Asic1
entrez
79123
canonical
uniprot
P55926
canonical
ensembl
ENSRNOG00000059765
resolver
ensembl
ENSRNOG00055029116
resolver
ensembl
ENSRNOG00060006660
resolver
ensembl
ENSRNOG00065022925
resolver
ensp
ENSRNOP00000072206
resolver
genesymbol
Asic1
resolver
genesymbol_syn
Accn2
resolver
genesymbol_syn
Bnac2
resolver
uniprot
O88762
resolver
uniprot
Q91YB8
resolver
uniprot
Q99NA1
resolver
uniprot_entry
ASIC1_RAT
resolver
uniprot_sec
O88762
resolver
uniprot_sec
Q91YB8
resolver
uniprot_sec
Q99NA1
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by the diuretic drug amiloride (PubMed:9062189). External calcium is required to potentiate proton activation of ASIC1 at physiological concentrations, but at higher, non-physiological concentrations, it inhibits activation (PubMed:12198124, PubMed:15369669, PubMed:9062189). Also potentiated by other multivalent cations like Mg(2+), Ba(2+) (PubMed:12198124). Activated by FMRFamide-related neuropeptides (PubMed:10798398). Inhibited by anti-inflammatory drugs like salicylic acid (PubMed:11588175). The spider venom psalmotoxin-1 specifically inhibits the ASIC1 homotrimer (PubMed:10829030, PubMed:26248594). The snake venom mambalgin-1, mambalgin-2 and mambalgin-3 inhibit the homotrimer of Asic1a (ASIC1 isoform 1) (PubMed:23034652, PubMed:23624383, PubMed:24323786, PubMed:24695733, PubMed:26680001). The snake venom mambalgin-1 and mambalgin-2 inhibit heterotrimers of Asic1a-Asic1b (ASIC1 isoform 1-ASIC1 isoform 3) (PubMed:23034652). Heterotrimer of Asic1a-Asic2a is inhibited by the snake venom mambalgin-1, mambalgin-2 and mambalgin-3 (PubMed:23034652, PubMed:23624383, PubMed:26680001). Heterotrimer of Asic1a-Asic2b is inhibited by the snake venom mambalgin-1 and mambalgin-2 (PubMed:23034652). The spider venom Pi-theraphotoxin-Hm3a inhibits the homotrimer of Asic1a (ASIC1 isoform 1) (PubMed:28327374). The spider venom Pi-theraphotoxin-Hm3a inhibits heterotrimers of Asic1a-Asic1b (ASIC1 isoform 1-ASIC1 isoform 3) (PubMed:28327374). The spider venom Pi-hexatoxin-Hi1a inhibits the ASIC1 homotrimer (PubMed:28320941). {ECO:0000269|PubMed:10798398, ECO:0000269|PubMed:10829030, ECO:0000269|PubMed:11588175, ECO:0000269|PubMed:12198124, ECO:0000269|PubMed:15369669, ECO:0000269|PubMed:23034652, ECO:0000269|PubMed:23624383, ECO:0000269|PubMed:24323786, ECO:0000269|PubMed:24695733, ECO:0000269|PubMed:26248594, ECO:0000269|PubMed:26680001, ECO:0000269|PubMed:28320941, ECO:0000269|PubMed:28327374, ECO:0000269|PubMed:9062189}.; ACTIVITY REGULATION: [Isoform ASIC1b]: Not inhibited by extracellular calcium. {ECO:0000269|PubMed:15452199, ECO:0000269|PubMed:9707631}.
uniprot
proteins
amino_acid_sequence
MELKTEEEEVGGVQPVSIQAFASSSTLHGLAHIFSYERLSLKRALWALCFLGSLAVLLCVCTERVQYYFCYHHVTKLDEVAASQLTFPAVTLCNLNEFRFSQVSKNDLYHAGELLALLNNRYEIPDTQMADEKQLEILQDKANFRSFKPKPFNMREFYDRAGHDIRDMLLSCHFRGEACSAEDFKVVFTRYGKCYTFNSGQDGRPRLKTMKGGTGNGLEIMLDIQQDEYLPVWGETDETSFEAGIKVQIHSQDEPPFIDQLGFGVAPGFQTFVSCQEQRLIYLPSPWGTCNAVTMDSDFFDSYSITACRIDCETRYLVENCNCRMVHMPGDAPYCTPEQYKECADPALDFLVEKDQEYCVCEMPCNLTRYGKELSMVKIPSKASAKYLAKKFNKSEQYIGENILVLDIFFEVLNYETIEQKKAYEIAGLLGDIGGQMGLFIGASILTVLELFDYAYEVIKHRLCRRGKCQKEAKRSSADKGVALSLDDVKRHNPCESLRGHPAGMTYAANILPHHPARGTFEDFTC
uniprot
proteins
function
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 (PubMed:11448963, PubMed:9062189, PubMed:9360943). Upon extracellular pH drop this channel elicits transient, fast activating, and completely desensitizing inward currents (PubMed:12198124, PubMed:9062189, PubMed:9360943). Displays high selectivity for sodium ions but can also permit the permeation of other cations (PubMed:11448963, PubMed:9062189, PubMed:9360943). Regulates more or less directly intracellular calcium concentration and CaMKII phosphorylation, and thereby the density of dendritic spines (PubMed:15369669). Modulates neuronal activity in the circuits underlying innate fear (By similarity). {ECO:0000250|UniProtKB:Q6NXK8, ECO:0000269|PubMed:11448963, ECO:0000269|PubMed:12198124, ECO:0000269|PubMed:15369669, ECO:0000269|PubMed:9062189, ECO:0000269|PubMed:9360943}.; FUNCTION: [Isoform ASIC1a]: Permeable to other cations including calcium, lithium and potassium. {ECO:0000269|PubMed:9062189, ECO:0000269|PubMed:9360943}.; FUNCTION: [Isoform ASIC1b]: pH activation and steady-state inactivation are shifted to more acidic values (PubMed:12198124). Forms channels that are not permeable to calcium as it discrimates stronger between monovalent cations (PubMed:9707631). {ECO:0000269|PubMed:12198124, ECO:0000269|PubMed:9707631}.; FUNCTION: [Isoform ASIC-beta2]: Has no pH-gated sodium channel activity per se but can associate with other ASICs and regulate their pH-sensitivity. {ECO:0000269|PubMed:11588592}.
uniprot
proteins
mass_dalton
59641
uniprot
proteins
mutagenesis
MUTAGEN 83; /note="S->P: No effect on pH-gated monoatomic ion channel activity. Increases desensitization rates; when associated with L-84 and M-85."; /evidence="ECO:0000269|PubMed:12947112"; MUTAGEN 84; /note="Q->L: No effect on pH-gated monoatomic ion channel activity. Increases desensitization rates; when associated with P-83 and M-85."; /evidence="ECO:0000269|PubMed:12947112"; MUTAGEN 85; /note="L->M: No effect on pH-gated monoatomic ion channel activity. Increases desensitization rates; when associated with P-83 and L-84."; /evidence="ECO:0000269|PubMed:12947112"; MUTAGEN 100; /note="F->L: No effect on channel activation and inactivation."; /evidence="ECO:0000269|PubMed:12198124"; MUTAGEN 103; /note="V->L: No effect on channel activation and inactivation."; /evidence="ECO:0000269|PubMed:12198124"; MUTAGEN 105; /note="K->Y: Activated and inactivated at lower pH."; /evidence="ECO:0000269|PubMed:12198124"; MUTAGEN 106; /note="N->P: Activated and inactivated at lower pH."; /evidence="ECO:0000269|PubMed:12198124"; MUTAGEN 128..131; /note="QMAD->HLVE: No effect on desensitization rates."; /evidence="ECO:0000269|PubMed:12947112"; MUTAGEN 173; /note="H->S: No significant decrease in inhibition by the spider pi-theraphotoxin-Hm3a."; /evidence="ECO:0000269|PubMed:28327374"; MUTAGEN 174; /note="F->Y: No significant decrease in inhibition by the spider pi-theraphotoxin-Hm3a."; /evidence="ECO:0000269|PubMed:28327374"; MUTAGEN 175; /note="R->C: 18-fold decrease in inhibition by the spider pi-theraphotoxin-Hm3a."; /evidence="ECO:0000269|PubMed:28327374"; MUTAGEN 177; /note="E->G: 10-fold decrease in inhibition by the spider pi-theraphotoxin-Hm3a."; /evidence="ECO:0000269|PubMed:28327374"; MUTAGEN 178; /note="A->P: No significant decrease in inhibition by the spider pi-theraphotoxin-Hm3a."; /evidence="ECO:0000269|PubMed:28327374"; MUTAGEN 178; /note="A->V: No significant decrease in inhibition by the spider pi-theraphotoxin-Hm3a."; /evidence="ECO:0000269|PubMed:28327374"; MUTAGEN 190; /note="R->K: Small decrease in inhibition by the snake mambalgin-2 toxin; when associated with Q-259 and E-260."; /evidence="ECO:0000269|PubMed:24695733"; MUTAGEN 235; /note="E->A: No change in the shift of pH for both activation and desensitization by the spider venom psalmotoxin-1."; /evidence="ECO:0000269|PubMed:26248594"; MUTAGEN 259; /note="D->Q: Small decrease in inhibition by the snake mambalgin-2 toxin; when associated with K-190 and E-260."; /evidence="ECO:0000269|PubMed:24695733"; MUTAGEN 260; /note="Q->E: Small decrease in inhibition by the snake mambalgin-2 toxin; when associated with K-190 and Q-259."; /evidence="ECO:0000269|PubMed:24695733"; MUTAGEN 316; /note="Y->A: No change in the shift of pH for both activation and desensitization by the spider venom psalmotoxin-1."; /evidence="ECO:0000269|PubMed:26248594"; MUTAGEN 349..350; /note="DF->GL: Complete loss in inhibition by 200 nM of the snake mambalgin-2 toxin."; /evidence="ECO:0000269|PubMed:24695733"; MUTAGEN 349; /note="D->G: High decrease in inhibition by the snake mambalgin-2 toxin."; /evidence="ECO:0000269|PubMed:24695733"; MUTAGEN 350; /note="F->A: Complete loss of inhibition by the spider Pi-hexatoxin-Hi1a, and by the snake mambalgin-2 toxin. Potentiated by the spider pi-theraphotoxin-Hm3a (at both pH 7.35 and 7.45) and inhibited at higher toxin concentration at pH 7.35. Complete loss in the shift of pH for both activation and desensitization by the spider venom psalmotoxin-1."; /evidence="ECO:0000269|PubMed:24323786, ECO:0000269|PubMed:26248594, ECO:0000269|PubMed:28320941, ECO:0000269|PubMed:28327374"; MUTAGEN 350; /note="F->L: 37-fold decrease in inhibition by the snake mambalgin-1 toxin. Very high decrease in inhibition by the snake mambalgin-2 toxin."; /evidence="ECO:0000269|PubMed:24695733, ECO:0000269|PubMed:26680001"; MUTAGEN 352; /note="V->A: Moderate decrease in inhibition by the snake mambalgin-2 toxin."; /evidence="ECO:0000269|PubMed:24695733"; MUTAGEN 354; /note="K->A: No change in the shift of pH for both activation and desensitization by the spider venom psalmotoxin-1."; /evidence="ECO:0000269|PubMed:26248594"; MUTAGEN 356; /note="Q->S: Moderate decrease in inhibition by the snake mambalgin-2 toxin."; /evidence="ECO:0000269|PubMed:24695733"; MUTAGEN 357; /note="E->N: Moderate decrease in inhibition by the snake mambalgin-2 toxin."; /evidence="ECO:0000269|PubMed:24695733"; MUTAGEN 425; /note="E->G: Reduction of Ca(2+) block. Loss of Ca(2+) block; when associated with C-432."; /evidence="ECO:0000269|PubMed:15452199"; MUTAGEN 431; /note="G->V,F: Constitutive channel activity."; /evidence="ECO:0000269|PubMed:9360943"; MUTAGEN 432; /note="D->A: Reduction of Ca(2+) block."; /evidence="ECO:0000269|PubMed:15452199"; MUTAGEN 432; /note="D->C: Reduction of Ca(2+) block. Loss of Ca(2+) block; when associated with G-425."; /evidence="ECO:0000269|PubMed:15452199"; MUTAGEN 436; /note="Q->N: No effect on Ca(2+) block."; /evidence="ECO:0000269|PubMed:15452199
uniprot
proteins
post_translational_modification
PTM: pH-gating could be regulated by serine proteases. {ECO:0000250|UniProtKB:P78348}.; PTM: Phosphorylation by PKA regulates interaction with PICK1 and subcellular localization. Phosphorylation by PKC may regulate the channel. {ECO:0000250|UniProtKB:P78348}.
uniprot
proteins
protein_family
ASIC1 subfamily
uniprot
proteins
protein_family
Amiloride-sensitive sodium channel (TC 1.A.6) family
uniprot
proteins
pubmed
10798398
uniprot
proteins
pubmed
10829030
uniprot
proteins
pubmed
11448963
uniprot
proteins
pubmed
11588175
uniprot
proteins
pubmed
11588592
uniprot
proteins
pubmed
11842212
uniprot
proteins
pubmed
12198124
uniprot
proteins
pubmed
12947112
uniprot
proteins
pubmed
15369669
uniprot
proteins
pubmed
15452199
uniprot
proteins
pubmed
23034652
uniprot
proteins
pubmed
23624383
uniprot
proteins
pubmed
24323786
uniprot
proteins
pubmed
24695733
uniprot
proteins
pubmed
26248594
uniprot
proteins
pubmed
26680001
uniprot
proteins
pubmed
28320941
uniprot
proteins
pubmed
28327374
uniprot
proteins
pubmed
40712023
uniprot
proteins
pubmed
9062189
uniprot
proteins
pubmed
9360943
uniprot
proteins
pubmed
9707631
uniprot
proteins
sequence_length
526
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11842212, ECO:0000269|PubMed:9062189, ECO:0000269|PubMed:9707631}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P78348}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q6NXK8}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q6NXK8}. Note=Isolated in synaptosomes from the dendritic synapses of neurons. {ECO:0000250|UniProtKB:Q6NXK8}.; SUBCELLULAR LOCATION: [Isoform ASIC1a]: Cell membrane {ECO:0000269|PubMed:40712023}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 50..66; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P78348"; TRANSMEM 426..456; /note="Discontinuously helical"; /evidence="ECO:0000250|UniProtKB:P78348
uniprot
proteins