Asic2
entrez
25364
canonical
uniprot
Q62962
canonical
ensembl
ENSRNOG00000058308
resolver
ensp
ENSRNOP00000068763
resolver
genesymbol
Asic2
resolver
genesymbol_syn
Accn1
resolver
genesymbol_syn
Bnac1
resolver
uniprot
O55163
resolver
uniprot_entry
ASIC2_RAT
resolver
uniprot_sec
O55163
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by the diuretic drug amiloride (PubMed:10842183, PubMed:9368048). Inhibited by gadolinium ions, the heterotrimer with ASIC3 being more sensitive (PubMed:10842183). Zn(2+) potentiates the acid activation of ASIC2-containing homomeric and heteromeric channels (PubMed:11457851). The snake venom mambalgin-1 and mambalgin-2 inhibit the homotrimers composed of ASIC1 and ASIC2 and have strong analgesic effects (PubMed:23034652). {ECO:0000269|PubMed:10842183, ECO:0000269|PubMed:11457851, ECO:0000269|PubMed:23034652, ECO:0000269|PubMed:9368048}.
uniprot
proteins
amino_acid_sequence
MDLKESPSEGSLQPSSIQIFANTSTLHGIRHIFVYGPLTIRRVLWAVAFVGSLGLLLVESSERVSYYFSYQHVTKVDEVVAQSLVFPAVTLCNLNGFRFSRLTTNDLYHAGELLALLDVNLQIPDPHLADPTVLEALRQKANFKHYKPKQFSMLEFLHRVGHDLKDMMLYCKFKGQECGHQDFTTVFTKYGKCYMFNSGEDGKPLLTTVKGGTGNGLEIMLDIQQDEYLPIWGETEETTFEAGVKVQIHSQSEPPFIQELGFGVAPGFQTFVATQEQRLTYLPPPWGECRSSEMGLDFFPVYSITACRIDCETRYIVENCNCRMVHMPGDAPFCTPEQHKECAEPALGLLAEKDSNYCLCRTPCNLTRYNKELSMVKIPSKTSAKYLEKKFNKSEKYISENILVLDIFFEALNYETIEQKKAYEVAALLGDIGGQMGLFIGASLLTILELFDYIYELIKEKLLDLLGKEEEEGSHDENMSTCDTMPNHSETISHTVNVPLQTALGTLEEIAC
uniprot
proteins
function
FUNCTION: Forms pH-gated trimeric sodium channels that act as postsynaptic excitatory sensors in the nervous system (PubMed:10842183, PubMed:22850675, PubMed:8631835, PubMed:9360943, PubMed:9368048). Upon extracellular acidification, these channels generate rapid, transient inward currents that fully desensitize (PubMed:10842183, PubMed:8631835, PubMed:9368048). Highly selective for sodium, they are permeable to other cations (PubMed:8631835). By forming heterotrimeric channels with ASIC1, could contribute to synaptic plasticity, learning, and memory. Additionally, as acid sensors at nerve terminals, plays a role in mechanosensation and phototransduction (By similarity). {ECO:0000250|UniProtKB:Q925H0, ECO:0000269|PubMed:10842183, ECO:0000269|PubMed:22850675, ECO:0000269|PubMed:8631835, ECO:0000269|PubMed:9360943, ECO:0000269|PubMed:9368048}.; FUNCTION: [Isoform 2]: Has no pH-gated sodium channel activity per se but can associate with other ASICs to produce functional channels with specific properties. {ECO:0000269|PubMed:9368048}.
uniprot
proteins
mass_dalton
57739
uniprot
proteins
mutagenesis
MUTAGEN 4; /note="K->N: No effect on N-glycosylation."; /evidence="ECO:0000269|PubMed:15504740"; MUTAGEN 22; /note="N->S: No effect on N-glycosylation."; /evidence="ECO:0000269|PubMed:15504740"; MUTAGEN 37; /note="P->N: No effect on N-glycosylation."; /evidence="ECO:0000269|PubMed:15504740"; MUTAGEN 63; /note="R->N: No effect on N-glycosylation."; /evidence="ECO:0000269|PubMed:15504740"; MUTAGEN 67; /note="Y->N: No effect on N-glycosylation."; /evidence="ECO:0000269|PubMed:15504740"; MUTAGEN 72; /note="H->A: Inactive. Active at lower pH; when associated with V-430."; /evidence="ECO:0000269|PubMed:11457851, ECO:0000269|PubMed:15504740"; MUTAGEN 72; /note="H->N: Increases N-glycosylation."; /evidence="ECO:0000269|PubMed:11457851, ECO:0000269|PubMed:15504740"; MUTAGEN 81; /note="A->N: Increases N-glycosylation."; /evidence="ECO:0000269|PubMed:15504740"; MUTAGEN 109; /note="H->A: No effect on pH dependence and function."; /evidence="ECO:0000269|PubMed:11457851"; MUTAGEN 127; /note="H->A: No effect on pH dependence and function."; /evidence="ECO:0000269|PubMed:11457851"; MUTAGEN 145; /note="H->A: No effect on pH dependence and function."; /evidence="ECO:0000269|PubMed:11457851"; MUTAGEN 158; /note="H->A: No effect on pH dependence and function."; /evidence="ECO:0000269|PubMed:11457851"; MUTAGEN 162; /note="H->A: Loss of potentiation by Zn(2+)."; /evidence="ECO:0000269|PubMed:11457851"; MUTAGEN 180; /note="H->A: No effect on pH dependence and function."; /evidence="ECO:0000269|PubMed:11457851"; MUTAGEN 249; /note="H->A: No effect on pH dependence and function."; /evidence="ECO:0000269|PubMed:11457851"; MUTAGEN 326; /note="H->A: No effect on pH dependence and function."; /evidence="ECO:0000269|PubMed:11457851"; MUTAGEN 339; /note="H->A: Loss of potentiation by Zn(2+)."; /evidence="ECO:0000269|PubMed:11457851"; MUTAGEN 365; /note="N->S: Reduces N-glycosylation. Abolishes N-glycosylation; when associated with S-392."; /evidence="ECO:0000269|PubMed:15504740"; MUTAGEN 392; /note="N->S: Reduces N-glycosylation. Abolishes N-glycosylation; when associated with S-365."; /evidence="ECO:0000269|PubMed:15504740"; MUTAGEN 414; /note="Y->N: Increases N-glycosylation."; /evidence="ECO:0000269|PubMed:15504740"; MUTAGEN 423..425; /note="YEV->NES: Increases N-glycosylation."; /evidence="ECO:0000269|PubMed:15504740"; MUTAGEN 430; /note="G->C: Partial activation."; /evidence="ECO:0000269|PubMed:11457851, ECO:0000269|PubMed:8631835"; MUTAGEN 430; /note="G->F: Constitutive activation causing cell death. Inactive; when associated with F-443."; /evidence="ECO:0000269|PubMed:11457851, ECO:0000269|PubMed:8631835"; MUTAGEN 430; /note="G->K,T: Constitutive activation causing cell death."; /evidence="ECO:0000269|PubMed:11457851, ECO:0000269|PubMed:8631835"; MUTAGEN 430; /note="G->S: No constitutive activation."; /evidence="ECO:0000269|PubMed:11457851, ECO:0000269|PubMed:8631835"; MUTAGEN 430; /note="G->V: Constitutive activation causing cell death. Activated at lower pH; when associated with A-72."; /evidence="ECO:0000269|PubMed:11457851, ECO:0000269|PubMed:8631835"; MUTAGEN 443; /note="S->F: Loss of function. Inactive; when associated with F-430."; /evidence="ECO:0000269|PubMed:8631835"; MUTAGEN 453..455; /note="YIY->NIS: No effect on N-glycosylation."; /evidence="ECO:0000269|PubMed:15504740"; MUTAGEN 478; /note="N->S: No effect on N-glycosylation."; /evidence="ECO:0000269|PubMed:15504740"; MUTAGEN 487; /note="N->S: No effect on N-glycosylation."; /evidence="ECO:0000269|PubMed:15504740"; MUTAGEN Q62962-2:60; /note="S->G: Reduces activation by PKC through PICK1 of ASIC2/ASIC2 channels."; /evidence="ECO:0000269|PubMed:14976185"; MUTAGEN Q62962-2:481; /note="G->F,K: Not constitutively activated."; /evidence="ECO:0000269|PubMed:9368048
uniprot
proteins
protein_family
ASIC2 subfamily
uniprot
proteins
protein_family
Amiloride-sensitive sodium channel (TC 1.A.6) family
uniprot
proteins
pubmed
10842183
uniprot
proteins
pubmed
11457851
uniprot
proteins
pubmed
11588175
uniprot
proteins
pubmed
11842212
uniprot
proteins
pubmed
14976185
uniprot
proteins
pubmed
15504740
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
22850675
uniprot
proteins
pubmed
23034652
uniprot
proteins
pubmed
8631835
uniprot
proteins
pubmed
9360943
uniprot
proteins
pubmed
9368048
uniprot
proteins
sequence_length
512
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10842183, ECO:0000269|PubMed:11842212, ECO:0000269|PubMed:15504740}; Multi-pass membrane protein {ECO:0000269|PubMed:15504740}. Note=Localized at the plasma membrane of neurons, in the soma and punctated peripheral processes. {ECO:0000250|UniProtKB:Q925H0}.
uniprot
proteins
transmembrane_region
TRANSMEM 38..58; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 428..448; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins