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

 ASIC3_MOUSE             Reviewed;         530 AA.
Q6X1Y6; Q7TQH4;
13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
13-SEP-2005, sequence version 2.
10-OCT-2018, entry version 121.
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;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY,
SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
TISSUE=Inner ear;
PubMed=15051137; DOI=10.1016/S0378-5955(04)00015-2;
Hildebrand M.S., de Silva M.G., Klockars T., Rose E., Price M.,
Smith R.J.H., McGuirt W.T., Christopoulos H., Petit C., Dahl H.-H.M.;
"Characterisation of DRASIC in the mouse inner ear.";
Hear. Res. 190:149-160(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
REGULATION BY FMRFAMIDE-RELATED PEPTIDES.
PubMed=10798398; DOI=10.1016/S0896-6273(00)81144-7;
Askwith C.C., Cheng C., Ikuma M., Benson C., Price M.P., Welsh M.J.;
"Neuropeptide FF and FMRFamide potentiate acid-evoked currents from
sensory neurons and proton-gated DEG/ENaC channels.";
Neuron 26:133-141(2000).
[4]
TISSUE SPECIFICITY, AND FUNCTION.
PubMed=11754838; DOI=10.1016/S0896-6273(01)00547-5;
Price M.P., McIlwrath S.L., Xie J., Cheng C., Qiao J., Tarr D.E.,
Sluka K.A., Brennan T.J., Lewin G.R., Welsh M.J.;
"The DRASIC cation channel contributes to the detection of cutaneous
touch and acid stimuli in mice.";
Neuron 32:1071-1083(2001).
[5]
FUNCTION.
PubMed=12060708; DOI=10.1073/pnas.122245999;
Chen C.-C., Zimmer A., Sun W.-H., Hall J., Brownstein M.J., Zimmer A.;
"A role for ASIC3 in the modulation of high-intensity pain stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 99:8992-8997(2002).
[6]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=14659506; DOI=10.1016/S0304-3959(03)00269-0;
Sluka K.A., Price M.P., Breese N.M., Stucky C.L., Wemmie J.A.,
Welsh M.J.;
"Chronic hyperalgesia induced by repeated acid injections in muscle is
abolished by the loss of ASIC3, but not ASIC1.";
Pain 106:229-239(2003).
[7]
INTERACTION WITH LIN7B; MAGI1; GOPC AND DLG4.
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).
[8]
INTERACTION WITH STOM.
PubMed=15471860; DOI=10.1074/jbc.M407708200;
Price M.P., Thompson R.J., Eshcol J.O., Wemmie J.A., Benson C.J.;
"Stomatin modulates gating of acid-sensing ion channels.";
J. Biol. Chem. 279:53886-53891(2004).
[9]
INTERACTION WITH STOM.
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).
-!- 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:11754838, ECO:0000269|PubMed:12060708,
ECO:0000269|PubMed:14659506}.
-!- SUBUNIT: Homotrimer or heterotrimer with other ASIC proteins (By
similarity). Interacts with DLG4 and ASIC2 (By similarity).
Interacts with LIN7B, MAGI1/BAIAP1 and GOPC. Interacts with STOM;
this regulates channel activity. {ECO:0000250,
ECO:0000269|PubMed:15317815, ECO:0000269|PubMed:15471860,
ECO:0000269|PubMed:22850675}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15051137};
Multi-pass membrane protein {ECO:0000269|PubMed:15051137}.
Cytoplasm {ECO:0000269|PubMed:15051137}. Note=Cell surface
expression may be stabilized by interaction with LIN7B and
cytoplasmic retention by interaction with DLG4 (By similarity). In
part cytoplasmic in cochlea cells. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q6X1Y6-1; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=2;
IsoId=Q6X1Y6-2; Sequence=VSP_015606, VSP_015607;
-!- TISSUE SPECIFICITY: Expressed in liver, lung, kidney, testis,
brain, eye and cochlea. Expressed in spiral ganglion and sensory
hair cells of the organ of Corti in the cochlea (at protein
level). Expressed in dorsal root ganglion innervating muscles and
spinal chord. Expressed in peripheral sensory nerve termimals like
nerves of the Meissner corpuscle, palisades of lanceolate nerve
endings, site of mechanoreception in guard hair follicles, and
Merkel cell-neurite complexes. {ECO:0000269|PubMed:11754838,
ECO:0000269|PubMed:14659506, ECO:0000269|PubMed:15051137}.
-!- PTM: Phosphorylated by PKA. 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 (By similarity). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice display altered responses to mechanical
and acid stimuli. They do not develop chronic hyperalgesia induced
by repeated acid injection. {ECO:0000269|PubMed:15051137}.
-!- MISCELLANEOUS: Sensitized and potentiated by NPFF and NPSF.
Inhibited by anti-inflammatory drugs, like salicylic acid (By
similarity). Potentiated by FMRFamide-related neuropeptides.
Regulated by lactate and Ca(2+). {ECO:0000250}.
-!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
1.A.6) family. ASIC3 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY261387; AAP88539.1; -; mRNA.
EMBL; AC113055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS51433.1; -. [Q6X1Y6-1]
CCDS; CCDS80225.1; -. [Q6X1Y6-2]
RefSeq; NP_001297403.1; NM_001310474.1. [Q6X1Y6-2]
RefSeq; NP_892045.2; NM_183000.2. [Q6X1Y6-1]
UniGene; Mm.299636; -.
ProteinModelPortal; Q6X1Y6; -.
SMR; Q6X1Y6; -.
STRING; 10090.ENSMUSP00000039914; -.
ChEMBL; CHEMBL3232696; -.
iPTMnet; Q6X1Y6; -.
PhosphoSitePlus; Q6X1Y6; -.
PaxDb; Q6X1Y6; -.
PRIDE; Q6X1Y6; -.
Ensembl; ENSMUST00000049346; ENSMUSP00000039914; ENSMUSG00000038276. [Q6X1Y6-2]
Ensembl; ENSMUST00000196296; ENSMUSP00000143083; ENSMUSG00000038276. [Q6X1Y6-1]
GeneID; 171209; -.
KEGG; mmu:171209; -.
UCSC; uc008wrj.1; mouse. [Q6X1Y6-1]
UCSC; uc008wrk.1; mouse. [Q6X1Y6-2]
CTD; 9311; -.
MGI; MGI:2159339; Asic3.
eggNOG; KOG4294; Eukaryota.
eggNOG; ENOG410ZNFK; LUCA.
GeneTree; ENSGT00760000119120; -.
HOGENOM; HOG000247010; -.
HOVERGEN; HBG004150; -.
InParanoid; Q6X1Y6; -.
KO; K04830; -.
OMA; TRMGQCY; -.
OrthoDB; EOG091G053J; -.
PhylomeDB; Q6X1Y6; -.
TreeFam; TF330663; -.
Reactome; R-MMU-2672351; Stimuli-sensing channels.
PRO; PR:Q6X1Y6; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000038276; Expressed in 43 organ(s), highest expression level in cochlea.
CleanEx; MM_ACCN3; -.
ExpressionAtlas; Q6X1Y6; baseline and differential.
Genevisible; Q6X1Y6; MM.
GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005261; F:cation channel activity; IDA:MGI.
GO; GO:0042931; F:enterobactin transmembrane transporter activity; IMP:MGI.
GO; GO:0015280; F:ligand-gated sodium channel activity; ISO:MGI.
GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
GO; GO:0006812; P:cation transport; IDA:MGI.
GO; GO:0050907; P:detection of chemical stimulus involved in sensory perception; IMP:MGI.
GO; GO:0050968; P:detection of chemical stimulus involved in sensory perception of pain; IMP:MGI.
GO; GO:0050974; P:detection of mechanical stimulus involved in sensory perception; IMP:MGI.
GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; IMP:MGI.
GO; GO:0050961; P:detection of temperature stimulus involved in sensory perception; IMP:MGI.
GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; IMP:MGI.
GO; GO:0034220; P:ion transmembrane transport; IMP:MGI.
GO; GO:0010447; P:response to acidic pH; IDA:MGI.
GO; GO:0009408; P:response to heat; IMP:MGI.
GO; GO:0009612; P:response to mechanical stimulus; IMP:MGI.
GO; GO:0050915; P:sensory perception of sour taste; ISO:MGI.
GO; GO:0006814; P:sodium ion transport; ISO: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;
Alternative splicing; 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 1 530 Acid-sensing ion channel 3.
/FTId=PRO_0000181302.
TOPO_DOM 1 43 Cytoplasmic. {ECO:0000255}.
TRANSMEM 44 62 Helical. {ECO:0000255}.
TOPO_DOM 63 440 Extracellular. {ECO:0000255}.
TRANSMEM 441 460 Helical. {ECO:0000255}.
TOPO_DOM 461 530 Cytoplasmic. {ECO:0000255}.
MOTIF 527 530 PDZ-binding. {ECO:0000250}.
SITE 26 26 Potassium ion selectivity and
permeability. {ECO:0000250}.
CARBOHYD 176 176 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 397 397 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 93 187 {ECO:0000250}.
DISULFID 165 172 {ECO:0000250}.
DISULFID 283 369 {ECO:0000250}.
DISULFID 314 365 {ECO:0000250}.
DISULFID 318 363 {ECO:0000250}.
DISULFID 327 349 {ECO:0000250}.
DISULFID 329 341 {ECO:0000250}.
VAR_SEQ 355 440 DAMLRKDTCVCPNPCATTRYAKELSMVRIPSRASARYLARK
YNRSETYITENVLVLDIFFEALNYEAVEQKAAYEVSELLGD
IGGQ -> GRMYWFWISSLKPSTMRPWNKRQLMKCRSCWET
LGDRWDCLSEPACLPSSRSSTTSVRFFKTESWGTSGTEGAL
KGALATLCSRKS (in isoform 2).
{ECO:0000303|PubMed:15051137}.
/FTId=VSP_015606.
VAR_SEQ 441 530 Missing (in isoform 2).
{ECO:0000303|PubMed:15051137}.
/FTId=VSP_015607.
SEQUENCE 530 AA; 58704 MW; 6C97378D2135D5F1 CRC64;
MKPPSGLEEA QRRQASDIRV FANSCTMHGL GHIFGPGGLT LRRGLWATAV LLSLAAFLYQ
VAERVRYYGE FHHKTTLDER ESHQLTFPAV TLCNINPLRR SRLTPNDLHW AGTALLGLDP
AEHAAYLRAL GQPPAPPGFM PSPTFDMAQL YARAGHSLED MLLDCRYRGQ PCGPENFTVI
FTRMGQCYTF NSGAQGAELL TTPKGGAGNG LEIMLDVQQE EYLPIWKDME ETPFEVGIRV
QIHGQEEPPA IDQLGFGAAP GHQTFVSCQQ QQLSFLPPPW GDCNTASVDP DFDPEPSDPL
GSPSSSPPYS LIGCRLACES RYVARKCGCR MMHMPGNSPV CSPQQYKDCA SPALDAMLRK
DTCVCPNPCA TTRYAKELSM VRIPSRASAR YLARKYNRSE TYITENVLVL DIFFEALNYE
AVEQKAAYEV SELLGDIGGQ MGLFIGASLL TILEILDYLC EVFQDRVLGY FWNRRSSQRR
SGNTLLQEEL NGHRTHVPHL SLGPRPPTAP SAVTKTLAAS HRTCYLVTRL


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