P07510 · ACHG_HUMAN
- ProteinAcetylcholine receptor subunit gamma
- GeneCHRNG
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids517 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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.
Catalytic activity
- K+(in) = K+(out)
- Na+(in) = Na+(out)
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | acetylcholine-gated channel complex | |
Cellular Component | neuron projection | |
Cellular Component | plasma membrane | |
Cellular Component | postsynaptic membrane | |
Cellular Component | synapse | |
Molecular Function | acetylcholine receptor activity | |
Molecular Function | acetylcholine-gated monoatomic cation-selective channel activity | |
Molecular Function | channel activity | |
Molecular Function | transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential | |
Biological Process | acetylcholine receptor signaling pathway | |
Biological Process | membrane depolarization | |
Biological Process | muscle contraction | |
Biological Process | signal transduction |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAcetylcholine receptor subunit gamma
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP07510
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Postsynaptic cell membrane ; Multi-pass membrane protein
Cell membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 23-240 | Extracellular | ||||
Sequence: RNQEERLLADLMQNYDPNLRPAERDSDVVNVSLKLTLTNLISLNEREEALTTNVWIEMQWCDYRLRWDPRDYEGLWVLRVPSTMVWRPDIVLENNVDGVFEVALYCNVLVSPDGCIYWLPPAIFRSACSISVTYFPFDWQNCSLIFQSQTYSTNEIDLQLSQEDGQTIEWIFIDPEAFTENGEWAIQHRPAKMLLDPAAPAQEAGHQKVVFYLLIQRK | ||||||
Transmembrane | 241-265 | Helical | ||||
Sequence: PLFYVINIIAPCVLISSVAILIHFL | ||||||
Transmembrane | 275-293 | Helical | ||||
Sequence: TVAINVLLAQTVFLFLVAK | ||||||
Transmembrane | 309-330 | Helical | ||||
Sequence: LTFLLVVTILIVVNAVVVLNVS | ||||||
Topological domain | 331-474 | Cytoplasmic | ||||
Sequence: LRSPHTHSMARGVRKVFLRLLPQLLRMHVRPLAPAAVQDTQSRLQNGSSGWSITTGEEVALCLPRSELLFQQWQRQGLVAAALEKLEKGPELGLSQFCGSLKQAAPAIQACVEACNLIACARHQQSHFDNGNEEWFLVGRVLDR | ||||||
Transmembrane | 475-495 | Helical | ||||
Sequence: VCFLAMLSLFICGTAGIFLMA |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Multiple pterygium syndrome, lethal type (LMPS)
- Note
- DescriptionMultiple pterygia are found infrequently in children with arthrogryposis and in fetuses with fetal akinesia syndrome. In lethal multiple pterygium syndrome there is intrauterine growth retardation, multiple pterygia, and flexion contractures causing severe arthrogryposis and fetal akinesia. Subcutaneous edema can be severe, causing fetal hydrops with cystic hygroma and lung hypoplasia. Oligohydramnios and facial anomalies are frequent.
- See alsoMIM:253290
Natural variants in LMPS
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_030753 | 107 | V>G | in EVMPS and LMPS; dbSNP:rs267606726 | |
VAR_030755 | 239 | R>C | in EVMPS and LMPS; dbSNP:rs121912670 |
Multiple pterygium syndrome, Escobar variant (EVMPS)
- Note
- DescriptionNon-lethal form of arthrogryposis multiplex congenita. It is an autosomal recessive condition characterized by excessive webbing (pterygia), congenital contractures (arthrogryposis), and scoliosis. Variable other features include intrauterine death, congenital respiratory distress, short stature, faciocranial dysmorphism, ptosis, low-set ears, arachnodactyly and cryptorchism in males. Congenital contractures are common and may be caused by reduced fetal movements at sensitive times of development. Possible causes of decreased fetal mobility include space constraints such as oligohydramnion, drugs, metabolic conditions or neuromuscular disorders including myasthenia gravis.
- See alsoMIM:265000
Natural variants in EVMPS
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_030753 | 107 | V>G | in EVMPS and LMPS; dbSNP:rs267606726 | |
VAR_030755 | 239 | R>C | in EVMPS and LMPS; dbSNP:rs121912670 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_030753 | 107 | in EVMPS and LMPS; dbSNP:rs267606726 | |||
Sequence: V → G | ||||||
Natural variant | VAR_030754 | 149 | in dbSNP:rs2289080 | |||
Sequence: A → T | ||||||
Natural variant | VAR_030755 | 239 | in EVMPS and LMPS; dbSNP:rs121912670 | |||
Sequence: R → C |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 672 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-22 | |||||
Sequence: MHGGQGPLLLLLLLAVCLGAQG | ||||||
Chain | PRO_0000000334 | 23-517 | Acetylcholine receptor subunit gamma | |||
Sequence: RNQEERLLADLMQNYDPNLRPAERDSDVVNVSLKLTLTNLISLNEREEALTTNVWIEMQWCDYRLRWDPRDYEGLWVLRVPSTMVWRPDIVLENNVDGVFEVALYCNVLVSPDGCIYWLPPAIFRSACSISVTYFPFDWQNCSLIFQSQTYSTNEIDLQLSQEDGQTIEWIFIDPEAFTENGEWAIQHRPAKMLLDPAAPAQEAGHQKVVFYLLIQRKPLFYVINIIAPCVLISSVAILIHFLPAKAGGQKCTVAINVLLAQTVFLFLVAKKVPETSQAVPLISKYLTFLLVVTILIVVNAVVVLNVSLRSPHTHSMARGVRKVFLRLLPQLLRMHVRPLAPAAVQDTQSRLQNGSSGWSITTGEEVALCLPRSELLFQQWQRQGLVAAALEKLEKGPELGLSQFCGSLKQAAPAIQACVEACNLIACARHQQSHFDNGNEEWFLVGRVLDRVCFLAMLSLFICGTAGIFLMAHYNRVPALPFPGDPRPYLPSPD | ||||||
Glycosylation | 52 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 150↔164 | |||||
Sequence: CSISVTYFPFDWQNC | ||||||
Glycosylation | 163 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Pentamer of two alpha chains, and one each of the beta, delta, and gamma (in immature muscle) or epsilon (in mature muscle) chains.
Binary interactions
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
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.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
P07510-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length517
- Mass (Da)57,883
- Last updated2007-02-20 v2
- Checksum7C78F533D4997D7A
P07510-2
- Name2
- Differences from canonical
- 117-169: NVDGVFEVALYCNVLVSPDGCIYWLPPAIFRSACSISVTYFPFDWQNCSLIFQ → K
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_055775 | 117-169 | in isoform 2 | |||
Sequence: NVDGVFEVALYCNVLVSPDGCIYWLPPAIFRSACSISVTYFPFDWQNCSLIFQ → K | ||||||
Sequence conflict | 189 | in Ref. 5; AAI11803 | ||||
Sequence: T → S |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X01715 EMBL· GenBank· DDBJ | CAA25861.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
X01716 EMBL· GenBank· DDBJ | CAA25861.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
X01717 EMBL· GenBank· DDBJ | CAA25861.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
X01718 EMBL· GenBank· DDBJ | CAA25861.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
X01719 EMBL· GenBank· DDBJ | CAA25861.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
X01720 EMBL· GenBank· DDBJ | CAA25861.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
X01721 EMBL· GenBank· DDBJ | CAA25861.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
X04759 EMBL· GenBank· DDBJ | CAA25861.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AK125362 EMBL· GenBank· DDBJ | BAG54190.1 EMBL· GenBank· DDBJ | mRNA | ||
AC092165 EMBL· GenBank· DDBJ | AAY24103.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
BC111802 EMBL· GenBank· DDBJ | AAI11803.1 EMBL· GenBank· DDBJ | mRNA |