Q07001 · ACHD_HUMAN
- ProteinAcetylcholine receptor subunit delta
- GeneCHRND
- 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
Aspect | Term | |
---|---|---|
Cellular Component | acetylcholine-gated channel complex | |
Cellular Component | neuromuscular junction | |
Cellular Component | neuron projection | |
Cellular Component | plasma membrane | |
Cellular Component | postsynaptic membrane | |
Cellular Component | postsynaptic specialization membrane | |
Cellular Component | synapse | |
Molecular Function | acetylcholine binding | |
Molecular Function | acetylcholine receptor activity | |
Molecular Function | acetylcholine-gated monoatomic cation-selective 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 | musculoskeletal movement | |
Biological Process | neuromuscular process | |
Biological Process | signal transduction | |
Biological Process | skeletal muscle contraction | |
Biological Process | skeletal muscle tissue growth |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAcetylcholine receptor subunit delta
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ07001
- 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 | 22-245 | Extracellular | ||||
Sequence: LNEEERLIRHLFQEKGYNKELRPVAHKEESVDVALALTLSNLISLKEVEETLTTNVWIEHGWTDNRLKWNAEEFGNISVLRLPPDMVWLPEIVLENNNDGSFQISYSCNVLVYHYGFVYWLPPAIFRSSCPISVTYFPFDWQNCSLKFSSLKYTAKEITLSLKQDAKENRTYPVEWIIIDPEGFTENGEWEIVHRPARVNVDPRAPLDSPSRQDITFYLIIRRK | ||||||
Transmembrane | 246-270 | Helical | ||||
Sequence: PLFYIINILVPCVLISFMVNLVFYL | ||||||
Transmembrane | 278-299 | Helical | ||||
Sequence: TSVAISVLLAQSVFLLLISKRL | ||||||
Transmembrane | 312-333 | Helical | ||||
Sequence: FLLFGMVLVTMVVVICVIVLNI | ||||||
Topological domain | 334-471 | Cytoplasmic | ||||
Sequence: HFRTPSTHVLSEGVKKLFLETLPELLHMSRPAEDGPSPGALVRRSSSLGYISKAEEYFLLKSRSDLMFEKQSERHGLARRLTTARRPPASSEQAQQELFNELKPAVDGANFIVNHMRDQNNYNEEKDSWNRVARTVDR | ||||||
Transmembrane | 472-490 | Helical | ||||
Sequence: LCLFVVTPVMVVGTAWIFL |
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_043905 | 95 | F>L | in LMPS; dbSNP:rs121909506 |
Myasthenic syndrome, congenital, 3A, slow-channel (CMS3A)
- Note
- DescriptionA form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness affecting the axial and limb muscles (with hypotonia in early-onset forms), the ocular muscles (leading to ptosis and ophthalmoplegia), and the facial and bulbar musculature (affecting sucking and swallowing, and leading to dysphonia). The symptoms fluctuate and worsen with physical effort. CMS3A is a slow-channel myasthenic syndrome. It is caused by kinetic abnormalities of the AChR, resulting in prolonged AChR channel opening episodes, prolonged endplate currents, and depolarization block. This is associated with calcium overload, which may contribute to subsequent degeneration of the endplate and postsynaptic membrane.
- See alsoMIM:616321
Natural variants in CMS3A
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_019566 | 289 | S>F | in CMS3A; delayed closure of AchR ion channels, increasing the propensity for open-channel block, as well as a reduced rate of channel opening; dbSNP:rs121909502 |
Myasthenic syndrome, congenital, 3B, fast-channel (CMS3B)
- Note
- DescriptionA form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness affecting the axial and limb muscles (with hypotonia in early-onset forms), the ocular muscles (leading to ptosis and ophthalmoplegia), and the facial and bulbar musculature (affecting sucking and swallowing, and leading to dysphonia). The symptoms fluctuate and worsen with physical effort. CMS3B is a fast-channel myasthenic syndrome. It is caused by kinetic abnormalities of the AChR, resulting in brief opening and activity of the channel, with a rapid decay in endplate current, failure to achieve threshold depolarization of the endplate and consequent failure to fire an action potential.
- See alsoMIM:616322
Natural variants in CMS3B
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_073691 | 42 | L>P | in CMS3B; results in reduced gating efficiency; slows opening of the channel; decreases probability that the channel will open in response to ACh | |
VAR_073692 | 79 | I>K | in CMS3B; prevents expression of the AChR on the cell surface; is a null mutation; dbSNP:rs121909509 | |
VAR_021210 | 80 | E>K | in CMS3B; reduced adult and fetal AChR expression and a reduced probability of both adult and fetal AChR being in the open state; dbSNP:rs121909504 | |
VAR_021211 | 271 | P>Q | in CMS3B; burst duration was decreased and disassociation of ACh was increased resulting in brief channel opening episodes; shows abnormal association with alpha CHRNA1 subunit resulting in a decreased number of fully assembled AChRs; dbSNP:rs121909503 |
Myasthenic syndrome, congenital, 3C, associated with acetylcholine receptor deficiency (CMS3C)
- Note
- DescriptionA form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness affecting the axial and limb muscles (with hypotonia in early-onset forms), the ocular muscles (leading to ptosis and ophthalmoplegia), and the facial and bulbar musculature (affecting sucking and swallowing, and leading to dysphonia). The symptoms fluctuate and worsen with physical effort. CMS3C is an autosomal recessive disorder of postsynaptic neuromuscular transmission, due to deficiency of AChR at the endplate that results in low amplitude of the miniature endplate potential and current.
- See alsoMIM:616323
Natural variants in CMS3C
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_073694 | 402 | E>K | in CMS3C; results in reduced expression of the AChR at the cell surface; impairs normal clustering of the AChR channel with RAPSN; dbSNP:rs145955590 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_073691 | 42 | in CMS3B; results in reduced gating efficiency; slows opening of the channel; decreases probability that the channel will open in response to ACh | |||
Sequence: L → P | ||||||
Natural variant | VAR_073692 | 79 | in CMS3B; prevents expression of the AChR on the cell surface; is a null mutation; dbSNP:rs121909509 | |||
Sequence: I → K | ||||||
Natural variant | VAR_021210 | 80 | in CMS3B; reduced adult and fetal AChR expression and a reduced probability of both adult and fetal AChR being in the open state; dbSNP:rs121909504 | |||
Sequence: E → K | ||||||
Natural variant | VAR_043905 | 95 | in LMPS; dbSNP:rs121909506 | |||
Sequence: F → L | ||||||
Natural variant | VAR_073693 | 114 | has no appreciable kinetic effects; allows for robust AChR expression; dbSNP:rs760395222 | |||
Sequence: V → L | ||||||
Natural variant | VAR_021211 | 271 | in CMS3B; burst duration was decreased and disassociation of ACh was increased resulting in brief channel opening episodes; shows abnormal association with alpha CHRNA1 subunit resulting in a decreased number of fully assembled AChRs; dbSNP:rs121909503 | |||
Sequence: P → Q | ||||||
Natural variant | VAR_021212 | 288 | in dbSNP:rs41265127 | |||
Sequence: Q → E | ||||||
Natural variant | VAR_019566 | 289 | in CMS3A; delayed closure of AchR ion channels, increasing the propensity for open-channel block, as well as a reduced rate of channel opening; dbSNP:rs121909502 | |||
Sequence: S → F | ||||||
Mutagenesis | 290 | Increased length of channel opening. | ||||
Sequence: V → A | ||||||
Natural variant | VAR_036031 | 398 | in a breast cancer sample; somatic mutation; dbSNP:rs749461400 | |||
Sequence: D → E | ||||||
Natural variant | VAR_073694 | 402 | in CMS3C; results in reduced expression of the AChR at the cell surface; impairs normal clustering of the AChR channel with RAPSN; dbSNP:rs145955590 | |||
Sequence: E → K |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 654 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, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-21 | UniProt | |||||
Sequence: MEGPVLTLGLLAALAVCGSWG | |||||||
Chain | PRO_0000000322 | 22-517 | UniProt | Acetylcholine receptor subunit delta | |||
Sequence: LNEEERLIRHLFQEKGYNKELRPVAHKEESVDVALALTLSNLISLKEVEETLTTNVWIEHGWTDNRLKWNAEEFGNISVLRLPPDMVWLPEIVLENNNDGSFQISYSCNVLVYHYGFVYWLPPAIFRSSCPISVTYFPFDWQNCSLKFSSLKYTAKEITLSLKQDAKENRTYPVEWIIIDPEGFTENGEWEIVHRPARVNVDPRAPLDSPSRQDITFYLIIRRKPLFYIINILVPCVLISFMVNLVFYLPADSGEKTSVAISVLLAQSVFLLLISKRLPATSMAIPLIGKFLLFGMVLVTMVVVICVIVLNIHFRTPSTHVLSEGVKKLFLETLPELLHMSRPAEDGPSPGALVRRSSSLGYISKAEEYFLLKSRSDLMFEKQSERHGLARRLTTARRPPASSEQAQQELFNELKPAVDGANFIVNHMRDQNNYNEEKDSWNRVARTVDRLCLFVVTPVMVVGTAWIFLQGVYNQPPPQPFPGDPYSYNVQDKRFI | |||||||
Glycosylation | 97 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 151↔165 | UniProt | |||||
Sequence: CPISVTYFPFDWQNC | |||||||
Glycosylation | 164 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue (large scale data) | 379 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 390 | UniProt | Phosphotyrosine; by Tyr-kinases | ||||
Sequence: Y |
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. The muscle heteropentamer composed of alpha-1, beta-1, delta, epsilon subunits interacts with the alpha-conotoxin ImII (PubMed:15609996).
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. Delta/CHRND 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.
Q07001-1
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)58,895
- Last updated1994-06-01 v1
- Checksum195CEF69358758BD
Q07001-2
- Name2
- Differences from canonical
- 67-81: Missing
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_046423 | 67-81 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X55019 EMBL· GenBank· DDBJ | CAA38759.1 EMBL· GenBank· DDBJ | mRNA | ||
AK291526 EMBL· GenBank· DDBJ | BAF84215.1 EMBL· GenBank· DDBJ | mRNA | ||
AK300109 EMBL· GenBank· DDBJ | BAG61904.1 EMBL· GenBank· DDBJ | mRNA | ||
AK315297 EMBL· GenBank· DDBJ | BAG37703.1 EMBL· GenBank· DDBJ | mRNA | ||
AC092165 EMBL· GenBank· DDBJ | AAY24102.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471063 EMBL· GenBank· DDBJ | EAW71003.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC093923 EMBL· GenBank· DDBJ | AAH93923.1 EMBL· GenBank· DDBJ | mRNA | ||
BC093925 EMBL· GenBank· DDBJ | AAH93925.1 EMBL· GenBank· DDBJ | mRNA |