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Acid-sensing ion channel 1 (ASIC1) (Acid-sensing ion channel) (Amiloride-sensitive cation channel 2, neuronal) (Brain sodium channel 2) (BNaC2)

 ASIC1_MOUSE             Reviewed;         526 AA.
Q6NXK8; Q50K97;
13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
05-DEC-2018, entry version 119.
RecName: Full=Acid-sensing ion channel 1;
Short=ASIC1;
AltName: Full=Acid-sensing ion channel;
AltName: Full=Amiloride-sensitive cation channel 2, neuronal;
AltName: Full=Brain sodium channel 2;
Short=BNaC2;
Name=Asic1; Synonyms=Accn2, Asic, Bnac2;
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).
Ugawa S., Shimada S.;
"Mus musculus mRNA for ASIC1b.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND FUNCTION.
PubMed=11988176; DOI=10.1016/S0896-6273(02)00661-X;
Wemmie J.A., Chen J., Askwith C.C., Hruska-Hageman A.M., Price M.P.,
Nolan B.C., Yoder P.G., Lamani E., Hoshi T., Freeman J.H. Jr.,
Welsh M.J.;
"The acid-activated ion channel ASIC contributes to synaptic
plasticity, learning, and memory.";
Neuron 34:463-477(2002).
[4]
TISSUE SPECIFICITY, AND FUNCTION.
PubMed=12843249;
Wemmie J.A., Askwith C.C., Lamani E., Cassell M.D., Freeman J.H. Jr.,
Welsh M.J.;
"Acid-sensing ion channel 1 is localized in brain regions with high
synaptic density and contributes to fear conditioning.";
J. Neurosci. 23:5496-5502(2003).
[5]
FUNCTION.
PubMed=15369669; DOI=10.1016/j.cell.2004.08.026;
Xiong Z.-G., Zhu X.-M., Chu X.-P., Minami M., Hey J., Wei W.-L.,
MacDonald J.F., Wemmie J.A., Price M.P., Welsh M.J., Simon R.P.;
"Neuroprotection in ischemia: blocking calcium-permeable acid-sensing
ion channels.";
Cell 118:687-698(2004).
[6]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=15578512; DOI=10.1053/j.gastro.2004.08.061;
Page A.J., Brierley S.M., Martin C.M., Martinez-Salgado C.,
Wemmie J.A., Brennan T.J., Symonds E., Omari T., Lewin G.R.,
Welsh M.J., Blackshaw L.A.;
"The ion channel ASIC1 contributes to visceral but not cutaneous
mechanoreceptor function.";
Gastroenterology 127:1739-1747(2004).
[7]
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).
[8]
FUNCTION.
PubMed=17060608; DOI=10.1073/pnas.0608018103;
Zha X.-M., Wemmie J.A., Green S.H., Welsh M.J.;
"Acid-sensing ion channel 1a is a postsynaptic proton receptor that
affects the density of dendritic spines.";
Proc. Natl. Acad. Sci. U.S.A. 103:16556-16561(2006).
[9]
FUNCTION IN CONTROL OF FEAR, AND DISRUPTION PHENOTYPE.
PubMed=17662962; DOI=10.1016/j.biopsych.2007.05.008;
Coryell M.W., Ziemann A.E., Westmoreland P.J., Haenfler J.M.,
Kurjakovic Z., Zha X.-M., Price M., Schnizler M.K., Wemmie J.A.;
"Targeting ASIC1a reduces innate fear and alters neuronal activity in
the fear circuit.";
Biol. Psychiatry 62:1140-1148(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-497, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Proton-gated sodium channel; it is activated by a drop
of the extracellular pH and then becomes rapidly desensitized.
Generates a biphasic current with a fast inactivating and a slow
sustained phase. Has high selectivity for sodium ions and can also
transport lithium ions with high efficiency. Can also transport
potassium ions, but with lower efficiency. It is nearly
impermeable to the larger rubidium and cesium ions. Mediates
glutamate-independent Ca(2+) entry into neurons upon acidosis.
This Ca(2+) overloading is toxic for cortical neurons and may be
in part responsible for ischemic brain injury. Heteromeric channel
assembly seems to modulate channel properties. Functions as a
postsynaptic proton receptor that influences intracellular Ca(2+)
concentration and calmodulin-dependent protein kinase II
phosphorylation and thereby the density of dendritic spines.
Modulates activity in the circuits underlying innate fear.
{ECO:0000269|PubMed:11988176, ECO:0000269|PubMed:12843249,
ECO:0000269|PubMed:15369669, ECO:0000269|PubMed:15578512,
ECO:0000269|PubMed:17060608, ECO:0000269|PubMed:17662962}.
-!- ACTIVITY REGULATION: Inhibited by the diuretic amiloride.
-!- SUBUNIT: Homotrimer or heterotrimer with other ASIC proteins (By
similarity). Interacts with PRKCABP and ASIC2 (By similarity).
Interacts with STOM (PubMed:15471860). {ECO:0000250,
ECO:0000269|PubMed:15471860}.
-!- INTERACTION:
Q12791:KCNMA1 (xeno); NbExp=2; IntAct=EBI-15686410, EBI-1220676;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass
membrane protein {ECO:0000250}. Note=Localizes in synaptosomes at
dendritic synapses of neurons. Colocalizes with DLG4.
{ECO:0000269|PubMed:11988176}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Asic1a, Asic alpha;
IsoId=Q6NXK8-1; Sequence=Displayed;
Name=2; Synonyms=Asic1b, Asic beta;
IsoId=Q6NXK8-2; Sequence=VSP_015614, VSP_015615;
-!- TISSUE SPECIFICITY: Expressed in brain areas receiving strong
excitatory corticofugal input. In hippocampus, expressed in the
hilus of the dentate gyrus. In the cerebral cortex expressed in
anterior and posterior cingulate cortex, sensory and motor
cortices. In the sensory cortex strongest expression is detected
in the whisker barrel field. In sensorimotor and cingulate cortex
expression is elevated in layer III. Also expressed in basal
ganglia, striatum, ventral pallidum, olfactory tubercle, and
nucleus accumbens. Weakly expressed in thalamus with the exception
of the habenula and the medial septal nuclei. In olfactory bulb,
preferentially expressed in the glomerular layer, within
glomeruli. Expressed in cerebellum in the molecular and granule
cell layers. Strongly expressed in amygdala complex, particularly
in the lateral and basolateral nuclei. Isoform 1 is more abundant
in brain compared to isoform 2 (at protein level). Expressed in
the nodose ganglion and dorsal root ganglion. Expressed in
dendritic spine cells. {ECO:0000269|PubMed:11988176,
ECO:0000269|PubMed:12843249, ECO:0000269|PubMed:15578512}.
-!- DOMAIN: Channel opening involves a conformation change that
affects primarily the extracellular domain and the second
transmembrane helix and its orientation in the membrane. In the
open state, the second transmembrane helix is nearly perpendicular
to the plane of the membrane; in the desensitized state it is
strongly tilted. Besides, the second transmembrane domain is
discontinuously helical in the open state. The GAS motif of the
selectivity filter is in an extended conformation, giving rise to
a distinct kink in the polypeptide chain. A domain swap between
subunits gives rise to a full-length transmembrane helix (By
similarity). {ECO:0000250}.
-!- PTM: Phosphorylation by PKA regulates interaction with PRKCABP and
subcellular location. Phosphorylation by PKC may regulate the
channel (By similarity). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice display reduced spatial learning and
memory capability, associated with absence of proton-gated
currents in hippocampal neurons and impairment of hippocampal long
term potentiation (LTP). They also show an increased
mechanosensitivity of colonic and gastroesophageal
mechanoreceptors and prolonged gastric emptying and an altered
fear conditioning. {ECO:0000269|PubMed:17662962}.
-!- MISCELLANEOUS: Potentiated by Ca(2+), Mg(2+), Ba(2+), multivalent
cations and potentiated by FMRFamide-related neuropeptides. PH
dependence may be regulated by serine proteases. 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. ASIC1 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AB208022; BAD97849.1; -; mRNA.
EMBL; BC067025; AAH67025.1; -; mRNA.
CCDS; CCDS27826.1; -. [Q6NXK8-1]
RefSeq; NP_001276720.1; NM_001289791.1. [Q6NXK8-2]
RefSeq; NP_033727.1; NM_009597.1. [Q6NXK8-1]
UniGene; Mm.440107; -.
ProteinModelPortal; Q6NXK8; -.
SMR; Q6NXK8; -.
BioGrid; 197918; 2.
DIP; DIP-29728N; -.
IntAct; Q6NXK8; 2.
STRING; 10090.ENSMUSP00000023758; -.
ChEMBL; CHEMBL3232694; -.
iPTMnet; Q6NXK8; -.
PhosphoSitePlus; Q6NXK8; -.
PaxDb; Q6NXK8; -.
PeptideAtlas; Q6NXK8; -.
PRIDE; Q6NXK8; -.
Ensembl; ENSMUST00000023758; ENSMUSP00000023758; ENSMUSG00000023017. [Q6NXK8-1]
Ensembl; ENSMUST00000228185; ENSMUSP00000154379; ENSMUSG00000023017. [Q6NXK8-2]
GeneID; 11419; -.
KEGG; mmu:11419; -.
UCSC; uc007xqa.2; mouse. [Q6NXK8-1]
UCSC; uc011zzg.2; mouse. [Q6NXK8-2]
CTD; 41; -.
MGI; MGI:1194915; Asic1.
eggNOG; KOG4294; Eukaryota.
eggNOG; ENOG410ZNFK; LUCA.
GeneTree; ENSGT00940000158414; -.
HOGENOM; HOG000247010; -.
HOVERGEN; HBG004150; -.
InParanoid; Q6NXK8; -.
KO; K04829; -.
OMA; CSDKKHK; -.
OrthoDB; EOG091G053J; -.
PhylomeDB; Q6NXK8; -.
TreeFam; TF330663; -.
Reactome; R-MMU-2672351; Stimuli-sensing channels.
ChiTaRS; Asic1; mouse.
PRO; PR:Q6NXK8; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000023017; Expressed in 124 organ(s), highest expression level in brain.
CleanEx; MM_ACCN2; -.
Genevisible; Q6NXK8; MM.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0043198; C:dendritic shaft; ISO:MGI.
GO; GO:0043197; C:dendritic spine; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0045202; C:synapse; IDA:MGI.
GO; GO:0044736; F:acid-sensing ion channel activity; IDA:MGI.
GO; GO:0005261; F:cation channel activity; IDA:MGI.
GO; GO:0005216; F:ion channel activity; ISO:MGI.
GO; GO:0022839; F:ion gated channel activity; IDA:MGI.
GO; GO:0015077; F:monovalent inorganic cation transmembrane transporter activity; ISO:MGI.
GO; GO:0008306; P:associative learning; IMP:MGI.
GO; GO:0001662; P:behavioral fear response; IMP:MGI.
GO; GO:0070588; P:calcium ion transmembrane transport; IMP:MGI.
GO; GO:0006812; P:cation transport; IDA:MGI.
GO; GO:0071467; P:cellular response to pH; ISS:UniProtKB.
GO; GO:0034220; P:ion transmembrane transport; IDA:MGI.
GO; GO:0007613; P:memory; IMP:MGI.
GO; GO:0015672; P:monovalent inorganic cation transport; ISO:MGI.
GO; GO:0046929; P:negative regulation of neurotransmitter secretion; IMP:MGI.
GO; GO:0070207; P:protein homotrimerization; ISS:UniProtKB.
GO; GO:0042391; P:regulation of membrane potential; IMP:MGI.
GO; GO:0010447; P:response to acidic pH; IDA:MGI.
GO; GO:0001975; P:response to amphetamine; IMP:MGI.
GO; GO:0050915; P:sensory perception of sour taste; ISO:MGI.
GO; GO:0035725; P:sodium ion transmembrane transport; ISS:UniProtKB.
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; Calcium; Calcium transport; 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 1 526 Acid-sensing ion channel 1.
/FTId=PRO_0000181295.
TOPO_DOM 1 45 Cytoplasmic. {ECO:0000250}.
TRANSMEM 46 69 Helical. {ECO:0000250}.
TOPO_DOM 70 425 Extracellular. {ECO:0000250}.
TRANSMEM 426 452 Discontinuously helical. {ECO:0000250}.
TOPO_DOM 453 526 Cytoplasmic. {ECO:0000250}.
MOTIF 442 444 Selectivity filter. {ECO:0000305}.
SITE 71 71 Important for channel gating.
{ECO:0000250}.
SITE 79 79 Important for channel desensitizing.
{ECO:0000250}.
SITE 287 287 Important for channel gating.
{ECO:0000250}.
MOD_RES 477 477 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:P78348}.
MOD_RES 497 497 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CARBOHYD 366 366 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 393 393 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 93 194 {ECO:0000250|UniProtKB:Q1XA76}.
DISULFID 172 179 {ECO:0000250|UniProtKB:Q1XA76}.
DISULFID 290 365 {ECO:0000250|UniProtKB:Q1XA76}.
DISULFID 308 361 {ECO:0000250|UniProtKB:Q1XA76}.
DISULFID 312 359 {ECO:0000250|UniProtKB:Q1XA76}.
DISULFID 321 343 {ECO:0000250|UniProtKB:Q1XA76}.
DISULFID 323 335 {ECO:0000250|UniProtKB:Q1XA76}.
VAR_SEQ 1 184 Missing (in isoform 2).
{ECO:0000303|Ref.1}.
/FTId=VSP_015614.
VAR_SEQ 185 185 K -> MPIQIFCSVSFSSGEEAPGSMGDIWGPHHHHRQQQD
SSESEEEEEKEKESGMELDEGDSPRDLVAFANSCTLHGASH
VFVEGGPGPRQALWAVAFVIALGAFLCQVGDRVAYYLSYPH
VTLLDEVATTELVFPAVTFCNTNAVRLSQLSYPDLLYLAPM
LGLDESDDPGVPLAPPGPEAFSGEPFNLHRFYNRSCHRLED
MLLYCSYCGGPCGPHNFS (in isoform 2).
{ECO:0000303|Ref.1}.
/FTId=VSP_015615.
SEQUENCE 526 AA; 59668 MW; 5462B3FEB5532726 CRC64;
MELKTEEEEV GGVQPVSIQA FASSSTLHGL AHIFSYERLS LKRALWALCF LGSLAVLLCV
CTERVQYYFC YHHVTKLDEV AASQLTFPAV TLCNLNEFRF SQVSKNDLYH AGELLALLNN
RYEIPDTQMA DEKQLEILQD KANFRSFKPK PFNMREFYDR AGHDIRDMLL SCHFRGEACS
AEDFKVVFTR YGKCYTFNSG QDGRPRLKTM KGGTGNGLEI MLDIQQDEYL PVWGETDETS
FEAGIKVQIH SQDEPPFIDQ LGFGVAPGFQ TFVSCQEQRL IYLPSPWGTC NAVTMDSDFF
DSYSITACRI DCETRYLVEN CNCRMVHMPG DAPYCTPEQY KECADPALDF LVEKDQEYCV
CEMPCNLTRY GKELSMVKIP SKASAKYLAK KFNKSEQYIG ENILVLDIFF EVLNYETIEQ
KKAYEIAGLL GDIGGQMGLF IGASILTVLE LFDYAYEVIK HRLCRRGKCQ KEAKRNSADK
GVALSLDDVK RHNPCESLRG HPAGMTYAAN ILPHHPARGT FEDFTC


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