CHRNA1

CHRNA1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesCHRNA1, ACHRA, ACHRD, CHRNA, CMS2A, FCCMS, SCCMS, CMS1A, CMS1B, Cholinergic receptor, nicotinic, alpha 1, cholinergic receptor nicotinic alpha 1 subunit
External IDsOMIM: 100690; MGI: 87885; HomoloGene: 59; GeneCards: CHRNA1; OMA:CHRNA1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001039523
NM_000079

NM_007389

RefSeq (protein)

NP_000070
NP_001034612

NP_031415

Location (UCSC)Chr 2: 174.75 – 174.79 MbChr 2: 73.39 – 73.41 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Neuronal acetylcholine receptor subunit alpha-1, also known as nAChRα1, is a protein that in humans is encoded by the CHRNA1 gene.[5] The protein encoded by this gene is a subunit of certain nicotinic acetylcholine receptors (nAchR).

The muscle acetylcholine receptor consists of 5 subunits of 4 different types: 2 alpha isoforms and 1 each of beta, gamma, and delta subunits.2 This gene encodes an alpha subunit that plays a role in acetylcholine binding/channel gating. Alternatively spliced transcript variants encoding different isoforms have been identified.[5]

Interactions

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Cholinergic receptor, nicotinic, alpha 1 has been shown to interact with CHRND.[6][7]

See also

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References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000138435Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000027107Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b "Entrez Gene: CHRNA1 cholinergic receptor, nicotinic, alpha 1 (muscle)".
  6. ^ Kreienkamp HJ, Maeda RK, Sine SM, Taylor P (March 1995). "Intersubunit contacts governing assembly of the mammalian nicotinic acetylcholine receptor". Neuron. 14 (3): 635–44. doi:10.1016/0896-6273(95)90320-8. PMID 7695910.
  7. ^ Wang ZZ, Hardy SF, Hall ZW (November 1996). "Assembly of the nicotinic acetylcholine receptor. The first transmembrane domains of truncated alpha and delta subunits are required for heterodimer formation in vivo". The Journal of Biological Chemistry. 271 (44): 27575–84. doi:10.1074/jbc.271.44.27575. PMID 8910344.

Further reading

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This article incorporates text from the United States National Library of Medicine, which is in the public domain.