P02718 (ACHD_TORCA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetylcholine receptor subunit delta

Gene names

Name:

CHNRD

Organism

Torpedo californica (Pacific electric ray)

Taxonomic identifier

7787 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Chondrichthyes › Elasmobranchii › Batoidea › Torpediniformes › Torpedinidae › Torpedo

Protein attributes

Sequence length	522 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subunit structure	Pentamer of two alpha chains, and one each of the beta, delta, and gamma chains.
Subcellular location	Cell junction › synapse › postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily. [View classification]

Ontologies

Keywords
Biological process	Ion transport Transport
Cellular component	Cell junction Cell membrane Membrane Postsynaptic cell membrane Synapse
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Ion channel Ligand-gated ion channel Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Cellular_component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell postsynaptic membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	acetylcholine-activated cation-selective channel activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Chain

22 – 522

501

Acetylcholine receptor subunit delta

PRO_0000000326

Regions

Topological domain

22 – 245

224

Extracellular

Transmembrane

246 – 270

25

Helical

Transmembrane

278 – 295

18

Helical

Transmembrane

312 – 333

22

Helical

Topological domain

334 – 476

143

Cytoplasmic

Transmembrane

477 – 497

21

Helical

Amino acid modifications

Modified residue

393

1

Phosphotyrosine; by Tyr-kinases Ref.3

Glycosylation

91

1

N-linked (GlcNAc...) Potential

Glycosylation

164

1

N-linked (GlcNAc...) Ref.2

Glycosylation

229

1

N-linked (GlcNAc...) Potential

Disulfide bond

151 ↔ 165

Ref.2

Secondary structure

1

.

.

.

522

Helix Strand Turn

Details...

Helix

277 – 297

21

Sequences

	Sequence		Length	Mass (Da)
	P02718 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 568CF9C3D3E91E28	FASTA	522	59,891
	10 20 30 40 50 60 MGNIHFVYLL ISCLYYSGCS GVNEEERLIN DLLIVNKYNK HVRPVKHNNE VVNIALSLTL 70 80 90 100 110 120 SNLISLKETD ETLTSNVWMD HAWYDHRLTW NASEYSDISI LRLPPELVWI PDIVLQNNND 130 140 150 160 170 180 GQYHVAYFCN VLVRPNGYVT WLPPAIFRSS CPINVLYFPF DWQNCSLKFT ALNYDANEIT 190 200 210 220 230 240 MDLMTDTIDG KDYPIEWIII DPEAFTENGE WEIIHKPAKK NIYPDKFPNG TNYQDVTFYL 250 260 270 280 290 300 IIRRKPLFYV INFITPCVLI SFLASLAFYL PAESGEKMST AISVLLAQAV FLLLTSQRLP 310 320 330 340 350 360 ETALAVPLIG KYLMFIMSLV TGVIVNCGIV LNFHFRTPST HVLSTRVKQI FLEKLPRILH 370 380 390 400 410 420 MSRADESEQP DWQNDLKLRR SSSVGYISKA QEYFNIKSRS ELMFEKQSER HGLVPRVTPR 430 440 450 460 470 480 IGFGNNNENI AASDQLHDEI KSGIDSTNYI VKQIKEKNAY DEEVGNWNLV GQTIDRLSMF 490 500 510 520 IITPVMVLGT IFIFVMGNFN HPPAKPFEGD PFDYSSDHPR CA

References

[1]	"Primary structures of beta- and delta-subunit precursors of Torpedo californica acetylcholine receptor deduced from cDNA sequences." Noda M., Takahashi H., Tanabe T., Toyosato M., Kikyotani S., Hirose T., Asai M., Takashima H., Inayama S., Miyata T., Numa S. Nature 301:251-255(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Assessment of the number of free cysteines and isolation and identification of cystine-containing peptides from acetylcholine receptor." Kellaris K.V., Ware D.K., Smith S., Kyte J. Biochemistry 28:3469-3482(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 125-134 AND 139-145, GLYCOSYLATION AT ASN-164, DISULFIDE BOND.
[3]	"Determination of the tyrosine phosphorylation sites of the nicotinic acetylcholine receptor." Wagner K., Edson K., Heginbotham L., Post M., Huganir R.L., Czernik A.J. J. Biol. Chem. 266:23784-23789(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-393.
[4]	"Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy." Opella S.J., Marassi F.M., Gesell J.J., Valente A.P., Kim Y., Oblatt-Montal M., Montal M. Nat. Struct. Biol. 6:374-379(1999) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 276-298.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J00965 mRNA. Translation: AAA49275.1.

PIR

ACRYD1. A03177.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EQ8	NMR	-	A/B/C/D/E	276-298	[»]
1LK1	model	-	B	23-246	[»]
1OED	electron microscopy	4.00	C	246-505	[»]
1OLK	model	-	D	24-246	[»]

ProteinModelPortal

P02718.

SMR

P02718. Positions 22-505.

ModBase

Search...

PTM databases

GlycoSuiteDB

P02718.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

HOVERGEN

HBG003756.

Family and domain databases

Gene3D

2.70.170.10. 1 hit.

InterPro

IPR006202. Neur_chan_lig-bd.
IPR006201. Neur_channel.
IPR006029. Neurotrans-gated_channel_TM.
IPR018000. Neurotransmitter_ion_chnl_CS.
IPR002394. Nicotinic_acetylcholine_rcpt.
[Graphical view]

PANTHER

PTHR18945. PTHR18945. 1 hit.

Pfam

PF02931. Neur_chan_LBD. 1 hit.
PF02932. Neur_chan_memb. 1 hit.
[Graphical view]

PRINTS

PR00254. NICOTINICR.
PR00252. NRIONCHANNEL.

SUPFAM

SSF90112. Neu_channel_TM. 1 hit.
SSF63712. Neur_chan_LBD. 1 hit.

TIGRFAMs

TIGR00860. LIC. 1 hit.

PROSITE

PS00236. NEUROTR_ION_CHANNEL. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P02718.

ChEMBL

CHEMBL3916.

EvolutionaryTrace

P02718.

Entry information

Entry name

ACHD_TORCA

Accession

Primary (citable) accession number: P02718

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	April 3, 2013
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program