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

 ASIC2_RAT               Reviewed;         512 AA.
Q62962; O55163;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
22-NOV-2017, entry version 137.
RecName: Full=Acid-sensing ion channel 2;
Short=ASIC2;
AltName: Full=Amiloride-sensitive brain sodium channel;
AltName: Full=Amiloride-sensitive brain sodium channel 2;
AltName: Full=Amiloride-sensitive cation channel 1, neuronal;
AltName: Full=Amiloride-sensitive cation channel neuronal 1;
AltName: Full=Brain sodium channel 1;
Short=BNC1;
Short=BNaC1;
AltName: Full=Mammalian degenerin homolog {ECO:0000303|PubMed:8631835};
Short=MDEG {ECO:0000303|PubMed:8631835};
Name=Asic2; Synonyms=Accn1, Bnac1, Mdeg;
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] (ISOFORM 1), TISSUE SPECIFICITY,
MUTAGENESIS OF GLY-430 AND SER-443, AND FUNCTION.
TISSUE=Brain;
PubMed=8631835; DOI=10.1074/jbc.271.18.10433;
Waldmann R., Champigny G., Voilley N., Lauritzen I., Lazdunski M.;
"The mammalian degenerin MDEG, an amiloride-sensitive cation channel
activated by mutations causing neurodegeneration in Caenorhabditis
elegans.";
J. Biol. Chem. 271:10433-10436(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY,
OLIGOMERIZATION, AND INTERACTION WITH ASIC3.
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, INTERACTION WITH ASIC2, AND FUNCTION.
PubMed=9360943; DOI=10.1074/jbc.272.46.28819;
Bassilana F., Champigny G., Waldmann R., de Weille J.R., Heurteaux C.,
Lazdunski M.;
"The acid-sensitive ionic channel subunit ASIC and the mammalian
degenerin MDEG form a heteromultimeric H+-gated Na+ channel with novel
properties.";
J. Biol. Chem. 272:28819-28822(1997).
[4]
MUTAGENESIS OF HIS-72; HIS-109; HIS-127; HIS-145; HIS-158; HIS-162;
HIS-180; HIS-249; HIS-326; HIS-339 AND GLY-430, AND REGULATION BY
PROTONS AND ZINC.
PubMed=11457851; DOI=10.1074/jbc.M105208200;
Baron A., Schaefer L., Lingueglia E., Champigny G., Lazdunski M.;
"Zn2+ and H+ are coactivators of acid-sensing ion channels.";
J. Biol. Chem. 276:35361-35367(2001).
[5]
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).
[6]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
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).
[7]
INTERACTION WITH ASIC3.
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).
[8]
GLYCOSYLATION AT ASN-365 AND ASN-392, MUTAGENESIS OF LYS-4; ASN-22;
PRO-37; ARG-63; TYR-67; HIS-72; ALA-81; ASN-365; ASN-392; TYR-414;
423-TYR--VAL-425; 453-TYR--TYR-455; ASN-478 AND ASN-487, AND TOPOLOGY.
PubMed=15504740; DOI=10.1074/jbc.M411849200;
Saugstad J.A., Roberts J.A., Dong J., Zeitouni S., Evans R.J.;
"Analysis of the membrane topology of the acid-sensing ion channel
2a.";
J. Biol. Chem. 279:55514-55519(2004).
[9]
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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND SER-11, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[11]
INTERACTION WITH SNAKE VENOM MAMBALGIN-1 AND MAMBALGIN-2, AND SUBUNIT.
TISSUE=Venom, and Venom gland;
PubMed=23034652; DOI=10.1038/nature11494;
Diochot S., Baron A., Salinas M., Douguet D., Scarzello S.,
Dabert-Gay A.-S., Debayle D., Friend V., Alloui A., Lazdunski M.,
Lingueglia E.;
"Black mamba venom peptides target acid-sensing ion channels to
abolish pain.";
Nature 490:552-555(2012).
[12]
INTERACTION WITH MAMBALGIN-1; MAMBALGIN-2 AND MAMBALGIN-3, SUBUNIT,
AND REVIEW.
PubMed=23624383; DOI=10.1016/j.toxicon.2013.04.008;
Baron A., Diochot S., Salinas M., Deval E., Noel J., Lingueglia E.;
"Venom toxins in the exploration of molecular, physiological and
pathophysiological functions of acid-sensing ion channels.";
Toxicon 75:187-204(2013).
-!- 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(+). Activation by an
extracellular pH drop is followed by a rapid pH-independent
inactivation. Heteromeric channel assembly seems to modulate
channel properties. {ECO:0000269|PubMed:22850675,
ECO:0000269|PubMed:8631835, ECO:0000269|PubMed:9360943}.
-!- SUBUNIT: Homotrimer or heterotrimer with other ASIC proteins (By
similarity). Interacts with PRKCABP (By similarity). Interacts
with STOM; this regulates channel activity. Interacts with ASIC1.
Isoform 2 interacts with ASIC3. Heterotrimer of Asic1a-Asic2a
interacts with the snake venom mambalgin-1, mambalgin-2 and
mambalgin-3 (PubMed:23034652, PubMed:23624383). Heterotrimer of
Asic1a-Asic2b interacts with the snake venom mambalgin-1 and
mambalgin-2 (PubMed:23034652). {ECO:0000250,
ECO:0000269|PubMed:14976185, ECO:0000269|PubMed:22850675,
ECO:0000269|PubMed:9360943, ECO:0000269|PubMed:9368048}.
-!- INTERACTION:
D4A100:Stoml3; NbExp=2; IntAct=EBI-15615798, EBI-15615743;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11842212,
ECO:0000269|PubMed:22850675}; Multi-pass membrane protein
{ECO:0000269|PubMed:11842212, ECO:0000269|PubMed:22850675}.
Note=Localized at the plasma membrane of neurons, in the soma and
punctated peripheral processes.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Mdeg1 {ECO:0000303|PubMed:9368048}, Asic2a;
IsoId=Q62962-1; Sequence=Displayed;
Name=2; Synonyms=Mdeg2 {ECO:0000303|PubMed:9368048}, Asic2b;
IsoId=Q62962-2; Sequence=VSP_015594, VSP_015595;
Note=Seems to be inactive as monomer or in a monomeric assembly
and is not activated by mutagenesis of Gly-430. Mutagenesis of
Ser-60 into Gly reduces activation by PKC through PRKCABP/PICK-1
of a ASIC3/ACCN3-ASIC2/ASIC2b channel.;
-!- TISSUE SPECIFICITY: Expressed in sciatic nerve and dorsal root
ganglion (DRG) (at protein level). Both isoforms display the same
expression pattern except in DRG where isoform 2 is more
abundantly expressed. Widely distributed throughout the brain.
Highly expressed in the main olfactory bulb, neo- and allo-
cortical regions, hippocampal formation, habenula, basolateral
amygdaloid nuclei, and cerebellum. In the olfactory system,
expressed in the glomerular cell layer, the internal granular
layer, and the mitral and internal plexiform cell layers. Within
the glomerular layer, restricted to the periglomerular cells. In
the neocortex, strongly expressed in the large pyramidal neurons
in all cortical layers as well as in the oligo-, astro-, or micro-
glia cells. In the hippocampal formation, expressed in dentate
granule cells and hilar neurons, as well as in pyramidal cells of
CA1-CA3 subfields. Expressed in stratum oriens and radiatum of all
subfields. Within the thalamus, expressed moderately in the medial
and lateral habenula. In the cerebellar cortex expressed in
Purkinje cells and granule cells. Expressed at low levels in
choroid plexus. {ECO:0000269|PubMed:11842212,
ECO:0000269|PubMed:8631835, ECO:0000269|PubMed:9360943,
ECO:0000269|PubMed:9368048}.
-!- DEVELOPMENTAL STAGE: Appears just before birth, reaches maximum
levels after birth, then declines slightly until adulthood.
-!- INDUCTION: Up-regulation upon tissues inflammation is abolished by
anti-inflammatory drugs. {ECO:0000269|PubMed:11588175}.
-!- MISCELLANEOUS: Regulated by Zn(2+). Inhibited by anti-inflammatory
drugs like salicylic acid.
-!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
1.A.6) family. ASIC2 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U53211; AAC52588.1; -; mRNA.
EMBL; Y14635; CAA74979.1; -; mRNA.
RefSeq; NP_001029186.1; NM_001034014.1. [Q62962-1]
RefSeq; NP_037024.2; NM_012892.2. [Q62962-2]
UniGene; Rn.37523; -.
ProteinModelPortal; Q62962; -.
SMR; Q62962; -.
DIP; DIP-41193N; -.
IntAct; Q62962; 1.
MINT; MINT-223656; -.
ChEMBL; CHEMBL3562171; -.
TCDB; 1.A.6.1.2; the epithelial na(+) channel (enac) family.
iPTMnet; Q62962; -.
PhosphoSitePlus; Q62962; -.
PRIDE; Q62962; -.
GeneID; 25364; -.
KEGG; rno:25364; -.
CTD; 40; -.
RGD; 2017; Asic2.
HOGENOM; HOG000247010; -.
HOVERGEN; HBG004150; -.
InParanoid; Q62962; -.
KO; K04828; -.
PhylomeDB; Q62962; -.
TreeFam; TF330663; -.
PRO; PR:Q62962; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0043197; C:dendritic spine; ISO:RGD.
GO; GO:0016021; C:integral component of membrane; ISO:RGD.
GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
GO; GO:0043005; C:neuron projection; ISO:RGD.
GO; GO:0043025; C:neuronal cell body; ISO:RGD.
GO; GO:0045202; C:synapse; ISO:RGD.
GO; GO:0005261; F:cation channel activity; ISO:RGD.
GO; GO:0005216; F:ion channel activity; IDA:RGD.
GO; GO:0022839; F:ion gated channel activity; ISO:RGD.
GO; GO:0015280; F:ligand-gated sodium channel activity; ISO:RGD.
GO; GO:0005248; F:voltage-gated sodium channel activity; IDA:RGD.
GO; GO:0006812; P:cation transport; ISO:RGD.
GO; GO:0071468; P:cellular response to acidic pH; IDA:RGD.
GO; GO:0035690; P:cellular response to drug; IDA:RGD.
GO; GO:0050974; P:detection of mechanical stimulus involved in sensory perception; ISO:RGD.
GO; GO:0034220; P:ion transmembrane transport; ISO:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
GO; GO:0007602; P:phototransduction; ISO:RGD.
GO; GO:2001259; P:positive regulation of cation channel activity; IDA:RGD.
GO; GO:0051965; P:positive regulation of synapse assembly; ISO:RGD.
GO; GO:0035418; P:protein localization to synapse; ISO:RGD.
GO; GO:0030193; P:regulation of blood coagulation; ISO:RGD.
GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
GO; GO:0034765; P:regulation of ion transmembrane transport; ISO:RGD.
GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
GO; GO:0003026; P:regulation of systemic arterial blood pressure by aortic arch baroreceptor feedback; ISO:RGD.
GO; GO:0019229; P:regulation of vasoconstriction; ISO:RGD.
GO; GO:0010447; P:response to acidic pH; ISO:RGD.
GO; GO:0009612; P:response to mechanical stimulus; ISO:RGD.
GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
GO; GO:0050915; P:sensory perception of sour taste; ISO:RGD.
GO; GO:0006814; P:sodium ion transport; IDA:RGD.
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_0000181292.
TOPO_DOM 1 37 Cytoplasmic.
{ECO:0000269|PubMed:15504740}.
TRANSMEM 38 58 Helical. {ECO:0000255}.
TOPO_DOM 59 427 Extracellular.
{ECO:0000269|PubMed:15504740}.
TRANSMEM 428 448 Helical. {ECO:0000255}.
TOPO_DOM 449 512 Cytoplasmic.
{ECO:0000269|PubMed:15504740}.
SITE 478 478 Not glycosylated.
SITE 487 487 Not glycosylated.
MOD_RES 8 8 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 11 11 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CARBOHYD 365 365 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15504740}.
CARBOHYD 392 392 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15504740}.
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_015594.
VAR_SEQ 185 185 T -> MSRSGGARLPATALSGPGRFRMAREQPAPVAVAAAR
QPGGDRSGDPALQGPGVARRGRPSLSRTKLHGLRHMCAGRT
AAGGSFQRRALWVLAFCTSLGLLLSWSSNRLLYWLSFPSHT
RVHREWSRQLPFPAVTVCNNNPLRFPRLSKGDLYYAGHWLG
LLLPNRTARPLVSELLRGDEPRRQWFRKLADFRLFLPPRHF
EGISAAFMDRLGHQLEDMLLSCKYRGELCGPHNFSS (in
isoform 2). {ECO:0000303|PubMed:9368048}.
/FTId=VSP_015595.
MUTAGEN 4 4 K->N: No effect on N-glycosylation.
{ECO:0000269|PubMed:15504740}.
MUTAGEN 22 22 N->S: No effect on N-glycosylation.
{ECO:0000269|PubMed:15504740}.
MUTAGEN 37 37 P->N: No effect on N-glycosylation.
{ECO:0000269|PubMed:15504740}.
MUTAGEN 63 63 R->N: No effect on N-glycosylation.
{ECO:0000269|PubMed:15504740}.
MUTAGEN 67 67 Y->N: No effect on N-glycosylation.
{ECO:0000269|PubMed:15504740}.
MUTAGEN 72 72 H->A: Inactive. Active at lower pH; when
associated with V-430.
{ECO:0000269|PubMed:11457851,
ECO:0000269|PubMed:15504740}.
MUTAGEN 72 72 H->N: Increases N-glycosylation.
{ECO:0000269|PubMed:11457851,
ECO:0000269|PubMed:15504740}.
MUTAGEN 81 81 A->N: Increases N-glycosylation.
{ECO:0000269|PubMed:15504740}.
MUTAGEN 109 109 H->A: No effect on pH dependence and
function. {ECO:0000269|PubMed:11457851}.
MUTAGEN 127 127 H->A: No effect on pH dependence and
function. {ECO:0000269|PubMed:11457851}.
MUTAGEN 145 145 H->A: No effect on pH dependence and
function. {ECO:0000269|PubMed:11457851}.
MUTAGEN 158 158 H->A: No effect on pH dependence and
function. {ECO:0000269|PubMed:11457851}.
MUTAGEN 162 162 H->A: Loss of potentiation by Zn(2+).
{ECO:0000269|PubMed:11457851}.
MUTAGEN 180 180 H->A: No effect on pH dependence and
function. {ECO:0000269|PubMed:11457851}.
MUTAGEN 249 249 H->A: No effect on pH dependence and
function. {ECO:0000269|PubMed:11457851}.
MUTAGEN 326 326 H->A: No effect on pH dependence and
function. {ECO:0000269|PubMed:11457851}.
MUTAGEN 339 339 H->A: Loss of potentiation by Zn(2+).
{ECO:0000269|PubMed:11457851}.
MUTAGEN 365 365 N->S: Reduces N-glycosylation. Abolishes
N-glycosylation; when associated with S-
392. {ECO:0000269|PubMed:15504740}.
MUTAGEN 392 392 N->S: Reduces N-glycosylation. Abolishes
N-glycosylation; when associated with S-
365. {ECO:0000269|PubMed:15504740}.
MUTAGEN 414 414 Y->N: Increases N-glycosylation.
{ECO:0000269|PubMed:15504740}.
MUTAGEN 423 425 YEV->NES: Increases N-glycosylation.
{ECO:0000269|PubMed:15504740}.
MUTAGEN 430 430 G->C: Partial activation.
{ECO:0000269|PubMed:11457851,
ECO:0000269|PubMed:8631835}.
MUTAGEN 430 430 G->F: Constitutive activation causing
cell death. Inactive; when associated
with F-443. {ECO:0000269|PubMed:11457851,
ECO:0000269|PubMed:8631835}.
MUTAGEN 430 430 G->K,T: Constitutive activation causing
cell death. {ECO:0000269|PubMed:11457851,
ECO:0000269|PubMed:8631835}.
MUTAGEN 430 430 G->S: No constitutive activation.
{ECO:0000269|PubMed:11457851,
ECO:0000269|PubMed:8631835}.
MUTAGEN 430 430 G->V: Constitutive activation causing
cell death. Activated at lower pH; when
associated with A-72.
{ECO:0000269|PubMed:11457851,
ECO:0000269|PubMed:8631835}.
MUTAGEN 443 443 S->F: Loss of function. Inactive; when
associated with F-430.
{ECO:0000269|PubMed:8631835}.
MUTAGEN 453 455 YIY->NIS: No effect on N-glycosylation.
{ECO:0000269|PubMed:15504740}.
MUTAGEN 478 478 N->S: No effect on N-glycosylation.
{ECO:0000269|PubMed:15504740}.
MUTAGEN 487 487 N->S: No effect on N-glycosylation.
{ECO:0000269|PubMed:15504740}.
SEQUENCE 512 AA; 57739 MW; 38D0A77C3C430B03 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 GASLLTILEL FDYIYELIKE KLLDLLGKEE EEGSHDENMS
TCDTMPNHSE TISHTVNVPL QTALGTLEEI AC


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