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Protein

Muscarinic acetylcholine receptor M3

Gene

Chrm3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.3 Publications

GO - Molecular functioni

  • acetylcholine binding Source: UniProtKB
  • drug binding Source: RGD
  • G-protein coupled acetylcholine receptor activity Source: UniProtKB

GO - Biological processi

  • G-protein coupled acetylcholine receptor signaling pathway Source: UniProtKB
  • positive regulation of smooth muscle contraction Source: RGD
  • regulation of vascular smooth muscle contraction Source: RGD
  • regulation of vasoconstriction Source: RGD
  • saliva secretion Source: InterPro
  • smooth muscle contraction Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

ReactomeiR-RNO-390648. Muscarinic acetylcholine receptors.
R-RNO-416476. G alpha (q) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
Muscarinic acetylcholine receptor M3
Gene namesi
Name:Chrm3
Synonyms:Chrm-3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 17

Organism-specific databases

RGDi2343. Chrm3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6666Extracellular1 PublicationAdd
BLAST
Transmembranei67 – 9024Helical; Name=1Add
BLAST
Topological domaini91 – 10313Cytoplasmic1 PublicationAdd
BLAST
Transmembranei104 – 12926Helical; Name=2Add
BLAST
Topological domaini130 – 14112Extracellular1 PublicationAdd
BLAST
Transmembranei142 – 16322Helical; Name=3Add
BLAST
Topological domaini164 – 18320Cytoplasmic1 PublicationAdd
BLAST
Transmembranei184 – 20522Helical; Name=4Add
BLAST
Topological domaini206 – 22823Extracellular1 PublicationAdd
BLAST
Transmembranei229 – 25123Helical; Name=5Add
BLAST
Topological domaini252 – 490239Cytoplasmic1 PublicationAdd
BLAST
Transmembranei491 – 51323Helical; Name=6Add
BLAST
Topological domaini514 – 52512Extracellular1 PublicationAdd
BLAST
Transmembranei526 – 54520Helical; Name=7Add
BLAST
Topological domaini546 – 58944Cytoplasmic1 PublicationAdd
BLAST

GO - Cellular componenti

  • asymmetric synapse Source: RGD
  • axon terminus Source: RGD
  • basolateral plasma membrane Source: UniProtKB-SubCell
  • cell junction Source: UniProtKB-KW
  • dendrite Source: RGD
  • integral component of plasma membrane Source: UniProtKB
  • plasma membrane Source: RGD
  • postsynaptic membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi148 – 1481Y → A: Decreased affinity for acetylcholine. 1 Publication
Mutagenesisi231 – 2311T → A: Decreased affinity for acetylcholine. 1 Publication
Mutagenesisi234 – 2341T → A: Strongly decreased affinity for acetylcholine. 2 Publications
Mutagenesisi506 – 5061Y → F: Decreased affinity for acetylcholine. 2 Publications
Mutagenesisi529 – 5291Y → F: Decreased affinity for acetylcholine. 1 Publication
Mutagenesisi533 – 5331Y → F: Decreased affinity for acetylcholine. 1 Publication

Chemistry

ChEMBLiCHEMBL1907609.
GuidetoPHARMACOLOGYi15.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 589589Muscarinic acetylcholine receptor M3PRO_0000069034Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi6 – 61N-linked (GlcNAc...)Sequence analysis
Glycosylationi15 – 151N-linked (GlcNAc...)Sequence analysis
Glycosylationi41 – 411N-linked (GlcNAc...)Sequence analysis
Glycosylationi48 – 481N-linked (GlcNAc...)Sequence analysis
Glycosylationi52 – 521N-linked (GlcNAc...)Sequence analysis
Disulfide bondi140 ↔ 220PROSITE-ProRule annotation1 Publication
Modified residuei384 – 3841PhosphoserineBy similarity
Disulfide bondi516 ↔ 519PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP08483.
PRIDEiP08483.

PTM databases

PhosphoSiteiP08483.

Expressioni

Gene expression databases

GenevisibleiP08483. RN.

Interactioni

Subunit structurei

Homodimer; the dimers can form tetramers.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Camk2aP112752EBI-7946407,EBI-2640645

Protein-protein interaction databases

IntActiP08483. 1 interaction.
STRINGi10116.ENSRNOP00000067435.

Chemistry

BindingDBiP08483.

Structurei

Secondary structure

1
589
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi65 – 9430Combined sources
Helixi96 – 983Combined sources
Helixi102 – 11817Combined sources
Helixi120 – 12910Combined sources
Beta strandi130 – 1323Combined sources
Helixi137 – 17034Combined sources
Beta strandi173 – 1753Combined sources
Turni176 – 1783Combined sources
Helixi181 – 21030Combined sources
Helixi223 – 2253Combined sources
Helixi228 – 23811Combined sources
Helixi240 – 25314Combined sources
Helixi255 – 2573Combined sources
Helixi483 – 50220Combined sources
Helixi504 – 51310Combined sources
Beta strandi517 – 5193Combined sources
Helixi522 – 53312Combined sources
Helixi535 – 54410Combined sources
Helixi548 – 5569Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AMKmodel-A56-560[»]
4DAJX-ray3.40A/B/C/D57-259[»]
A/B/C/D482-589[»]
4U14X-ray3.57A57-259[»]
A482-563[»]
4U15X-ray2.80A/B57-259[»]
A/B482-563[»]
4U16X-ray3.70A/B57-259[»]
A/B482-563[»]
ProteinModelPortaliP08483.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni147 – 1515Agonist bindingCurated
Regioni506 – 52924Agonist bindingCuratedAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi274 – 2807Basolateral sorting signalBy similarity

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

eggNOGiKOG4220. Eukaryota.
ENOG410YCQR. LUCA.
GeneTreeiENSGT00780000121874.
HOGENOMiHOG000231484.
HOVERGENiHBG105720.
InParanoidiP08483.
KOiK04131.
OMAiTHLGSYN.
OrthoDBiEOG7V49Z7.
PhylomeDBiP08483.
TreeFamiTF320495.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR001183. Musac_Ach_M3_rcpt.
IPR000995. Musac_Ach_rcpt.
[Graphical view]
PANTHERiPTHR24249:SF61. PTHR24249:SF61. 3 hits.
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR00243. MUSCARINICR.
PR00540. MUSCRINICM3R.
SMARTiSM01381. 7TM_GPCR_Srsx. 1 hit.
[Graphical view]
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P08483-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLHSNSTTS PLFPNISSSW VHSPSEAGLP LGTVTQLGSY NISQETGNFS
60 70 80 90 100
SNDTSSDPLG GHTIWQVVFI AFLTGFLALV TIIGNILVIV AFKVNKQLKT
110 120 130 140 150
VNNYFLLSLA CADLIIGVIS MNLFTTYIIM NRWALGNLAC DLWLSIDYVA
160 170 180 190 200
SNASVMNLLV ISFDRYFSIT RPLTYRAKRT TKRAGVMIGL AWVISFVLWA
210 220 230 240 250
PAILFWQYFV GKRTVPPGEC FIQFLSEPTI TFGTAIAAFY MPVTIMTILY
260 270 280 290 300
WRIYKETEKR TKELAGLQAS GTEAEAENFV HPTGSSRSCS SYELQQQGVK
310 320 330 340 350
RSSRRKYGRC HFWFTTKSWK PSAEQMDQDH SSSDSWNNND AAASLENSAS
360 370 380 390 400
SDEEDIGSET RAIYSIVLKL PGHSSILNST KLPSSDNLQV SNEDLGTVDV
410 420 430 440 450
ERNAHKLQAQ KSMGDGDNCQ KDFTKLPIQL ESAVDTGKTS DTNSSADKTT
460 470 480 490 500
ATLPLSFKEA TLAKRFALKT RSQITKRKRM SLIKEKKAAQ TLSAILLAFI
510 520 530 540 550
ITWTPYNIMV LVNTFCDSCI PKTYWNLGYW LCYINSTVNP VCYALCNKTF
560 570 580
RTTFKTLLLC QCDKRKRRKQ QYQQRQSVIF HKRVPEQAL
Length:589
Mass (Da):66,066
Last modified:November 1, 1988 - v1
Checksum:i9A5EF2FA653C830A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti184 – 1841A → R in AAA40661 (PubMed:3037705).Curated
Sequence conflicti184 – 1841A → R in AAA40662 (PubMed:3037705).Curated
Sequence conflicti184 – 1841A → R in BAA36839 (PubMed:9972520).Curated
Sequence conflicti516 – 5161C → R in AAA40659 (PubMed:3120722).Curated
Sequence conflicti556 – 5561T → M in AAA40659 (PubMed:3120722).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16407 mRNA. Translation: AAA40661.1.
M16408 Genomic DNA. Translation: AAA40662.1.
M18088 mRNA. Translation: AAA40659.1.
M62826 Genomic DNA. Translation: AAA41553.1.
AB017656 mRNA. Translation: BAA36839.1.
PIRiA29476.
B94518. B29514.
RefSeqiNP_036659.2. NM_012527.2.
XP_008769912.1. XM_008771690.1.
UniGeneiRn.87735.

Genome annotation databases

EnsembliENSRNOT00000075651; ENSRNOP00000067435; ENSRNOG00000049410.
GeneIDi24260.
KEGGirno:24260.
UCSCiRGD:2343. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16407 mRNA. Translation: AAA40661.1.
M16408 Genomic DNA. Translation: AAA40662.1.
M18088 mRNA. Translation: AAA40659.1.
M62826 Genomic DNA. Translation: AAA41553.1.
AB017656 mRNA. Translation: BAA36839.1.
PIRiA29476.
B94518. B29514.
RefSeqiNP_036659.2. NM_012527.2.
XP_008769912.1. XM_008771690.1.
UniGeneiRn.87735.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AMKmodel-A56-560[»]
4DAJX-ray3.40A/B/C/D57-259[»]
A/B/C/D482-589[»]
4U14X-ray3.57A57-259[»]
A482-563[»]
4U15X-ray2.80A/B57-259[»]
A/B482-563[»]
4U16X-ray3.70A/B57-259[»]
A/B482-563[»]
ProteinModelPortaliP08483.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP08483. 1 interaction.
STRINGi10116.ENSRNOP00000067435.

Chemistry

BindingDBiP08483.
ChEMBLiCHEMBL1907609.
GuidetoPHARMACOLOGYi15.

Protein family/group databases

GPCRDBiSearch...

PTM databases

PhosphoSiteiP08483.

Proteomic databases

PaxDbiP08483.
PRIDEiP08483.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000075651; ENSRNOP00000067435; ENSRNOG00000049410.
GeneIDi24260.
KEGGirno:24260.
UCSCiRGD:2343. rat.

Organism-specific databases

CTDi1131.
RGDi2343. Chrm3.

Phylogenomic databases

eggNOGiKOG4220. Eukaryota.
ENOG410YCQR. LUCA.
GeneTreeiENSGT00780000121874.
HOGENOMiHOG000231484.
HOVERGENiHBG105720.
InParanoidiP08483.
KOiK04131.
OMAiTHLGSYN.
OrthoDBiEOG7V49Z7.
PhylomeDBiP08483.
TreeFamiTF320495.

Enzyme and pathway databases

ReactomeiR-RNO-390648. Muscarinic acetylcholine receptors.
R-RNO-416476. G alpha (q) signalling events.

Miscellaneous databases

PROiP08483.

Gene expression databases

GenevisibleiP08483. RN.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR001183. Musac_Ach_M3_rcpt.
IPR000995. Musac_Ach_rcpt.
[Graphical view]
PANTHERiPTHR24249:SF61. PTHR24249:SF61. 3 hits.
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR00243. MUSCARINICR.
PR00540. MUSCRINICM3R.
SMARTiSM01381. 7TM_GPCR_Srsx. 1 hit.
[Graphical view]
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Identification of a family of muscarinic acetylcholine receptor genes."
    Bonner T.I., Buckley N.J., Young A.C., Brann M.R.
    Science 237:527-532(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  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: SEQUENCE REVISION TO 184.
  3. "A novel subtype of muscarinic receptor identified by homology screening."
    Braun T., Schofield P.R., Shivers B.D., Pritchett D.B., Seeburg P.H.
    Biochem. Biophys. Res. Commun. 149:125-132(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  4. "Molecular cloning of m3 muscarinic acetylcholine receptor in rat iris."
    Furuta M., Ohya S., Imaizumi Y., Watanabe M.
    J. Smooth Muscle Res. 34:111-122(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Iris.
  5. "Muscarinic acetylcholine receptors. Peptide sequencing identifies residues involved in antagonist binding and disulfide bond formation."
    Kurtenbach E., Curtis C.A.M., Pedder E.K., Aitken A., Harris A.C.M., Hulme E.C.
    J. Biol. Chem. 265:13702-13708(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 104-166.
  6. "Site-directed mutagenesis of the m3 muscarinic receptor: identification of a series of threonine and tyrosine residues involved in agonist but not antagonist binding."
    Wess J., Gdula D., Brann M.R.
    EMBO J. 10:3729-3734(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TYR-148; THR-231; THR-234; TYR-506; TYR-529 AND TYR-533, FUNCTION, SUBCELLULAR LOCATION.
  7. "Role of conserved threonine and tyrosine residues in acetylcholine binding and muscarinic receptor activation. A study with m3 muscarinic receptor point mutants."
    Wess J., Maggio R., Palmer J.R., Vogel Z.
    J. Biol. Chem. 267:19313-19319(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF THR-234 AND TYR-506, FUNCTION, SUBCELLULAR LOCATION.
  8. Cited for: X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 57-589 IN COMPLEX WITH THE INVERSE AGONIST TIOTROPIUM, FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, DISULFIDE BOND.

Entry informationi

Entry nameiACM3_RAT
AccessioniPrimary (citable) accession number: P08483
Secondary accession number(s): Q9QWK9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: November 1, 1988
Last modified: June 8, 2016
This is version 147 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.