GENTAUR Molecular Products.

 ASIC3_MOUSE             Reviewed;         530 AA.
 Q6X1Y6; Q7TQH4;
 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
 13-SEP-2005, sequence version 2.
 13-FEB-2019, entry version 125.
 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; ENSGT00940000162081; -.
 HOGENOM; HOG000247010; -.
 HOVERGEN; HBG004150; -.
 InParanoid; Q6X1Y6; -.
 KO; K04830; -.
 OMA; TPKGGMG; -.
 OrthoDB; 686369at2759; -.
 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.
 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; ISO:MGI.
 GO; GO:0005886; C:plasma membrane; ISO:MGI.
 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: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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