| Post Translational Modifications | pH-gating could be regulated by serine proteases. Phosphorylation by PKA regulates interaction with PICK1 and subcellular localization. Phosphorylation by PKC may regulate the channel. |
| Function | Forms voltage-independent, pH-gated trimeric sodium channels that act as postsynaptic excitatory receptors in the nervous system, playing a crucial role in regulating synaptic plasticity, learning, and memory. Upon extracellular pH drop this channel elicits transient, fast activating, and completely desensitizing inward currents. Displays high selectivity for sodium ions but can also permit the permeation of other cations. Regulates more or less directly intracellular calcium concentration and CaMKII phosphorylation, and thereby the density of dendritic spines. Modulates neuronal activity in the circuits underlying innate fear. Isoform Asic1a: Has high selectivity for sodium ions, but can also be permeable to other cations including calcium, lithium and potassium. Isoform Asic1b: Produces acid activated currents with a reduced amplitude and inactivates faster. Has high selectivity for sodium ions but also supports a calcium-mediated current which is sustained and maintained as long as acidic conditions are present. Also potentially permeable to lithium and potassium. Isoform 1: Has no measurable proton-gated sodium channel activity in vitro. |
| Protein Name | Acid-Sensing Ion Channel 1Asic1Amiloride-Sensitive Cation Channel 2 - NeuronalBrain Sodium Channel 2 |
| Database Links | Reactome: R-HSA-2672351 |
| Cellular Localisation | Cell MembraneMulti-Pass Membrane ProteinPostsynaptic Cell MembraneCell ProjectionDendriteIsolated In Synaptosomes From The Dendritic Synapses Of Neurons |
| Alternative Nanobody Names | Anti-Acid-Sensing Ion Channel 1 nanobodyAnti-Asic1 nanobodyAnti-Amiloride-Sensitive Cation Channel 2 - Neuronal nanobodyAnti-Brain Sodium Channel 2 nanobodyAnti-ASIC1 nanobodyAnti-ACCN2 nanobodyAnti-BNAC2 nanobody |
Information sourced from Uniprot.org
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