ASIC1
entrez
41
canonical
uniprot
P78348
canonical
ensembl
ENSG00000110881
resolver
ensp
ENSP00000228468
resolver
ensp
ENSP00000400228
resolver
ensp
ENSP00000402896
resolver
ensp
ENSP00000450247
resolver
ensp
ENSP00000565730
resolver
ensp
ENSP00000565732
resolver
ensp
ENSP00000565733
resolver
ensp
ENSP00000783046
resolver
genesymbol
ASIC1
resolver
genesymbol_syn
ACCN2
resolver
genesymbol_syn
BNAC2
resolver
hgnc
HGNC:100
resolver
uniprot
A3KN86
resolver
uniprot
A8K1U5
resolver
uniprot
E5KBL7
resolver
uniprot
P78349
resolver
uniprot
Q96CV2
resolver
uniprot_entry
A8K1U5_HUMAN
resolver
uniprot_entry
ASIC1_HUMAN
resolver
uniprot_sec
A3KN86
resolver
uniprot_sec
E5KBL7
resolver
uniprot_sec
P78349
resolver
uniprot_sec
Q96CV2
resolver
activity_regulation
ACTIVITY REGULATION: Potentiated by FMRFamide-related neuropeptides, which are induced during inflammation and modulate pain responses (PubMed:10798398). Inhibited by the diuretic drug amiloride (PubMed:34319232). Spider venom psalmotoxin-1 inhibits the channel by locking it in its desensitized conformation (PubMed:19654327, PubMed:21036899, PubMed:22760635, PubMed:34319232). The homotrimeric channel is inhibited by the spider venom pi-theraphotoxin-Hm3a (PubMed:28327374). Homotrimeric and heterotrimeric (with ASIC2 isoform 1) channels are inhibited by the snake venom mambalgin-1, which prevents proton-induced transitions from the resting closed state to the active and/or desensitized states (PubMed:23034652, PubMed:32915133). Inhibited by Texas coral snake toxin MitTx1 (PubMed:34319232). {ECO:0000269|PubMed:10798398, ECO:0000269|PubMed:19654327, ECO:0000269|PubMed:21036899, ECO:0000269|PubMed:22760635, ECO:0000269|PubMed:23034652, ECO:0000269|PubMed:28327374, ECO:0000269|PubMed:32915133, ECO:0000269|PubMed:34319232}.
uniprot
proteins
amino_acid_sequence
MELKAEEEEVGGVQPVSIQAFASSSTLHGLAHIFSYERLSLKRALWALCFLGSLAVLLCVCTERVQYYFHYHHVTKLDEVAASQLTFPAVTLCNLNEFRFSQVSKNDLYHAGELLALLNNRYEIPDTQMADEKQLEILQDKANFRSFKPKPFNMREFYDRAGHDIRDMLLSCHFRGEVCSAEDFKVVFTRYGKCYTFNSGRDGRPRLKTMKGGTGNGLEIMLDIQQDEYLPVWGETDETSFEAGIKVQIHSQDEPPFIDQLGFGVAPGFQTFVACQEQRLIYLPPPWGTCKAVTMDSDLDFFDSYSITACRIDCETRYLVENCNCRMVHMPGDAPYCTPEQYKECADPALDFLVEKDQEYCVCEMPCNLTRYGKELSMVKIPSKASAKYLAKKFNKSEQYIGENILVLDIFFEVLNYETIEQKKAYEIAGLLGDIGGQMGLFIGASILTVLELFDYAYEVIKHKLCRRGKCQKEAKRSSADKGVALSLDDVKRHNPCESLRGHPAGMTYAANILPHHPARGTFEDFTC
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:21036899, PubMed:32915133, PubMed:34319232). Upon extracellular pH drop this channel elicits transient, fast activating, and completely desensitizing inward currents (PubMed:21036899). Displays high selectivity for sodium ions but can also permit the permeation of other cations (PubMed:21036899). 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 (By similarity). {ECO:0000250|UniProtKB:Q6NXK8, ECO:0000269|PubMed:21036899, ECO:0000269|PubMed:32915133, ECO:0000269|PubMed:34319232}.; FUNCTION: [Isoform Asic1a]: Has high selectivity for sodium ions, but can also be permeable to other cations including calcium, lithium and potassium. {ECO:0000269|PubMed:21036899}.; FUNCTION: [Isoform Asic1b]: Produces acid activated currents with a reduced amplitude and inactivates faster (PubMed:21036899). 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 (PubMed:21036899). Also potentially permeable to lithium and potassium (PubMed:21036899). {ECO:0000269|PubMed:21036899}.; FUNCTION: [Isoform 1]: Has no measurable proton-gated sodium channel activity in vitro. {ECO:0000269|PubMed:21036899}.
uniprot
proteins
mass_dalton
59909
uniprot
proteins
mutagenesis
MUTAGEN 102; /note="Q->R: Decreased inhibition by mambalgin-1; when associated with E-167."; /evidence="ECO:0000269|PubMed:32915133"; MUTAGEN 155; /note="R->L,F: Decreased inhibition by mambalgin-1."; /evidence="ECO:0000269|PubMed:32915133"; MUTAGEN 167; /note="D->E: Decreased inhibition by mambalgin-1; when associated with R-102."; /evidence="ECO:0000269|PubMed:32915133"; MUTAGEN 347; /note="D->A: Loss of inhibition by mambalgin-1. Changed pH-gating as lower pH is required for activation."; /evidence="ECO:0000269|PubMed:32915133"; MUTAGEN 351; /note="D->G: Decreased inhibition by mambalgin-1. Changed pH-gating as lower pH is required for activation."; /evidence="ECO:0000269|PubMed:32915133"; MUTAGEN 352; /note="F->L: Complete loss in the shift of pH for both activation and desensitization by the spider venom psalmotoxin-1. Decreased inhibition by mambalgin-1."; /evidence="ECO:0000269|PubMed:19654327, ECO:0000269|PubMed:32915133"; MUTAGEN 357; /note="D->A,N: Changed pH-gating as lower pH is required for activation."; /evidence="ECO:0000269|PubMed:19654327"; MUTAGEN 360; /note="Y->A: Loss of inhibition by mambalgin-1."; /evidence="ECO:0000269|PubMed:32915133"; MUTAGEN 478; /note="S->A: No effect on phosphorylation."; /evidence="ECO:0000269|PubMed:12578970"; MUTAGEN 479; /note="S->A: Loss of phosphorylation."; /evidence="ECO:0000269|PubMed:12578970
uniprot
proteins
post_translational_modification
PTM: pH-gating could be regulated by serine proteases. {ECO:0000269|PubMed:15247234}.; PTM: Phosphorylation by PKA regulates interaction with PICK1 and subcellular localization (PubMed:12578970). Phosphorylation by PKC may regulate the channel (PubMed:12244121). {ECO:0000269|PubMed:12244121, ECO:0000269|PubMed:12578970}.
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
11802773
uniprot
proteins
pubmed
12244121
uniprot
proteins
pubmed
12578970
uniprot
proteins
pubmed
15247234
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
19654327
uniprot
proteins
pubmed
21036899
uniprot
proteins
pubmed
22760635
uniprot
proteins
pubmed
23034652
uniprot
proteins
pubmed
28327374
uniprot
proteins
pubmed
32915133
uniprot
proteins
pubmed
34319232
uniprot
proteins
pubmed
9037075
uniprot
proteins
sequence_length
528
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12578970, ECO:0000269|PubMed:21036899}; Multi-pass membrane protein {ECO:0000269|PubMed:32915133, ECO:0000269|PubMed:34319232}. 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:0000250|UniProtKB:P55926}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 50..66; /note="Helical"; /evidence="ECO:0000305|PubMed:34319232, ECO:0007744|PDB:7RNN"; TRANSMEM 428..458; /note="Discontinuously helical"; /evidence="ECO:0000305|PubMed:34319232, ECO:0007744|PDB:7RNN
uniprot
proteins