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Acid-sensing ion channel 3 (ASIC3) (Amiloride-sensitive cation channel 3) (Dorsal root ASIC) (DRASIC)

 ASIC3_RAT               Reviewed;         533 AA.
O35240;
13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
22-NOV-2017, entry version 130.
RecName: Full=Acid-sensing ion channel 3;
Short=ASIC3;
AltName: Full=Amiloride-sensitive cation channel 3;
AltName: Full=Dorsal root ASIC;
Short=DRASIC;
Name=Asic3; Synonyms=Accn3, Drasic;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=9261094; DOI=10.1074/jbc.272.34.20975;
Waldmann R., Bassilana F., de Weille J.R., Champigny G., Heurteaux C.,
Lazdunski M.;
"Molecular cloning of a non-inactivating proton-gated Na+ channel
specific for sensory neurons.";
J. Biol. Chem. 272:20975-20978(1997).
[2]
INTERACTION WITH ASIC1.
STRAIN=Wistar; TISSUE=Brain;
PubMed=9368048; DOI=10.1074/jbc.272.47.29778;
Lingueglia E., de Weille J.R., Bassilana F., Heurteaux C., Sakai H.,
Waldmann R., Lazdunski M.;
"A modulatory subunit of acid sensing ion channels in brain and dorsal
root ganglion cells.";
J. Biol. Chem. 272:29778-29783(1997).
[3]
TISSUE SPECIFICITY.
PubMed=9707631; DOI=10.1073/pnas.95.17.10240;
Chen C.-C., England S., Akopian A.N., Wood J.N.;
"A sensory neuron-specific, proton-gated ion channel.";
Proc. Natl. Acad. Sci. U.S.A. 95:10240-10245(1998).
[4]
MUTAGENESIS OF VAL-20; PHE-21 AND THR-26.
PubMed=10187795; DOI=10.1074/jbc.274.15.10129;
Coscoy S., de Weille J.R., Lingueglia E., Lazdunski M.;
"The pre-transmembrane 1 domain of acid-sensing ion channels
participates in the ion pore.";
J. Biol. Chem. 274:10129-10132(1999).
[5]
TISSUE SPECIFICITY.
PubMed=10842183; DOI=10.1074/jbc.M004114200;
Babinski K., Catarsi S., Biagini G., Seguela P.;
"Mammalian ASIC2a and ASIC3 subunits co-assemble into heteromeric
proton-gated channels sensitive to Gd3+.";
J. Biol. Chem. 275:28519-28525(2000).
[6]
INDUCTION, AND INHIBITION BY DRUGS.
PubMed=11588175;
Voilley N., de Weille J.R., Mamet J., Lazdunski M.;
"Nonsteroid anti-inflammatory drugs inhibit both the activity and the
inflammation-induced expression of acid-sensing ion channels in
nociceptors.";
J. Neurosci. 21:8026-8033(2001).
[7]
REGULATION BY LACTATE, AND FUNCTION.
PubMed=11528414; DOI=10.1038/nn0901-869;
Immke D.C., McCleskey E.W.;
"Lactate enhances the acid-sensing Na+ channel on ischemia-sensing
neurons.";
Nat. Neurosci. 4:869-870(2001).
[8]
REGULATION BY NPFF.
PubMed=11587714; DOI=10.1016/S0028-3908(01)00107-1;
Catarsi S., Babinski K., Seguela P.;
"Selective modulation of heteromeric ASIC proton-gated channels by
neuropeptide FF.";
Neuropharmacology 41:592-600(2001).
[9]
FUNCTION.
PubMed=11120882; DOI=10.1073/pnas.98.2.711;
Sutherland S.P., Benson C.J., Adelman J.P., McCleskey E.W.;
"Acid-sensing ion channel 3 matches the acid-gated current in cardiac
ischemia-sensing neurons.";
Proc. Natl. Acad. Sci. U.S.A. 98:711-716(2001).
[10]
INDUCTION.
PubMed=12486159;
Mamet J., Baron A., Lazdunski M., Voilley N.;
"Proinflammatory mediators, stimulators of sensory neuron excitability
via the expression of acid-sensing ion channels.";
J. Neurosci. 22:10662-10670(2002).
[11]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=11842212; DOI=10.1073/pnas.042688199;
Alvarez de la Rosa D., Zhang P., Shao D., White F., Canessa C.M.;
"Functional implications of the localization and activity of acid-
sensitive channels in rat peripheral nervous system.";
Proc. Natl. Acad. Sci. U.S.A. 99:2326-2331(2002).
[12]
DEVELOPMENTAL STAGE, AND INDUCTION BY NGFB.
PubMed=14522957; DOI=10.1074/jbc.M309468200;
Mamet J., Lazdunski M., Voilley N.;
"How nerve growth factor drives physiological and inflammatory
expressions of acid-sensing ion channel 3 in sensory neurons.";
J. Biol. Chem. 278:48907-48913(2003).
[13]
REGULATION BY LACTATE AND CALCIUM.
PubMed=12526774; DOI=10.1016/S0896-6273(02)01130-3;
Immke D.C., McCleskey E.W.;
"Protons open acid-sensing ion channels by catalyzing relief of Ca2+
blockade.";
Neuron 37:75-84(2003).
[14]
FUNCTION.
PubMed=12668052; DOI=10.1016/S0028-3908(03)00047-9;
Deval E., Baron A., Lingueglia E., Mazarguil H., Zajac J.-M.,
Lazdunski M.;
"Effects of neuropeptide SF and related peptides on acid sensing ion
channel 3 and sensory neuron excitability.";
Neuropharmacology 44:662-671(2003).
[15]
INHIBITION BY APETX2 TOXIN.
PubMed=15044953; DOI=10.1038/sj.emboj.7600177;
Diochot S., Baron A., Rash L.D., Deval E., Escoubas P., Scarzello S.,
Salinas M., Lazdunski M.;
"A new sea anemone peptide, APETx2, inhibits ASIC3, a major acid-
sensitive channel in sensory neurons.";
EMBO J. 23:1516-1525(2004).
[16]
MUTAGENESIS OF THR-40 AND SER-523, AND PHOSPHORYLATION AT THR-40 AND
SER-523.
PubMed=14976185; DOI=10.1074/jbc.M313078200;
Deval E., Salinas M., Baron A., Lingueglia E., Lazdunski M.;
"ASIC2b-dependent regulation of ASIC3, an essential acid-sensing ion
channel subunit in sensory neurons via the partner protein PICK-1.";
J. Biol. Chem. 279:19531-19539(2004).
[17]
INTERACTION WITH DLG4, AND SUBCELLULAR LOCATION.
PubMed=15317815; DOI=10.1074/jbc.M405874200;
Hruska-Hageman A.M., Benson C.J., Leonard A.S., Price M.P.,
Welsh M.J.;
"PSD-95 and Lin-7b interact with acid-sensing ion channel-3 and have
opposite effects on H+- gated current.";
J. Biol. Chem. 279:46962-46968(2004).
[18]
FUNCTION, INTERACTION WITH STOM, AND SUBCELLULAR LOCATION.
PubMed=22850675; DOI=10.1038/emboj.2012.203;
Brand J., Smith E.S., Schwefel D., Lapatsina L., Poole K.,
Omerbasic D., Kozlenkov A., Behlke J., Lewin G.R., Daumke O.;
"A stomatin dimer modulates the activity of acid-sensing ion
channels.";
EMBO J. 31:3635-3646(2012).
[19]
SUBUNIT, AND INTERACTION WITH CONO-RFAMIDE CNF-TX1.1.
PubMed=28396446; DOI=10.1073/pnas.1616232114;
Reimers C., Lee C.H., Kalbacher H., Tian Y., Hung C.H., Schmidt A.,
Prokop L., Kauferstein S., Mebs D., Chen C.C., Gruender S.;
"Identification of a cono-RFamide from the venom of Conus textile that
targets ASIC3 and enhances muscle pain.";
Proc. Natl. Acad. Sci. U.S.A. 114:E3507-E3515(2017).
-!- FUNCTION: Cation channel with high affinity for sodium, which is
gated by extracellular protons and inhibited by the diuretic
amiloride. Generates a biphasic current with a fast inactivating
and a slow sustained phase. In sensory neurons is proposed to
mediate the pain induced by acidosis that occurs in ischemic,
damaged or inflamed tissue. May be involved in hyperalgesia. May
play a role in mechanoreception. Heteromeric channel assembly
seems to modulate channel properties.
{ECO:0000269|PubMed:11120882, ECO:0000269|PubMed:11528414,
ECO:0000269|PubMed:12668052, ECO:0000269|PubMed:22850675,
ECO:0000269|PubMed:28396446}.
-!- SUBUNIT: Homotrimer or heterotrimer with other ASIC proteins (By
similarity). Interacts with LIN7B, MAGI1 and GOPC (By similarity).
Interacts with DLG4 and ASIC2. Interacts with STOM; this regulates
channel activity. Homotrimeric ASIC3 and ASIC3-containing
heterotrimers interact with the cono-RFamide CNF-Tx1.1, and
probably CNF-Tx1.2 and CNF-Tx1.3 (AC P0DL71) (PubMed:28396446).
{ECO:0000250, ECO:0000269|PubMed:15317815,
ECO:0000269|PubMed:22850675, ECO:0000269|PubMed:28396446,
ECO:0000269|PubMed:9368048}.
-!- INTERACTION:
Q63ZW7-3:Patj (xeno); NbExp=2; IntAct=EBI-982374, EBI-8158524;
Q9JJ19:Slc9a3r1; NbExp=5; IntAct=EBI-982374, EBI-982391;
Q920G2:Slc9a3r2; NbExp=2; IntAct=EBI-982374, EBI-982439;
P54116:Stom (xeno); NbExp=3; IntAct=EBI-982374, EBI-8004826;
D4A100:Stoml3; NbExp=2; IntAct=EBI-982374, EBI-15615743;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
{ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=In
part cytoplasmic in cochlea cells (By similarity). Cell surface
expression may be stabilized by interaction with LIN7B and
cytoplasmic retention by interaction with DLG4. {ECO:0000250,
ECO:0000269|PubMed:11842212, ECO:0000269|PubMed:15317815,
ECO:0000269|PubMed:22850675}.
-!- TISSUE SPECIFICITY: Expressed in sciatic nerve and dorsal root
ganglion (at protein level). Expressed in sensory neurons of
dorsal root ganglion. Expressed in Golgi interneurons in the
granular layer. Also found in superior cervical ganglia, spinal
chord and brain stem. {ECO:0000269|PubMed:10842183,
ECO:0000269|PubMed:11842212, ECO:0000269|PubMed:9261094,
ECO:0000269|PubMed:9707631}.
-!- DEVELOPMENTAL STAGE: Expression is first detected at E15.5.
Strongly expressed perinatally. {ECO:0000269|PubMed:14522957}.
-!- INDUCTION: Transcriptionally regulated by the proinflamatory
mediators nerve growth factor, serotonin, interleukin-1 and
bradykinin. Up-regulation upon tissues inflammation is abolished
by anti-inflammatory drugs. {ECO:0000269|PubMed:11588175,
ECO:0000269|PubMed:12486159, ECO:0000269|PubMed:14522957}.
-!- DOMAIN: The PDZ domain-binding motif is involved in interaction
with LIN7A, GOPC and MAGI1/BAIAP1. {ECO:0000250}.
-!- PTM: Phosphorylated by PKA (By similarity). Phosphorylated by PKC.
In vitro, PRKCABP/PICK-1 is necessary for PKC phosphorylation and
activation of a ASIC3/ACCN3-ASIC2/ASIC2b channel, but does not
activate a homomeric ASIC3/ACCN3 channel. {ECO:0000250,
ECO:0000269|PubMed:14976185}.
-!- MISCELLANEOUS: Potentiated by FMRFamide-related neuropeptides (By
similarity). Sensitized and potentiated by NPFF and NPSF.
Regulated by lactate and Ca(2+). Specifically inhibited by APETx2,
a sea anemone toxin. Inhibited by anti-inflammatory drugs like
salicylic acid. {ECO:0000250}.
-!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
1.A.6) family. ASIC3 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AF013598; AAB69328.1; -; mRNA.
RefSeq; NP_775158.1; NM_173135.1.
UniGene; Rn.24225; -.
ProteinModelPortal; O35240; -.
SMR; O35240; -.
DIP; DIP-35759N; -.
IntAct; O35240; 5.
MINT; MINT-1777886; -.
STRING; 10116.ENSRNOP00000011300; -.
BindingDB; O35240; -.
ChEMBL; CHEMBL5757; -.
TCDB; 1.A.6.1.2; the epithelial na(+) channel (enac) family.
iPTMnet; O35240; -.
PhosphoSitePlus; O35240; -.
PaxDb; O35240; -.
PRIDE; O35240; -.
Ensembl; ENSRNOT00000011300; ENSRNOP00000011300; ENSRNOG00000008380.
GeneID; 286920; -.
KEGG; rno:286920; -.
CTD; 9311; -.
RGD; 708578; Asic3.
eggNOG; KOG4294; Eukaryota.
eggNOG; ENOG410ZNFK; LUCA.
GeneTree; ENSGT00760000119120; -.
HOGENOM; HOG000247010; -.
HOVERGEN; HBG004150; -.
InParanoid; O35240; -.
KO; K04830; -.
OMA; TRMGQCY; -.
OrthoDB; EOG091G053J; -.
PhylomeDB; O35240; -.
TreeFam; TF330663; -.
Reactome; R-RNO-2672351; Stimuli-sensing channels.
PRO; PR:O35240; -.
Proteomes; UP000002494; Chromosome 4.
Bgee; ENSRNOG00000008380; -.
Genevisible; O35240; RN.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
GO; GO:0005261; F:cation channel activity; ISO:RGD.
GO; GO:0042931; F:enterobactin transporter activity; ISO:RGD.
GO; GO:0015280; F:ligand-gated sodium channel activity; IDA:MGI.
GO; GO:0030165; F:PDZ domain binding; IMP:RGD.
GO; GO:0006812; P:cation transport; ISO:RGD.
GO; GO:0050907; P:detection of chemical stimulus involved in sensory perception; ISO:RGD.
GO; GO:0050968; P:detection of chemical stimulus involved in sensory perception of pain; ISO:RGD.
GO; GO:0050974; P:detection of mechanical stimulus involved in sensory perception; ISO:RGD.
GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; ISO:RGD.
GO; GO:0050961; P:detection of temperature stimulus involved in sensory perception; ISO:RGD.
GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; ISO:RGD.
GO; GO:0034220; P:ion transmembrane transport; ISO:RGD.
GO; GO:0010447; P:response to acidic pH; IDA:MGI.
GO; GO:0009408; P:response to heat; ISO:RGD.
GO; GO:0009612; P:response to mechanical stimulus; ISO:RGD.
GO; GO:0050915; P:sensory perception of sour taste; ISO:RGD.
GO; GO:0006814; P:sodium ion transport; IDA:MGI.
InterPro; IPR001873; ENaC.
InterPro; IPR004724; ENaC_chordates.
InterPro; IPR020903; ENaC_CS.
PANTHER; PTHR11690; PTHR11690; 1.
Pfam; PF00858; ASC; 1.
PRINTS; PR01078; AMINACHANNEL.
TIGRFAMs; TIGR00859; ENaC; 1.
PROSITE; PS01206; ASC; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Cytoplasm; Disulfide bond;
Glycoprotein; Ion channel; Ion transport; Membrane; Phosphoprotein;
Reference proteome; Sodium; Sodium channel; Sodium transport;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 533 Acid-sensing ion channel 3.
/FTId=PRO_0000181303.
TOPO_DOM 1 19 Cytoplasmic. {ECO:0000255}.
TRANSMEM 20 40 Helical. {ECO:0000255}.
TOPO_DOM 41 435 Extracellular. {ECO:0000255}.
TRANSMEM 436 456 Helical. {ECO:0000255}.
TOPO_DOM 457 533 Cytoplasmic. {ECO:0000255}.
MOTIF 530 533 PDZ-binding. {ECO:0000250}.
SITE 26 26 Potassium ion selectivity and
permeability.
MOD_RES 40 40 Phosphothreonine; by PKC.
{ECO:0000305|PubMed:14976185}.
MOD_RES 523 523 Phosphoserine; by PKC.
{ECO:0000305|PubMed:14976185}.
CARBOHYD 176 176 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 400 400 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 93 187 {ECO:0000250}.
DISULFID 165 172 {ECO:0000250}.
DISULFID 283 372 {ECO:0000250}.
DISULFID 317 368 {ECO:0000250}.
DISULFID 321 366 {ECO:0000250}.
DISULFID 330 352 {ECO:0000250}.
DISULFID 332 344 {ECO:0000250}.
MUTAGEN 20 20 V->P: No effect on selectivity or channel
function. {ECO:0000269|PubMed:10187795}.
MUTAGEN 21 21 F->S: Loss of channel function.
{ECO:0000269|PubMed:10187795}.
MUTAGEN 26 26 T->K: Alters selectivity of the channel
for sodium. No effect on channel
function. {ECO:0000269|PubMed:10187795}.
MUTAGEN 40 40 T->G: Loss of regulation by PKC through
PRKCABP; when associated with G-523.
{ECO:0000269|PubMed:14976185}.
MUTAGEN 523 523 S->G: Loss of regulation by PKC through
PRKCABP; when associated with G-40.
{ECO:0000269|PubMed:14976185}.
SEQUENCE 533 AA; 59227 MW; 294B57322C74B3DC CRC64;
MKPRSGLEEA QRRQASDIRV FASSCTMHGL GHIFGPGGLT LRRGLWATAV LLSLAAFLYQ
VAERVRYYGE FHHKTTLDER ESHQLTFPAV TLCNINPLRR SRLTPNDLHW AGTALLGLDP
AEHAAYLRAL GQPPAPPGFM PSPTFDMAQL YARAGHSLED MLLDCRYRGQ PCGPENFTVI
FTRMGQCYTF NSGAHGAELL TTPKGGAGNG LEIMLDVQQE EYLPIWKDME ETPFEVGIRV
QIHSQDEPPA IDQLGFGAAP GHQTFVSCQQ QQLSFLPPPW GDCNTASLDP DDFDPEPSDP
LGSPRPRPSP PYSLIGCRLA CESRYVARKC GCRMMHMPGN SPVCSPQQYK DCASPALDAM
LRKDTCVCPN PCATTRYAKE LSMVRIPSRA SARYLARKYN RSESYITENV LVLDIFFEAL
NYEAVEQKAA YEVSELLGDI GGQMGLFIGA SLLTILEILD YLCEVFQDRV LGYFWNRRSA
QKRSGNTLLQ EELNGHRTHV PHLSLGPRPP TTPCAVTKTL SASHRTCYLV TRL


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