Asic3
entrez
286920
canonical
uniprot
O35240
canonical
ensembl
ENSRNOG00000008380
resolver
ensembl
ENSRNOG00055022738
resolver
ensembl
ENSRNOG00060022384
resolver
ensembl
ENSRNOG00065017478
resolver
ensp
ENSRNOP00000011300
resolver
ensp
ENSRNOP00000107682
resolver
ensp
ENSRNOP00055031698
resolver
ensp
ENSRNOP00060032063
resolver
ensp
ENSRNOP00065023149
resolver
enst
ENSRNOT00000011300
resolver
enst
ENSRNOT00000165465
resolver
enst
ENSRNOT00055039031
resolver
enst
ENSRNOT00060038811
resolver
enst
ENSRNOT00065029200
resolver
genesymbol
Asic3
resolver
genesymbol_syn
Accn3
resolver
genesymbol_syn
Drasic
resolver
uniprot
A0ABK0LU69
resolver
uniprot_entry
A0ABK0LU69_RAT
resolver
uniprot_entry
ASIC3_RAT
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by the diuretic drug amiloride (PubMed:10842183, PubMed:9261094). Inhibited by gadolinium ions (PubMed:10842183). Inhibited by extracellular Ca(2+) (PubMed:11120882, PubMed:12526774). Activated by lactate (PubMed:11528414, PubMed:12526774). Salicylic acid, diclofenac and aspirin inhibit the sustained current component (PubMed:11588175). Activated by the vertebrate neuropeptides NPFF and NPSF, and the related FMRFamide (PubMed:11587714, PubMed:12668052). Specifically and reversibly inhibited by the a sea anemone toxin APETx2 (PubMed:15044953). ASIC3-containing channels are potentiated by the cono-RFamide CNF-Tx1.1, and probably CNF-Tx1.2 and CNF-Tx1.3 (AC P0DL71) (PubMed:28396446). {ECO:0000269|PubMed:10842183, ECO:0000269|PubMed:11120882, ECO:0000269|PubMed:11528414, ECO:0000269|PubMed:11587714, ECO:0000269|PubMed:11588175, ECO:0000269|PubMed:12526774, ECO:0000269|PubMed:12668052, ECO:0000269|PubMed:15044953, ECO:0000269|PubMed:28396446, ECO:0000269|PubMed:9261094}.
uniprot
proteins
amino_acid_sequence
MKPRSGLEEAQRRQASDIRVFASSCTMHGLGHIFGPGGLTLRRGLWATAVLLSLAAFLYQVAERVRYYGEFHHKTTLDERESHQLTFPAVTLCNINPLRRSRLTPNDLHWAGTALLGLDPAEHAAYLRALGQPPAPPGFMPSPTFDMAQLYARAGHSLEDMLLDCRYRGQPCGPENFTVIFTRMGQCYTFNSGAHGAELLTTPKGGAGNGLEIMLDVQQEEYLPIWKDMEETPFEVGIRVQIHSQDEPPAIDQLGFGAAPGHQTFVSCQQQQLSFLPPPWGDCNTASLDPDDFDPEPSDPLGSPRPRPSPPYSLIGCRLACESRYVARKCGCRMMHMPGNSPVCSPQQYKDCASPALDAMLRKDTCVCPNPCATTRYAKELSMVRIPSRASARYLARKYNRSESYITENVLVLDIFFEALNYEAVEQKAAYEVSELLGDIGGQMGLFIGASLLTILEILDYLCEVFQDRVLGYFWNRRSAQKRSGNTLLQEELNGHRTHVPHLSLGPRPPTTPCAVTKTLSASHRTCYLVTRL
uniprot
proteins
function
FUNCTION: Forms pH-gated heterotrimeric sodium channels that act as postsynaptic excitatory receptors in the nervous system (PubMed:10842183, PubMed:11120882, PubMed:11587714, PubMed:9261094). Upon extracellular acidification, these channels generate a biphasic current with a fast inactivating and a slow sustained phase (PubMed:10842183, PubMed:11120882). ASIC3 is more sensitive to protons and gates between closed, open, and desensitized states faster than other ASICs (PubMed:11120882). Displays high selectivity for sodium ions but can also permit the permeation of other cations (PubMed:10842183, PubMed:11120882). As a neuronal acid sensor, probably contributes to mechanoreception, acid nociception, and heat nociception (By similarity). By forming heterotrimeric channels with ASIC2, generates a biphasic current with a fast inactivating and a slow sustained phase, which in sensory neurons is proposed to mediate the pain induced by acidosis that occurs in ischemic, damaged or inflamed tissues (PubMed:10842183, PubMed:11120882, PubMed:28396446, PubMed:9368048). {ECO:0000250|UniProtKB:Q6X1Y6, ECO:0000269|PubMed:10842183, ECO:0000269|PubMed:11120882, ECO:0000269|PubMed:11587714, ECO:0000269|PubMed:28396446, ECO:0000269|PubMed:9261094, ECO:0000269|PubMed:9368048}.
uniprot
proteins
mass_dalton
59227
uniprot
proteins
mutagenesis
MUTAGEN 20; /note="V->P: No effect on ion selectivity or channel function."; /evidence="ECO:0000269|PubMed:10187795"; MUTAGEN 21; /note="F->S: Loss of channel function."; /evidence="ECO:0000269|PubMed:10187795"; MUTAGEN 26; /note="T->K: Alters selectivity of the channel for sodium. No effect on channel function."; /evidence="ECO:0000269|PubMed:10187795"; MUTAGEN 40; /note="T->G: Loss of regulation by PKC; when associated with G-523."; /evidence="ECO:0000269|PubMed:14976185"; MUTAGEN 523; /note="S->G: Loss of regulation by PKC; when associated with G-40."; /evidence="ECO:0000269|PubMed:14976185
uniprot
proteins
post_translational_modification
PTM: Could be phosphorylated by PKC, promoting activation of ASIC2/ASIC3 heterotrimers. {ECO:0000269|PubMed:14976185}.
uniprot
proteins
protein_family
ASIC3 subfamily
uniprot
proteins
protein_family
Amiloride-sensitive sodium channel (TC 1.A.6) family
uniprot
proteins
pubmed
10187795
uniprot
proteins
pubmed
10842183
uniprot
proteins
pubmed
11120882
uniprot
proteins
pubmed
11528414
uniprot
proteins
pubmed
11587714
uniprot
proteins
pubmed
11588175
uniprot
proteins
pubmed
11842212
uniprot
proteins
pubmed
12486159
uniprot
proteins
pubmed
12526774
uniprot
proteins
pubmed
12668052
uniprot
proteins
pubmed
14522957
uniprot
proteins
pubmed
14976185
uniprot
proteins
pubmed
15044953
uniprot
proteins
pubmed
15317815
uniprot
proteins
pubmed
22850675
uniprot
proteins
pubmed
28396446
uniprot
proteins
pubmed
9261094
uniprot
proteins
pubmed
9368048
uniprot
proteins
pubmed
9707631
uniprot
proteins
sequence_length
533
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10842183, ECO:0000269|PubMed:11842212, ECO:0000269|PubMed:15317815, ECO:0000269|PubMed:9261094}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q6X1Y6}. Note=Preferentially expressed at the plasma membrane of the soma and cellular processes of neurons (PubMed:11842212). In part cytoplasmic in cochlea cells (By similarity). Localized in specialized sensory nerve endings (By similarity). {ECO:0000250|UniProtKB:Q6X1Y6, ECO:0000269|PubMed:11842212}.
uniprot
proteins
transmembrane_region
TRANSMEM 20..40; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 436..456; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins