSVILSVVVL NLHHRSPHTH QMPFWVRQIF 350
    IHKLPPYLGL KRPKPERDQL PEPHHSLSPR SGWGRGTDEY FIRKPPSDFL 400
    FPKLNRFQPE SSAPDLRRFI DGPTRAVGLP QELREVISSI SYMARQLQEQ 450
    EDHDALKEDW QFVAMVVDRL FLWTFIVFTS VGTLVIFLDA TYHLPPPEPF 500
    P 501
    Length:501
    Mass (Da):56,931
    Last modified:July 1, 1989 - v1
    Checksum:i787BDDA90EBB0EF2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14537 mRNA. Translation: AAA37154.1.
    J04699 Genomic DNA. Translation: AAA37156.1.
    AK087554 mRNA. Translation: BAC39924.1.
    AL603707 Genomic DNA. Translation: CAI51959.1.
    CCDSiCCDS24910.1.
    PIRiA33358. A25338.
    RefSeqiNP_033731.3. NM_009601.4.
    UniGeneiMm.86425.

    Genome annotation databases

    EnsembliENSMUST00000045971; ENSMUSP00000047270; ENSMUSG00000041189.
    GeneIDi11443.
    KEGGimmu:11443.
    UCSCiuc007jrq.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14537 mRNA. Translation: AAA37154.1 .
    J04699 Genomic DNA. Translation: AAA37156.1 .
    AK087554 mRNA. Translation: BAC39924.1 .
    AL603707 Genomic DNA. Translation: CAI51959.1 .
    CCDSi CCDS24910.1.
    PIRi A33358. A25338.
    RefSeqi NP_033731.3. NM_009601.4.
    UniGenei Mm.86425.

    3D structure databases

    ProteinModelPortali P09690.
    SMRi P09690. Positions 24-341, 435-500.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 197935. 1 interaction.
    IntActi P09690. 4 interactions.
    MINTi MINT-2983098.

    Chemistry

    BindingDBi P09690.
    ChEMBLi CHEMBL3038460.
    GuidetoPHARMACOLOGYi 471.

    PTM databases

    PhosphoSitei P09690.

    Proteomic databases

    PRIDEi P09690.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000045971 ; ENSMUSP00000047270 ; ENSMUSG00000041189 .
    GeneIDi 11443.
    KEGGi mmu:11443.
    UCSCi uc007jrq.2. mouse.

    Organism-specific databases

    CTDi 1140.
    MGIi MGI:87890. Chrnb1.

    Phylogenomic databases

    eggNOGi NOG243276.
    GeneTreei ENSGT00750000117375.
    HOGENOMi HOG000006757.
    HOVERGENi HBG003756.
    InParanoidi Q5F292.
    KOi K04812.
    OMAi FIDGPNR.
    OrthoDBi EOG70ZZN7.
    PhylomeDBi P09690.
    TreeFami TF315605.

    Miscellaneous databases

    NextBioi 278748.
    PROi P09690.
    SOURCEi Search...

    Gene expression databases

    Bgeei P09690.
    Genevestigatori P09690.

    Family and domain databases

    Gene3Di 1.20.120.370. 2 hits.
    2.70.170.10. 1 hit.
    InterProi IPR027361. 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 ]
    PANTHERi PTHR18945. PTHR18945. 1 hit.
    Pfami PF02931. Neur_chan_LBD. 1 hit.
    PF02932. Neur_chan_memb. 1 hit.
    [Graphical view ]
    PRINTSi PR00254. NICOTINICR.
    PR00252. NRIONCHANNEL.
    SUPFAMi SSF63712. SSF63712. 1 hit.
    SSF90112. SSF90112. 1 hit.
    TIGRFAMsi TIGR00860. LIC. 1 hit.
    PROSITEi PS00236. NEUROTR_ION_CHANNEL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.

    Entry informationi

    Entry nameiACHB_MOUSE
    AccessioniPrimary (citable) accession number: P09690
    Secondary accession number(s): Q5F292
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 134 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

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3