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P20309

- ACM3_HUMAN

UniProt

P20309 - ACM3_HUMAN

Protein

Muscarinic acetylcholine receptor M3

Gene

CHRM3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 1 (01 Feb 1991)
      Previous versions | rss
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    Functioni

    The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover.1 Publication

    GO - Molecular functioni

    1. acetylcholine binding Source: UniProtKB
    2. drug binding Source: Ensembl
    3. G-protein coupled acetylcholine receptor activity Source: UniProtKB
    4. phosphatidylinositol phospholipase C activity Source: ProtInc
    5. protein binding Source: IntAct
    6. receptor activity Source: ProtInc

    GO - Biological processi

    1. cell proliferation Source: ProtInc
    2. cellular protein modification process Source: ProtInc
    3. energy reserve metabolic process Source: Reactome
    4. G-protein coupled acetylcholine receptor signaling pathway Source: UniProtKB
    5. G-protein coupled receptor signaling pathway Source: ProtInc
    6. nervous system development Source: ProtInc
    7. positive regulation of smooth muscle contraction Source: Ensembl
    8. regulation of insulin secretion Source: Reactome
    9. regulation of vascular smooth muscle contraction Source: Ensembl
    10. saliva secretion Source: InterPro
    11. signal transduction Source: ProtInc
    12. small molecule metabolic process Source: Reactome
    13. smooth muscle contraction Source: Ensembl

    Keywords - Molecular functioni

    G-protein coupled receptor, Receptor, Transducer

    Enzyme and pathway databases

    ReactomeiREACT_16943. Muscarinic acetylcholine receptors.
    REACT_18283. G alpha (q) signalling events.
    REACT_18405. Acetylcholine regulates insulin secretion.
    SignaLinkiP20309.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Muscarinic acetylcholine receptor M3
    Gene namesi
    Name:CHRM3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:1952. CHRM3.

    Subcellular locationi

    GO - Cellular componenti

    1. asymmetric synapse Source: Ensembl
    2. axon terminus Source: Ensembl
    3. basolateral plasma membrane Source: UniProtKB-SubCell
    4. cell junction Source: UniProtKB-KW
    5. dendrite Source: Ensembl
    6. integral component of plasma membrane Source: UniProtKB
    7. plasma membrane Source: Reactome
    8. postsynaptic membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Involvement in diseasei

    Eagle-Barrett syndrome (EGBRS) [MIM:100100]: A syndrome characterized by thin abdominal musculature with overlying lax skin, cryptorchism, megacystis with disorganized detrusor muscle, and urinary tract abnormalities.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi276 – 2761E → A: Loss of basolateral sorting. 1 Publication
    Mutagenesisi276 – 2761E → D: Loss of basolateral sorting. No effect on basolateral sorting; when associated with L-280 and L-281. 1 Publication
    Mutagenesisi280 – 2801F → A: Loss of basolateral sorting. 1 Publication
    Mutagenesisi280 – 2801F → L: No effect on basolateral sorting. 1 Publication
    Mutagenesisi281 – 2811V → A: Loss of basolateral sorting. 1 Publication
    Mutagenesisi281 – 2811V → L: No effect on basolateral sorting. 1 Publication

    Organism-specific databases

    MIMi100100. phenotype.
    Orphaneti2970. Prune belly syndrome.
    PharmGKBiPA112.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 590590Muscarinic acetylcholine receptor M3PRO_0000069029Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi5 – 51N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi6 – 61N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi15 – 151N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi41 – 411N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi48 – 481N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi141 ↔ 221PROSITE-ProRule annotation
    Disulfide bondi517 ↔ 520PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP20309.
    PaxDbiP20309.
    PRIDEiP20309.

    PTM databases

    PhosphoSiteiP20309.

    Expressioni

    Gene expression databases

    ArrayExpressiP20309.
    BgeeiP20309.
    CleanExiHS_CHRM3.
    GenevestigatoriP20309.

    Organism-specific databases

    HPAiCAB010409.
    HPA024106.

    Interactioni

    Subunit structurei

    Homodimer; the dimers can form tetramers.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NALCNQ8IZF03EBI-2687785,EBI-7085333

    Protein-protein interaction databases

    BioGridi107553. 4 interactions.
    DIPiDIP-44291N.
    IntActiP20309. 3 interactions.
    MINTiMINT-4953628.
    STRINGi9606.ENSP00000255380.

    Structurei

    Secondary structure

    1
    590
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi280 – 2834

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CSANMR-A271-289[»]
    ProteinModelPortaliP20309.
    SMRiP20309. Positions 64-559.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP20309.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 6767ExtracellularBy similarityAdd
    BLAST
    Topological domaini92 – 10413CytoplasmicBy similarityAdd
    BLAST
    Topological domaini131 – 14212ExtracellularBy similarityAdd
    BLAST
    Topological domaini165 – 18420CytoplasmicBy similarityAdd
    BLAST
    Topological domaini207 – 22923ExtracellularBy similarityAdd
    BLAST
    Topological domaini253 – 491239CytoplasmicBy similarityAdd
    BLAST
    Topological domaini515 – 52612ExtracellularBy similarityAdd
    BLAST
    Topological domaini547 – 59044CytoplasmicBy similarityAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei68 – 9124Helical; Name=1By similarityAdd
    BLAST
    Transmembranei105 – 13026Helical; Name=2By similarityAdd
    BLAST
    Transmembranei143 – 16422Helical; Name=3By similarityAdd
    BLAST
    Transmembranei185 – 20622Helical; Name=4By similarityAdd
    BLAST
    Transmembranei230 – 25223Helical; Name=5By similarityAdd
    BLAST
    Transmembranei492 – 51423Helical; Name=6By similarityAdd
    BLAST
    Transmembranei527 – 54620Helical; Name=7By similarityAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni148 – 1525Agonist bindingBy similarity
    Regioni507 – 53024Agonist bindingBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi275 – 2817Basolateral sorting signal

    Sequence similaritiesi

    Belongs to the G-protein coupled receptor 1 family. Muscarinic acetylcholine receptor subfamily. CHRM3 sub-subfamily.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG250863.
    HOGENOMiHOG000231484.
    HOVERGENiHBG105720.
    InParanoidiP20309.
    KOiK04131.
    OMAiIWQVVFI.
    OrthoDBiEOG7V49Z7.
    PhylomeDBiP20309.
    TreeFamiTF320495.

    Family and domain databases

    Gene3Di1.20.1070.10. 2 hits.
    InterProiIPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    IPR001183. Musac_Ach_M3_rcpt.
    IPR000995. Musac_Ach_rcpt.
    [Graphical view]
    PANTHERiPTHR24249:SF61. PTHR24249:SF61. 1 hit.
    PfamiPF00001. 7tm_1. 1 hit.
    [Graphical view]
    PRINTSiPR00237. GPCRRHODOPSN.
    PR00243. MUSCARINICR.
    PR00540. MUSCRINICM3R.
    PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
    PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P20309-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTLHNNSTTS PLFPNISSSW IHSPSDAGLP PGTVTHFGSY NVSRAAGNFS    50
    SPDGTTDDPL GGHTVWQVVF IAFLTGILAL VTIIGNILVI VSFKVNKQLK 100
    TVNNYFLLSL ACADLIIGVI SMNLFTTYII MNRWALGNLA CDLWLAIDYV 150
    ASNASVMNLL VISFDRYFSI TRPLTYRAKR TTKRAGVMIG LAWVISFVLW 200
    APAILFWQYF VGKRTVPPGE CFIQFLSEPT ITFGTAIAAF YMPVTIMTIL 250
    YWRIYKETEK RTKELAGLQA SGTEAETENF VHPTGSSRSC SSYELQQQSM 300
    KRSNRRKYGR CHFWFTTKSW KPSSEQMDQD HSSSDSWNNN DAAASLENSA 350
    SSDEEDIGSE TRAIYSIVLK LPGHSTILNS TKLPSSDNLQ VPEEELGMVD 400
    LERKADKLQA QKSVDDGGSF PKSFSKLPIQ LESAVDTAKT SDVNSSVGKS 450
    TATLPLSFKE ATLAKRFALK TRSQITKRKR MSLVKEKKAA QTLSAILLAF 500
    IITWTPYNIM VLVNTFCDSC IPKTFWNLGY WLCYINSTVN PVCYALCNKT 550
    FRTTFKMLLL CQCDKKKRRK QQYQQRQSVI FHKRAPEQAL 590
    Length:590
    Mass (Da):66,128
    Last modified:February 1, 1991 - v1
    Checksum:i5CB473C57B9526E9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti382 – 3843KLP → RLS in AAG30036. (PubMed:11238933)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti65 – 651V → I.
    Corresponds to variant rs2067481 [ dbSNP | Ensembl ].
    VAR_033461
    Natural varianti431 – 4311L → P.
    Corresponds to variant rs16839102 [ dbSNP | Ensembl ].
    VAR_049368

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15266 Genomic DNA. Translation: CAA33337.1.
    U29589 Genomic DNA. Translation: AAA70337.1.
    AB041395 Genomic DNA. Translation: BAA94480.1.
    AF498917 mRNA. Translation: AAM18940.1.
    AL356361 Genomic DNA. Translation: CAH72987.1.
    BC096844 mRNA. Translation: AAH96844.1.
    BC121026 mRNA. Translation: AAI21027.1.
    AF279779 mRNA. Translation: AAG30036.1.
    CCDSiCCDS1616.1.
    PIRiS10128.
    RefSeqiNP_000731.1. NM_000740.2.
    XP_005273089.1. XM_005273032.1.
    XP_005273090.1. XM_005273033.1.
    XP_005273091.1. XM_005273034.1.
    XP_006711795.1. XM_006711732.1.
    UniGeneiHs.155736.
    Hs.7138.

    Genome annotation databases

    EnsembliENST00000255380; ENSP00000255380; ENSG00000133019.
    GeneIDi1131.
    KEGGihsa:1131.
    UCSCiuc001hyp.3. human.

    Polymorphism databases

    DMDMi113125.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15266 Genomic DNA. Translation: CAA33337.1 .
    U29589 Genomic DNA. Translation: AAA70337.1 .
    AB041395 Genomic DNA. Translation: BAA94480.1 .
    AF498917 mRNA. Translation: AAM18940.1 .
    AL356361 Genomic DNA. Translation: CAH72987.1 .
    BC096844 mRNA. Translation: AAH96844.1 .
    BC121026 mRNA. Translation: AAI21027.1 .
    AF279779 mRNA. Translation: AAG30036.1 .
    CCDSi CCDS1616.1.
    PIRi S10128.
    RefSeqi NP_000731.1. NM_000740.2.
    XP_005273089.1. XM_005273032.1.
    XP_005273090.1. XM_005273033.1.
    XP_005273091.1. XM_005273034.1.
    XP_006711795.1. XM_006711732.1.
    UniGenei Hs.155736.
    Hs.7138.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CSA NMR - A 271-289 [» ]
    ProteinModelPortali P20309.
    SMRi P20309. Positions 64-559.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107553. 4 interactions.
    DIPi DIP-44291N.
    IntActi P20309. 3 interactions.
    MINTi MINT-4953628.
    STRINGi 9606.ENSP00000255380.

    Chemistry

    BindingDBi P20309.
    ChEMBLi CHEMBL245.
    DrugBanki DB00517. Anisotropine Methylbromide.
    DB00572. Atropine.
    DB00767. Benzquinamide.
    DB00185. Cevimeline.
    DB00785. Cryptenamine.
    DB01176. Cyclizine.
    DB00496. Darifenacin.
    DB00729. Diphemanil Methylsulfate.
    DB01231. Diphenidol.
    DB00725. Homatropine Methylbromide.
    DB01403. Methotrimeprazine.
    DB00340. Metixene.
    DB00334. Olanzapine.
    DB01062. Oxybutynin.
    DB00383. Oxyphencyclimine.
    DB00420. Promazine.
    DB01069. Promethazine.
    DB00777. Propiomazine.
    DB01591. Solifenacin.
    DB00372. Thiethylperazine.
    DB01409. Tiotropium.
    DB01036. Tolterodine.
    DB00505. Tridihexethyl.
    GuidetoPHARMACOLOGYi 15.

    Protein family/group databases

    GPCRDBi Search...

    PTM databases

    PhosphoSitei P20309.

    Polymorphism databases

    DMDMi 113125.

    Proteomic databases

    MaxQBi P20309.
    PaxDbi P20309.
    PRIDEi P20309.

    Protocols and materials databases

    DNASUi 1131.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000255380 ; ENSP00000255380 ; ENSG00000133019 .
    GeneIDi 1131.
    KEGGi hsa:1131.
    UCSCi uc001hyp.3. human.

    Organism-specific databases

    CTDi 1131.
    GeneCardsi GC01P239549.
    HGNCi HGNC:1952. CHRM3.
    HPAi CAB010409.
    HPA024106.
    MIMi 100100. phenotype.
    118494. gene.
    neXtProti NX_P20309.
    Orphaneti 2970. Prune belly syndrome.
    PharmGKBi PA112.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG250863.
    HOGENOMi HOG000231484.
    HOVERGENi HBG105720.
    InParanoidi P20309.
    KOi K04131.
    OMAi IWQVVFI.
    OrthoDBi EOG7V49Z7.
    PhylomeDBi P20309.
    TreeFami TF320495.

    Enzyme and pathway databases

    Reactomei REACT_16943. Muscarinic acetylcholine receptors.
    REACT_18283. G alpha (q) signalling events.
    REACT_18405. Acetylcholine regulates insulin secretion.
    SignaLinki P20309.

    Miscellaneous databases

    ChiTaRSi CHRM3. human.
    EvolutionaryTracei P20309.
    GeneWikii Muscarinic_acetylcholine_receptor_M3.
    GenomeRNAii 1131.
    NextBioi 4702.
    PROi P20309.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P20309.
    Bgeei P20309.
    CleanExi HS_CHRM3.
    Genevestigatori P20309.

    Family and domain databases

    Gene3Di 1.20.1070.10. 2 hits.
    InterProi IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    IPR001183. Musac_Ach_M3_rcpt.
    IPR000995. Musac_Ach_rcpt.
    [Graphical view ]
    PANTHERi PTHR24249:SF61. PTHR24249:SF61. 1 hit.
    Pfami PF00001. 7tm_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00237. GPCRRHODOPSN.
    PR00243. MUSCARINICR.
    PR00540. MUSCRINICM3R.
    PROSITEi PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
    PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Distinct primary structures, ligand-binding properties and tissue-specific expression of four human muscarinic acetylcholine receptors."
      Peralta E.G., Ashkenazi A., Winslow J.W., Smith D.H., Ramachandran J., Capon D.J.
      EMBO J. 6:3923-3929(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Cloning and expression of the human and rat m5 muscarinic acetylcholine receptor genes."
      Bonner T.I., Young A.C., Brann M.R., Buckley N.J.
      Neuron 1:403-410(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Human-specific amino acid changes found in 103 protein-coding genes."
      Kitano T., Liu Y.-H., Ueda S., Saitou N.
      Mol. Biol. Evol. 21:936-944(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
      Puhl H.L. III, Ikeda S.R., Aronstam R.S.
      Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    5. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. "Antisense promoter of human L1 retrotransposon drives transcription of adjacent cellular genes."
      Speek M.
      Mol. Cell. Biol. 21:1973-1985(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-384.
      Tissue: Teratocarcinoma.
    8. "Mutation of carboxyl-terminal threonine residues in human M3 muscarinic acetylcholine receptor modulates the extent of sequestration and desensitization."
      Yang J., Williams J.A., Yule D.I., Logsdon C.D.
      Mol. Pharmacol. 48:477-485(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. Cited for: INVOLVEMENT IN EGBRS.
    10. "The muscarinic M3 acetylcholine receptor exists as two differently sized complexes at the plasma membrane."
      Patowary S., Alvarez-Curto E., Xu T.R., Holz J.D., Oliver J.A., Milligan G., Raicu V.
      Biochem. J. 452:303-312(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, SUBCELLULAR LOCATION.
    11. "Identification and structural determination of the M(3) muscarinic acetylcholine receptor basolateral sorting signal."
      Iverson H.A., Fox D. III, Nadler L.S., Klevit R.E., Nathanson N.M.
      J. Biol. Chem. 280:24568-24575(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 271-289, MUTAGENESIS OF GLU-276; PHE-280 AND VAL-281, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiACM3_HUMAN
    AccessioniPrimary (citable) accession number: P20309
    Secondary accession number(s): Q0VAJ8
    , Q4QRI3, Q5VXY2, Q9HB60
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 152 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. 7-transmembrane G-linked receptors
      List of 7-transmembrane G-linked receptor entries
    2. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3