Aliases for CHRNA4 Gene
- Cholinergic Receptor Nicotinic Alpha 4 Subunit 2 3 5
- Cholinergic Receptor, Nicotinic, Alpha Polypeptide 4 2 3
- Cholinergic Receptor, Nicotinic, Alpha 4 (Neuronal) 2 3
- Cholinergic Receptor, Nicotinic Alpha 4 2 3
- NACRA4 3 4
- Neuronal Nicotinic Acetylcholine Receptor Alpha-4 Subunit 3
- Acetylcholine Receptor, Nicotinic, Alpha 4 (Neuronal) 2
External Ids for CHRNA4 Gene
Previous HGNC Symbols for CHRNA4 Gene
Previous GeneCards Identifiers for CHRNA4 Gene
This gene encodes a nicotinic acetylcholine receptor, which belongs to a superfamily of ligand-gated ion channels that play a role in fast signal transmission at synapses. These pentameric receptors can bind acetylcholine, which causes an extensive change in conformation that leads to the opening of an ion-conducting channel across the plasma membrane. This protein is an integral membrane receptor subunit that can interact with either nAChR beta-2 or nAChR beta-4 to form a functional receptor. Mutations in this gene cause nocturnal frontal lobe epilepsy type 1. Polymorphisms in this gene that provide protection against nicotine addiction have been described. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Feb 2012]
GeneCards Summary for CHRNA4 Gene
CHRNA4 (Cholinergic Receptor Nicotinic Alpha 4 Subunit) is a Protein Coding gene. Diseases associated with CHRNA4 include Epilepsy, Nocturnal Frontal Lobe, 1 and Tobacco Addiction. Among its related pathways are Sudden Infant Death Syndrome (SIDS) Susceptibility Pathways and Transmission across Chemical Synapses. Gene Ontology (GO) annotations related to this gene include ion channel activity. An important paralog of this gene is CHRNA2.
UniProtKB/Swiss-Prot for CHRNA4 Gene
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 permeable to sodium ions.
Nicotinic alpha4beta2 receptors have high affinity for nicotine and account for >90% of [3H]-nicotine binding to brain tissues. A stoichiometry of (alpha4)2(beta2)3 has been proposed, generating two agonist binding sites consistent with the model of the muscle nAChR.