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1.A.9.1.1
Nicotinic acetylcholine-activated cation-selective channel, pentameric α2βγδ (immature muscle) nα2βγδ (mature muscle). A  combination of symmetric and asymmetric motions opens the gate, and the asymmetric motion involves tilting of the TM2 helices (Szarecka et al. 2007). Acetylcholine receptor δ subunit mutations underlie a fast-channel myasthenic syndrome and arthrogryposis multiplex congenita (Brownlow et al., 2001; Webster et al., 2012). Residues in TMS2 and the cytoplasmic loop linking TMSs 3 and 4 influence conductance, selectivity, gating and desensitization (Peters et al., 2010). nAChR and TRPC channel proteins (1.A.4) mediate nicotine addiction in many animals from humans to worms (Feng et al., 2006). Cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor have been identified (Baier et al., 2011). Allosteric modulators of the α4β2 subtype of neuronal nicotinic acetylcholine receptors, the dominant type in the brain, are numerous (Pandya and Yakel, 2011).  α2β2 and α4βnicotinic acetylcholine receptors are inhibited by the β-amyloid(1-42) peptide (Pandya and Yakel, 2011b).  The A272E mutation in the alpha7 subunit gives rise to spinosad insensitivity without affecting activation by acetylcholine (Puinean et al. 2012). Inhibited by general anaesthetics (Nury et al., 2011). The X-ray crystal structures of the extracellular domain of the monomeric state of human neuronal alpha9 nicotinic acetylcholine receptor (nAChR) and of its complexes with the antagonists methyllycaconitine and alpha-bungarotoxin have been determined at resolutions of 1.8 A, 1.7 A and 2.7 A, respectively (Zouridakis et al. 2014).  Structurally similar allosteric modulators of α7 nAChR exhibit five different pharmacological effects (Gill-Thind et al. 2015).  Mutations causing slow-channel myasthenia show that a valine ring in the channel is optimized for stabilizing gating (Shen et al. 2016).  Quinoline derivatives act as agonists or antagonists depending on the type and subunit (Manetti et al. 2016). Conformational changes stabilize a twisted extracellular domain to promote transmembrane helix tilting, gate dilation, and the formation of a ""bubble"" that collapses to initiate ion conduction (Gupta et al. 2016). A high-affinity cholesterol-binding domain has been proposed for this and other ligand-gated ion channels (Di Scala et al. 2017). Positive allosteric modulators have been identified (Deba et al. 2018). Menthol stereoisomers exhibit fifferent effects on alpha4beta2 nAChR upregulation and dopamine neuron spontaneous firing (Henderson et al. 2019).

Accession Number:P07510
Protein Name:Acetylcholine receptor subunit gamma
Length:517
Molecular Weight:57883.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:4
Location1 / Topology2 / Orientation3: Cell junction1 / Multi-pass membrane protein2
Substrate inorganic cations

Cross database links:

Genevestigator: P07510
eggNOG: prNOG10027
HEGENOM: HBG387619
Drugbank: Drugbank Link   

External Searches:

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  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MHGGQGPLLL LLLLAVCLGA QGRNQEERLL ADLMQNYDPN LRPAERDSDV VNVSLKLTLT 
61:	NLISLNEREE ALTTNVWIEM QWCDYRLRWD PRDYEGLWVL RVPSTMVWRP DIVLENNVDG 
121:	VFEVALYCNV LVSPDGCIYW LPPAIFRSAC SISVTYFPFD WQNCSLIFQS QTYSTNEIDL 
181:	QLSQEDGQTI EWIFIDPEAF TENGEWAIQH RPAKMLLDPA APAQEAGHQK VVFYLLIQRK 
241:	PLFYVINIIA PCVLISSVAI LIHFLPAKAG GQKCTVAINV LLAQTVFLFL VAKKVPETSQ 
301:	AVPLISKYLT FLLVVTILIV VNAVVVLNVS LRSPHTHSMA RGVRKVFLRL LPQLLRMHVR 
361:	PLAPAAVQDT QSRLQNGSSG WSITTGEEVA LCLPRSELLF QQWQRQGLVA AALEKLEKGP 
421:	ELGLSQFCGS LKQAAPAIQA CVEACNLIAC ARHQQSHFDN GNEEWFLVGR VLDRVCFLAM 
481:	LSLFICGTAG IFLMAHYNRV PALPFPGDPR PYLPSPD