P02714 (ACHG_TORCA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetylcholine receptor subunit gamma

Gene names

Name:

CHRNG

Organism

Torpedo californica (Pacific electric ray)

Taxonomic identifier

7787 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Chondrichthyes › Elasmobranchii › Squalea › Hypnosqualea › Pristiorajea › Batoidea › Torpediniformes › Torpedinoidei › Torpedinidae › Torpedo

Protein attributes

Sequence length	506 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.
Post-translational modification	Seems not to be glycosylated on Asn-158.
Sequence similarities	Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Gamma/CHRNG sub-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	Ionic 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 receptor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

17

Chain

18 – 506

489

Acetylcholine receptor subunit gamma

PRO_0000000338

Regions

Topological domain

18 – 235

218

Extracellular

Transmembrane

236 – 260

25

Helical

Transmembrane

269 – 287

19

Helical

Transmembrane

303 – 324

22

Helical

Topological domain

325 – 466

142

Cytoplasmic

Transmembrane

467 – 490

24

Helical

Amino acid modifications

Modified residue

381

1

Phosphotyrosine; by Tyr-kinases Ref.4

Glycosylation

85

1

N-linked (GlcNAc...) Potential

Disulfide bond

145 ↔ 159

Ref.3

Experimental info

Sequence conflict

298

1

P → S in CAA24682. Ref.2

Secondary structure

1

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506

Helix Strand Turn

Details...

Helix

21 – 31

11

Beta strand

41 – 45

5

Beta strand

47 – 61

15

Turn

62 – 65

4

Beta strand

66 – 78

13

Turn

80 – 82

3

Beta strand

88 – 91

4

Beta strand

93 – 98

6

Helix

99 – 101

3

Beta strand

107 – 109

3

Beta strand

114 – 116

3

Beta strand

124 – 128

5

Beta strand

131 – 135

5

Beta strand

138 – 144

7

Turn

153 – 155

3

Beta strand

157 – 167

11

Helix

170 – 172

3

Beta strand

174 – 176

3

Beta strand

189 – 192

4

Turn

194 – 198

5

Beta strand

200 – 205

6

Beta strand

208 – 214

7

Beta strand

217 – 219

3

Beta strand

222 – 234

13

Sequences

	Sequence		Length	Mass (Da)
	P02714 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 48A5F5D82BC66C9D	FASTA	506	58,164
	10 20 30 40 50 60 MVLTLLLIIC LALEVRSENE EGRLIEKLLG DYDKRIIPAK TLDHIIDVTL KLTLTNLISL 70 80 90 100 110 120 NEKEEALTTN VWIEIQWNDY RLSWNTSEYE GIDLVRIPSE LLWLPDVVLE NNVDGQFEVA 130 140 150 160 170 180 YYANVLVYND GSMYWLPPAI YRSTCPIAVT YFPFDWQNCS LVFRSQTYNA HEVNLQLSAE 190 200 210 220 230 240 EGEAVEWIHI DPEDFTENGE WTIRHRPAKK NYNWQLTKDD TDFQEIIFFL IIQRKPLFYI 250 260 270 280 290 300 INIIAPCVLI SSLVVLVYFL PAQAGGQKCT LSISVLLAQT IFLFLIAQKV PETSLNVPLI 310 320 330 340 350 360 GKYLIFVMFV SMLIVMNCVI VLNVSLRTPN THSLSEKIKH LFLGFLPKYL GMQLEPSEET 370 380 390 400 410 420 PEKPQPRRRS SFGIMIKAEE YILKKPRSEL MFEEQKDRHG LKRVNKMTSD IDIGTTVDLY 430 440 450 460 470 480 KDLANFAPEI KSCVEACNFI AKSTKEQNDS GSENENWVLI GKVIDKACFW IALLLFSIGT 490 500 LAIFLTGHFN QVPEFPFPGD PRKYVP

References

[1]	"Structural homology of Torpedo californica acetylcholine receptor subunits." Noda M., Takahashi H., Tanabe T., Toyosato M., Kikyotani S., Furutani Y., Hirose T., Takashima H., Inayama S., Miyata T., Numa S. Nature 302:528-532(1983) [PubMed: 6188060] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Nucleotide and deduced amino acid sequences of Torpedo californica acetylcholine receptor gamma subunit." Claudio T., Ballivet M., Patrick J., Heinemann S.F. Proc. Natl. Acad. Sci. U.S.A. 80:1111-1115(1983) [PubMed: 6573658] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"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: 2742850] [Abstract] Cited for: PROTEIN SEQUENCE OF 123-147, DISULFIDE BOND.
[4]	"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: 1721053] [Abstract] Cited for: PHOSPHORYLATION AT TYR-381.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

V01393 mRNA. Translation: CAA24682.1.
V01394 mRNA. Translation: CAA24683.1.
J00966 mRNA. Translation: AAA49276.1.

PIR

ACRYG1. A93300.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LK1	model	-	D	19-236	[»]
1OED	electron microscopy	4.00	E	236-495	[»]
1OLK	model	-	B	20-236	[»]

ProteinModelPortal

P02714.

SMR

P02714. Positions 19-495.

ModBase

Search...

PTM databases

GlycoSuiteDB

P02714.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

HOVERGEN

HBG003756.

Family and domain databases

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]

Gene3D

G3DSA:2.70.170.10. Neur_chan_lig_bd. 1 hit.

PANTHER

PTHR18945. Neur_channel. 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.

PROSITE

PS00236. NEUROTR_ION_CHANNEL. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ACHG_TORCA

Accession

Primary (citable) accession number: P02714

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	January 25, 2012
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program