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Target not currently curated in GtoImmuPdb
Target id: 462
Nomenclature: nicotinic acetylcholine receptor α1 subunit
Gene and Protein Information  |
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| Species | TM | AA | Chromosomal Location | Gene Symbol | Gene Name | Reference |
| Human | 4 | 482 | 2q31.1 | CHRNA1 | cholinergic receptor nicotinic alpha 1 subunit | 11 |
| Mouse | 4 | 457 | 2 43.76 cM | Chrna1 | cholinergic receptor nicotinic alpha 1 subunit | 8 |
| Rat | 4 | 457 | 3q23 | Chrna1 | cholinergic receptor nicotinic alpha 1 subunit | 15 |
| Previous and Unofficial Names |
| acetylcholine receptor subunit alpha | Achr-1 | cholinergic receptor, nicotinic, alpha 1 (muscle) | cholinergic receptor, nicotinic alpha 1 | cholinergic receptor, nicotinic, alpha 1 | cholinergic receptor |
| Database Links |
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| Alphafold | P02708 (Hs), P04756 (Mm), P25108 (Rn) |
| CATH/Gene3D | 2.70.170.10 |
| ChEMBL Target | CHEMBL4808 (Hs), CHEMBL3038460 (Mm), CHEMBL3137264 (Mm), CHEMBL3885509 (Rn), CHEMBL4523658 (Rn) |
| DrugBank Target | P02708 (Hs) |
| Ensembl Gene | ENSG00000138435 (Hs), ENSMUSG00000027107 (Mm), ENSRNOG00000018286 (Rn) |
| Entrez Gene | 1134 (Hs), 11435 (Mm), 79557 (Rn) |
| Human Protein Atlas | ENSG00000138435 (Hs) |
| KEGG Gene | hsa:1134 (Hs), mmu:11435 (Mm), rno:79557 (Rn) |
| OMIM | 100690 (Hs) |
| Orphanet | ORPHA119411 (Hs) |
| Pharos | P02708 (Hs) |
| RefSeq Nucleotide | NM_001039523 (Hs), NM_007389 (Mm), NM_024485 (Rn) |
| RefSeq Protein | NP_001034612 (Hs), NP_031415 (Mm), NP_077811 (Rn) |
| UniProtKB | P02708 (Hs), P04756 (Mm), P25108 (Rn) |
| Wikipedia | CHRNA1 (Hs) |
| Functional Characteristics |
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| (α1)2βγδ: PCa/PNa = 0.16 - 0.2, Pf = 2.1 – 2.9%; (α1)2βδε: PCa/PNa = 0.65 – 1.38, Pf = 4.1 – 7.2% | |
| Natural/Endogenous Ligands |
| acetylcholine |
| Commonly used antagonists (Human) |
| (α1)2β1γδ and (α1)2β1δε: α-bungarotoxin > pancuronium > vecuronium > rocuronium > tubocurarine (IC50 = 43 - 82 nM) |
Download all structure-activity data for this target as a CSV file 
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| Channel Blockers | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Tissue Distribution Comments | |
| In vertebrates α1-subunit mRNA is generally expressed in skeletal muscle |
| Physiological Consequences of Altering Gene Expression
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| Clinically-Relevant Mutations and Pathophysiology
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| General Comments |
| The human α1 subunit exists as two variants that arise from alternative splicing. The long variant is tabulated above. |
1. An MC, Lin W, Yang J, Dominguez B, Padgett D, Sugiura Y, Aryal P, Gould TW, Oppenheim RW, Hester ME et al.. (2010) Acetylcholine negatively regulates development of the neuromuscular junction through distinct cellular mechanisms. Proc Natl Acad Sci USA, 107 (23): 10702-7. [PMID:20498043]
2. Croxen R, Newland C, Beeson D, Oosterhuis H, Chauplannaz G, Vincent A, Newsom-Davis J. (1997) Mutations in different functional domains of the human muscle acetylcholine receptor alpha subunit in patients with the slow-channel congenital myasthenic syndrome. Hum Mol Genet, 6 (5): 767-74. [PMID:9158151]
3. Engel AG, Ohno K, Milone M, Wang HL, Nakano S, Bouzat C, Pruitt 2nd JN, Hutchinson DO, Brengman JM, Bren N et al.. (1996) New mutations in acetylcholine receptor subunit genes reveal heterogeneity in the slow-channel congenital myasthenic syndrome. Hum Mol Genet, 5 (9): 1217-27. [PMID:8872460]
4. Engel AG, Ohno K, Sine SM. (2003) Sleuthing molecular targets for neurological diseases at the neuromuscular junction. Nat Rev Neurosci, 4 (5): 339-52. [PMID:12728262]
5. Engel AG, Shen XM, Selcen D, Sine SM. (2010) What have we learned from the congenital myasthenic syndromes. J Mol Neurosci, 40 (1-2): 143-53. [PMID:19688192]
6. Jonsson M, Gurley D, Dabrowski M, Larsson O, Johnson EC, Eriksson LI. (2006) Distinct pharmacologic properties of neuromuscular blocking agents on human neuronal nicotinic acetylcholine receptors: a possible explanation for the train-of-four fade. Anesthesiology, 105 (3): 521-33. [PMID:16931985]
7. Lindstrom JM. (2000) Acetylcholine receptors and myasthenia. Muscle Nerve, 23 (4): 453-77. [PMID:10716755]
8. Merlie JP, Sebbane R, Gardner S, Lindstrom J. (1983) cDNA clone for the alpha subunit of the acetylcholine receptor from the mouse muscle cell line BC3H-1. Proc Natl Acad Sci USA, 80 (12): 3845-9. [PMID:6344089]
9. Michalk A, Stricker S, Becker J, Rupps R, Pantzar T, Miertus J, Botta G, Naretto VG, Janetzki C, Yaqoob N et al.. (2008) Acetylcholine receptor pathway mutations explain various fetal akinesia deformation sequence disorders. Am J Hum Genet, 82 (2): 464-76. [PMID:18252226]
10. Milone M, Wang HL, Ohno K, Fukudome T, Pruitt JN, Bren N, Sine SM, Engel AG. (1997) Slow-channel myasthenic syndrome caused by enhanced activation, desensitization, and agonist binding affinity attributable to mutation in the M2 domain of the acetylcholine receptor alpha subunit. J Neurosci, 17 (15): 5651-65. [PMID:9221765]
11. Noda M, Furutani Y, Takahashi H, Toyosato M, Tanabe T, Shimizu S, Kikyotani S, Kayano T, Hirose T, Inayama S et al.. (1983) Cloning and sequence analysis of calf cDNA and human genomic DNA encoding alpha-subunit precursor of muscle acetylcholine receptor. Nature, 305 (5937): 818-23. [PMID:6688857]
12. Shen XM, Deymeer F, Sine SM, Engel AG. (2006) Slow-channel mutation in acetylcholine receptor alphaM4 domain and its efficient knockdown. Ann Neurol, 60 (1): 128-36. [PMID:16685696]
13. Sine SM, Ohno K, Bouzat C, Auerbach A, Milone M, Pruitt JN, Engel AG. (1995) Mutation of the acetylcholine receptor alpha subunit causes a slow-channel myasthenic syndrome by enhancing agonist binding affinity. Neuron, 15 (1): 229-39. [PMID:7619526]
14. Wang HL, Milone M, Ohno K, Shen XM, Tsujino A, Batocchi AP, Tonali P, Brengman J, Engel AG, Sine SM. (1999) Acetylcholine receptor M3 domain: stereochemical and volume contributions to channel gating. Nat Neurosci, 2 (3): 226-33. [PMID:10195214]
15. Witzemann V, Stein E, Barg B, Konno T, Koenen M, Kues W, Criado M, Hofmann M, Sakmann B. (1990) Primary structure and functional expression of the alpha-, beta-, gamma-, delta- and epsilon-subunits of the acetylcholine receptor from rat muscle. Eur J Biochem, 194 (2): 437-48. [PMID:1702709]
