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Acid-sensing ion channel 2 (ASIC2) (Amiloride-sensitive brain sodium channel) (Amiloride-sensitive cation channel 1, neuronal) (Brain sodium channel 1) (BNC1) (BNaC1)

 ASIC2_MOUSE             Reviewed;         512 AA.
Q925H0; Q5SUU2; Q61203;
07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
25-OCT-2017, entry version 122.
RecName: Full=Acid-sensing ion channel 2;
Short=ASIC2;
AltName: Full=Amiloride-sensitive brain sodium channel;
AltName: Full=Amiloride-sensitive cation channel 1, neuronal;
AltName: Full=Brain sodium channel 1 {ECO:0000303|PubMed:11306621};
Short=BNC1;
Short=BNaC1 {ECO:0000303|PubMed:11306621};
Name=Asic2; Synonyms=Accn1, Bnac1;
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).
STRAIN=BALB/cJ; 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).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=BALB/cJ;
PubMed=11306621;
Garcia-Anoveros J., Samad T.A., Zuvela-Jelaska L., Woolf C.J.,
Corey D.P.;
"Transport and localization of the DEG/ENaC ion channel BNaC1alpha to
peripheral mechanosensory terminals of dorsal root ganglia neurons.";
J. Neurosci. 21:2678-2686(2001).
[3]
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).
[4]
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).
[5]
TISSUE SPECIFICITY, FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=14762118; DOI=10.1523/JNEUROSCI.4698-03.2004;
Ettaiche M., Guy N., Hofman P., Lazdunski M., Waldmann R.;
"Acid-sensing ion channel 2 is important for retinal function and
protects against light-induced retinal degeneration.";
J. Neurosci. 24:1005-1012(2004).
[6]
TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=15537887; DOI=10.1523/JNEUROSCI.3196-04.2004;
Peng B.-G., Ahmad S., Chen S., Chen P., Price M.P., Lin X.;
"Acid-sensing ion channel 2 contributes a major component to acid-
evoked excitatory responses in spiral ganglion neurons and plays a
role in noise susceptibility of mice.";
J. Neurosci. 24:10167-10175(2004).
[7]
SUBCELLULAR LOCATION, AND INDUCTION BY NEUROTROPHIN.
PubMed=15708491; DOI=10.1016/j.neuroscience.2004.11.030;
McIlwrath S.L., Hu J., Anirudhan G., Shin J.-B., Lewin G.R.;
"The sensory mechanotransduction ion channel ASIC2 (acid sensitive ion
channel 2) is regulated by neurotrophin availability.";
Neuroscience 131:499-511(2005).
[8]
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. Also permeable for Li(+) and K(+). Generates a biphasic
current with a fast inactivating and a slow sustained phase.
Heteromeric channel assembly seems to modulate.
{ECO:0000269|PubMed:14762118}.
-!- SUBUNIT: Homotrimer or heterotrimer with other ASIC proteins (By
similarity). Interacts with PRKCABP and ASIC3 (By similarity).
Interacts with STOM; this regulates channel activity
(PubMed:15471860, PubMed:22850675). Heterotrimer of Asic1a-Asic2a
interacts with the snake venom mambalgin-1, mambalgin-2 and
mambalgin-3 (By similarity). Heterotrimer of Asic1a-Asic2b
interacts with the snake venom mambalgin-1 and mambalgin-2 (By
similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q62962,
ECO:0000269|PubMed:15471860, ECO:0000269|PubMed:22850675}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15537887,
ECO:0000269|PubMed:15708491}; Multi-pass membrane protein
{ECO:0000269|PubMed:15537887, ECO:0000269|PubMed:15708491}.
Note=Localized at the plasma membrane, in the soma and punctated
peripheral processes of neurons.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=BNaC1-alpha {ECO:0000303|PubMed:11306621},
Asic2a;
IsoId=Q925H0-1; Sequence=Displayed;
Name=2; Synonyms=Mdeg2 {ECO:0000303|PubMed:9368048}, Asic2b;
IsoId=Q925H0-2; Sequence=VSP_015592, VSP_015593;
-!- TISSUE SPECIFICITY: Expressed by sensory neurons. Expressed by
nociceptive sensory neurons, spiral ganglion (SG) neurons and the
retina (at protein level). Isoform 1 and isoform 2 are expressed
in outer nuclear layer of retina (photoreceptors) and to a lower
extent in distal and proximal inner nuclear layer.
{ECO:0000269|PubMed:14762118, ECO:0000269|PubMed:15537887}.
-!- DEVELOPMENTAL STAGE: Expression changes dramatically during
cochlear development. Expression is detected at E11.5 in otocyst
and increases in the SG neurons after E18.5. Also detected in the
lumen side of all cells forming the vestibular cavity and at the
top of the macula of saccule and utricle. Before birth expressed
by epithelial cells facing the endolymphatic space. Post-natally
expressed by cells in the apical turn of the cochlea, while
expression on the lumen side of the membranous labyrinth
decreases. Expression shifts gradually toward the top of
supporting cells and the spiral limbus. Also expressed by
vestibular ganglion neurons. Restricted to the SG neurons in the
mature cochlea (at protein level). {ECO:0000269|PubMed:15537887}.
-!- INDUCTION: Expression in a subset of neurons may be regulated by
neurotrophins. {ECO:0000269|PubMed:15708491}.
-!- DISRUPTION PHENOTYPE: Mice display altered rod phototransduction
and neurotransmission, associated with increased light-induced
retina damages. {ECO:0000269|PubMed:14762118}.
-!- MISCELLANEOUS: Regulated by Zn(2+). Inhibited by anti-inflammatory
drugs like salicylic acid (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
1.A.6) family. ASIC2 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Y14634; CAA74978.1; -; mRNA.
EMBL; AF348465; AAK40101.1; -; mRNA.
EMBL; AL645842; CAI24499.1; -; Genomic_DNA.
EMBL; AL626807; CAI24499.1; JOINED; Genomic_DNA.
EMBL; AL663025; CAI24499.1; JOINED; Genomic_DNA.
EMBL; AL645842; CAI24500.1; -; Genomic_DNA.
EMBL; AL645626; CAI24500.1; JOINED; Genomic_DNA.
EMBL; AL663025; CAI24500.1; JOINED; Genomic_DNA.
EMBL; AL626807; CAI25306.1; -; Genomic_DNA.
EMBL; AL645842; CAI25306.1; JOINED; Genomic_DNA.
EMBL; AL663025; CAI25306.1; JOINED; Genomic_DNA.
EMBL; AL645626; CAI25540.1; -; Genomic_DNA.
EMBL; AL645842; CAI25540.1; JOINED; Genomic_DNA.
EMBL; AL663025; CAI25540.1; JOINED; Genomic_DNA.
EMBL; AL663025; CAI25600.1; -; Genomic_DNA.
EMBL; AL626807; CAI25600.1; JOINED; Genomic_DNA.
EMBL; AL645842; CAI25600.1; JOINED; Genomic_DNA.
EMBL; AL663025; CAI25602.1; -; Genomic_DNA.
EMBL; AL645626; CAI25602.1; JOINED; Genomic_DNA.
EMBL; AL645842; CAI25602.1; JOINED; Genomic_DNA.
CCDS; CCDS25137.1; -. [Q925H0-2]
CCDS; CCDS36243.1; -. [Q925H0-1]
RefSeq; NP_001029185.1; NM_001034013.2. [Q925H0-1]
RefSeq; NP_031410.1; NM_007384.3. [Q925H0-2]
UniGene; Mm.234998; -.
UniGene; Mm.259072; -.
UniGene; Mm.330264; -.
UniGene; Mm.366419; -.
UniGene; Mm.392269; -.
UniGene; Mm.473675; -.
ProteinModelPortal; Q925H0; -.
SMR; Q925H0; -.
BioGrid; 197917; 2.
MINT; MINT-223604; -.
ChEMBL; CHEMBL3232695; -.
TCDB; 1.A.6.1.8; the epithelial na(+) channel (enac) family.
PhosphoSitePlus; Q925H0; -.
PRIDE; Q925H0; -.
Ensembl; ENSMUST00000021045; ENSMUSP00000021045; ENSMUSG00000020704. [Q925H0-2]
Ensembl; ENSMUST00000066197; ENSMUSP00000067095; ENSMUSG00000020704. [Q925H0-1]
GeneID; 11418; -.
KEGG; mmu:11418; -.
UCSC; uc007kmm.2; mouse. [Q925H0-1]
CTD; 40; -.
MGI; MGI:1100867; Asic2.
GeneTree; ENSGT00760000119120; -.
HOGENOM; HOG000247010; -.
HOVERGEN; HBG004150; -.
InParanoid; Q925H0; -.
KO; K04828; -.
OMA; HPNTRYE; -.
TreeFam; TF330663; -.
Reactome; R-MMU-2672351; Stimuli-sensing channels.
PRO; PR:Q925H0; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020704; -.
ExpressionAtlas; Q925H0; baseline and differential.
Genevisible; Q925H0; MM.
GO; GO:0043197; C:dendritic spine; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; IDA:MGI.
GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
GO; GO:0043005; C:neuron projection; IDA:MGI.
GO; GO:0043025; C:neuronal cell body; IDA:MGI.
GO; GO:0045202; C:synapse; IDA:MGI.
GO; GO:0005261; F:cation channel activity; IDA:MGI.
GO; GO:0005216; F:ion channel activity; IDA:MGI.
GO; GO:0022839; F:ion gated channel activity; IDA:MGI.
GO; GO:0015280; F:ligand-gated sodium channel activity; IDA:MGI.
GO; GO:0006812; P:cation transport; IDA:MGI.
GO; GO:0050974; P:detection of mechanical stimulus involved in sensory perception; IMP:MGI.
GO; GO:0034220; P:ion transmembrane transport; IDA:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
GO; GO:0007602; P:phototransduction; IMP:MGI.
GO; GO:0051965; P:positive regulation of synapse assembly; IMP:MGI.
GO; GO:0035418; P:protein localization to synapse; IMP:MGI.
GO; GO:0030193; P:regulation of blood coagulation; ISO:MGI.
GO; GO:0010468; P:regulation of gene expression; ISO:MGI.
GO; GO:0034765; P:regulation of ion transmembrane transport; IMP:MGI.
GO; GO:0042391; P:regulation of membrane potential; IMP:MGI.
GO; GO:0003026; P:regulation of systemic arterial blood pressure by aortic arch baroreceptor feedback; IMP:MGI.
GO; GO:0019229; P:regulation of vasoconstriction; IMP:MGI.
GO; GO:0010447; P:response to acidic pH; IDA:MGI.
GO; GO:0009612; P:response to mechanical stimulus; IMP:MGI.
GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
GO; GO:0050915; P:sensory perception of sour taste; ISO:MGI.
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;
Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Ion channel; Ion transport; Membrane;
Phosphoprotein; Reference proteome; Sodium; Sodium channel;
Sodium transport; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 512 Acid-sensing ion channel 2.
/FTId=PRO_0000181291.
TOPO_DOM 1 37 Cytoplasmic. {ECO:0000250}.
TRANSMEM 38 58 Helical. {ECO:0000255}.
TOPO_DOM 59 427 Extracellular. {ECO:0000250}.
TRANSMEM 428 448 Helical. {ECO:0000255}.
TOPO_DOM 449 512 Cytoplasmic. {ECO:0000250}.
MOD_RES 8 8 Phosphoserine.
{ECO:0000250|UniProtKB:Q62962}.
MOD_RES 11 11 Phosphoserine.
{ECO:0000250|UniProtKB:Q62962}.
CARBOHYD 365 365 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
CARBOHYD 392 392 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
DISULFID 92 193 {ECO:0000250}.
DISULFID 171 178 {ECO:0000250}.
DISULFID 289 364 {ECO:0000250}.
DISULFID 307 360 {ECO:0000250}.
DISULFID 311 358 {ECO:0000250}.
DISULFID 320 342 {ECO:0000250}.
DISULFID 322 334 {ECO:0000250}.
VAR_SEQ 1 184 Missing (in isoform 2).
{ECO:0000303|PubMed:9368048}.
/FTId=VSP_015592.
VAR_SEQ 185 185 T -> MSRSGGARLPATALSGPGRFRMAREQPAPAAVAAAR
QPGGDRSGDRELQGPGVARRGRPSLSRTKLHGLRHMCAGRT
AAGGSFQRRALWVLAFCTSLGLLLSWSSNRLLYWLSFPSHT
RVHREWSRQLPFPAVTVCNNNPLRFPRLSKGDLYYAGHWLG
LLLPNRTARPLVSELLRGDEPRRQWFRKLADFRLFLPPRHF
EGISAAFMDRLGHQLEDMLLSCKYRGELCGPHNFSS (in
isoform 2). {ECO:0000303|PubMed:9368048}.
/FTId=VSP_015593.
SEQUENCE 512 AA; 57739 MW; 7D81A77C3B347B04 CRC64;
MDLKESPSEG SLQPSSIQIF ANTSTLHGIR HIFVYGPLTI RRVLWAVAFV GSLGLLLVES
SERVSYYFSY QHVTKVDEVV AQSLVFPAVT LCNLNGFRFS RLTTNDLYHA GELLALLDVN
LQIPDPHLAD PTVLEALRQK ANFKHYKPKQ FSMLEFLHRV GHDLKDMMLY CKFKGQECGH
QDFTTVFTKY GKCYMFNSGE DGKPLLTTVK GGTGNGLEIM LDIQQDEYLP IWGETEETTF
EAGVKVQIHS QSEPPFIQEL GFGVAPGFQT FVATQEQRLT YLPPPWGECR SSEMGLDFFP
VYSITACRID CETRYIVENC NCRMVHMPGD APFCTPEQHK ECAEPALGLL AEKDSNYCLC
RTPCNLTRYN KELSMVKIPS KTSAKYLEKK FNKSEKYISE NILVLDIFFE ALNYETIEQK
KAYEVAALLG DIGGQMGLFI GASILTILEL FDYIYELIKE KLLDLLGKEE EEGSHDENMS
TCDTMPNHSE TISHTVNVPL QTALGTLEEI AC


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