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InterPro: IPR000995 Muscarinic acetylcholine receptor

Protein matchesHelp
UniProtKB
Matches:
139 proteins
AccessionHelp IPR000995 Musac_rcpt
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR000276 7TM GPCR, rhodopsin-like
Children IPR000502 Muscarinic acetylcholine receptor M5
IPR001065 Muscarinic acetylcholine receptor M2
IPR001183 Muscarinic acetylcholine receptor M3
IPR001432 Muscarinic acetylcholine receptor M4
IPR002228 Muscarinic acetylcholine receptor M1
GO Term annotationHelp
Function GO:0004981 muscarinic acetylcholine receptor activity
Component GO:0016020 membrane
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

G-protein-coupled receptors, GPCRs, constitute a vast protein family that encompasses a wide range of functions (including various autocrine, paracrine and endocrine processes). They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups. We use the term clan to describe the GPCRs, as they embrace a group of families for which there are indications of evolutionary relationship, but between which there is no statistically significant similarity in sequence [1]. The currently known clan members include the rhodopsin-like GPCRs, the secretin-like GPCRs, the cAMP receptors, the fungal mating pheromone receptors, and the metabotropic glutamate receptor family. There is a specialised database for GPCRs (http://www.gpcr.org/7tm/).

The rhodopsin-like GPCRs themselves represent a widespread protein family that includes hormone, neurotransmitter and light receptors, all of which transduce extracellular signals through interaction with guanine nucleotide-binding (G) proteins. Although their activating ligands vary widely in structure and character, the amino acid sequences of the receptors are very similar and are believed to adopt a common structural framework comprising 7 transmembrane (TM) helices [2, 3, 4].

The muscarinic acetylcholine receptors, present in the central nervous system, spinal cord motoneurons and autonomic preganglia, modulate a variety of physiological functions: these include airway, eye and intestinal smooth muscle contractions; heart rate; and glandular secretions. The receptors mediate adenylate cyclase attenuation, calcium and potassium channel activation, and phosphatidyl inositol turnover [5]. This diversity may result from the occurrence of multiple receptor subtypes, which have been classified based on observed differences in ligand binding to receptors in membranes from several tissues.

Database linksHelp
Blocks: IPB000995

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR000995 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P04761 Muscarinic acetylcholine receptor M1

P12657 Muscarinic acetylcholine receptor M1

P16395 Muscarinic acetylcholine receptor DM1

P20309 Muscarinic acetylcholine receptor M3

Q09388 Probable muscarinic acetylcholine receptor gar-2

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR000276 7TM GPCR, rhodopsin-like
IPR017452 GPCR, rhodopsin-like superfamily
IPR001183 Muscarinic acetylcholine receptor M3
IPR000995 Muscarinic acetylcholine receptor
IPR002228 Muscarinic acetylcholine receptor M1
SWISS-MODEL
PDB Chain
ModBase

PublicationsHelp
1. Attwood TK, Findlay JB.
Fingerprinting G-protein-coupled receptors.
Protein Eng. 7 195-203 1994 [PubMed: 8170923]
http://dx.doi.org/10.1093/protein/7.2.195
2. Birnbaumer L.
G proteins in signal transduction.
Annu. Rev. Pharmacol. Toxicol. 30 675-705 1990 [PubMed: 2111655]
http://dx.doi.org/10.1146/annurev.pa.30.040190.003331
3. Casey PJ, Gilman AG.
G protein involvement in receptor-effector coupling.
J. Biol. Chem. 263 2577-80 1988 [PubMed: 2830256]
http://intl.jbc.org/cgi/content/abstract/263/6/2577
4. Attwood TK, Findlay JB.
Design of a discriminating fingerprint for G-protein-coupled receptors.
Protein Eng. 6 167-76 1993 [PubMed: 8386361]
http://dx.doi.org/10.1093/protein/6.2.167
5. Kerlavage AR, Fraser CM, Chung FZ, Venter JC.
Molecular structure and evolution of adrenergic and cholinergic receptors.
Proteins 1 287-301 1986 [PubMed: 3329731]
http://dx.doi.org/10.1002/prot.340010403

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InterPro 23.1