TCDB is operated by the Saier Lab Bioinformatics Group
« See all members of the family


1.A.9.1.9
The cation-selective pentameric nicotinic acetylcholine receptor, nAChR, with α (461 aas; P02710), β (493 aas; P02712), γ (506 aas; P02714) and δ (522 aas; P02718) subunits.  The transmembrane domain of the uncoupled nAChR adopts a conformation distinct from that of the resting or desensitized state (Sun et al. 2016).  Studies with this receptor have been reviewed (Unwin 2013).  Many small molecules interact with nAChRs including d-tubocurarine, snake venom protein α-bungarotoxin (α-Bgt), and α-conotoxins, neurotoxic peptides from Conus snails. Various more recently discovered compounds of different structural classes also interact with nAChRs including the low-molecular weight alkaloids, pibocin, varacin and makaluvamines C and G. 6-Bromohypaphorine from the mollusk Hermissenda crassicornis does not bind to Torpedo nAChR but behaves as an agonist on human α7 nAChR (Kudryavtsev et al. 2015). Dimethylaniline mimics the low potency and non-competitive actions of lidocaine on nAChRs, as opposed to the high potency and voltage-dependent block by lidocaine (Alberola-Die et al. 2016).  Cholesterol is a potent modulator of the Torpedo nAChR (Baenziger et al. 2017). Cholesterol may play a mechanical role by conferring local rigidity to the membrane so that there is productive coupling between the extracellular and membrane domains, leading to opening of the channel (Unwin 2017).

Accession Number:P02718
Protein Name:Acetylcholine receptor subunit delta
Length:522
Molecular Weight:59891.00
Species:Tetronarce californica (Pacific electric ray) [7787]
Number of TMSs:4
Location1 / Topology2 / Orientation3: Cell junction1 / Multi-pass membrane protein2
Substrate ions

Cross database links:

Structure:
1oed   4aq5     

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
Window Size: Angle:  
Window Size: Angle:  
FASTA formatted sequence
1:	MGNIHFVYLL ISCLYYSGCS GVNEEERLIN DLLIVNKYNK HVRPVKHNNE VVNIALSLTL 
61:	SNLISLKETD ETLTSNVWMD HAWYDHRLTW NASEYSDISI LRLPPELVWI PDIVLQNNND 
121:	GQYHVAYFCN VLVRPNGYVT WLPPAIFRSS CPINVLYFPF DWQNCSLKFT ALNYDANEIT 
181:	MDLMTDTIDG KDYPIEWIII DPEAFTENGE WEIIHKPAKK NIYPDKFPNG TNYQDVTFYL 
241:	IIRRKPLFYV INFITPCVLI SFLASLAFYL PAESGEKMST AISVLLAQAV FLLLTSQRLP 
301:	ETALAVPLIG KYLMFIMSLV TGVIVNCGIV LNFHFRTPST HVLSTRVKQI FLEKLPRILH 
361:	MSRADESEQP DWQNDLKLRR SSSVGYISKA QEYFNIKSRS ELMFEKQSER HGLVPRVTPR 
421:	IGFGNNNENI AASDQLHDEI KSGIDSTNYI VKQIKEKNAY DEEVGNWNLV GQTIDRLSMF 
481:	IITPVMVLGT IFIFVMGNFN HPPAKPFEGD PFDYSSDHPR CA