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

 ASIC1_RAT               Reviewed;         526 AA.
P55926; O88762; Q91YB8; Q99NA1;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
27-SEP-2017, entry version 141.
RecName: Full=Acid-sensing ion channel 1 {ECO:0000303|PubMed:9062189};
Short=ASIC1 {ECO:0000303|PubMed:9062189};
AltName: Full=Amiloride-sensitive cation channel 2, neuronal;
AltName: Full=Brain sodium channel 2;
Short=BNaC2;
Name=Asic1; Synonyms=Accn2, Bnac2;
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), FUNCTION, SUBCELLULAR
LOCATION, AND ENZYME REGULATION.
PubMed=9062189; DOI=10.1038/386173a0;
Waldmann R., Champigny G., Bassilana F., Heurteaux C., Lazdunski M.;
"A proton-gated cation channel involved in acid-sensing.";
Nature 386:173-177(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Spinal ganglion;
PubMed=9707631; DOI=10.1073/pnas.95.17.10240;
Chen C.-C., England S., Akopian A.N., Wood J.N.;
"A sensory neuron-specific, proton-gated ion channel.";
Proc. Natl. Acad. Sci. U.S.A. 95:10240-10245(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), DOMAIN, AND FUNCTION.
TISSUE=Inner ear;
PubMed=11448963; DOI=10.1074/jbc.M104030200;
Baessler E.-L., Ngo-Anh T.J., Geisler H.-S., Ruppersberg J.P.,
Gruender S.;
"Molecular and functional characterization of acid-sensing ion channel
(ASIC) 1b.";
J. Biol. Chem. 276:33782-33787(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
FUNCTION.
TISSUE=Trigeminal ganglion;
PubMed=11588592; DOI=10.1097/00001756-200109170-00022;
Ugawa S., Ueda T., Takahashi E., Hirabayashi Y., Yoneda T., Komai S.,
Shimada S.;
"Cloning and functional expression of ASIC-beta2, a splice variant of
ASIC-beta.";
NeuroReport 12:2865-2869(2001).
[5]
TISSUE SPECIFICITY, INTERACTION WITH ASIC1, MUTAGENESIS OF GLY-431,
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).
[6]
INTERACTION WITH THE SPIDER VENOM PSALMOTOXIN-1 TOXIN, AND SUBUNIT.
PubMed=10829030; DOI=10.1074/jbc.M003643200;
Escoubas P., de Weille J.R., Lecoq A., Diochot S., Waldmann R.,
Champigny G., Moinier D., Menez A., Lazdunski M.;
"Isolation of a tarantula toxin specific for a class of proton-gated
Na+ channels.";
J. Biol. Chem. 275:25116-25121(2000).
[7]
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).
[8]
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).
[9]
MUTAGENESIS OF PHE-100; VAL-103; LYS-105 AND ASN-106, AND FUNCTION.
PubMed=12198124; DOI=10.1074/jbc.M205877200;
Babini E., Paukert M., Geisler H.-S., Gruender S.;
"Alternative splicing and interaction with di- and polyvalent cations
control the dynamic range of acid-sensing ion channel 1 (ASIC1).";
J. Biol. Chem. 277:41597-41603(2002).
[10]
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).
[11]
MUTAGENESIS OF SER-83; GLN-84; LEU-85 AND 128-GLN--ASP-131.
PubMed=12947112; DOI=10.1074/jbc.M304441200;
Coric T., Zhang P., Todorovic N., Canessa C.M.;
"The extracellular domain determines the kinetics of desensitization
in acid-sensitive ion channel 1.";
J. Biol. Chem. 278:45240-45247(2003).
[12]
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).
[13]
MUTAGENESIS OF GLU-425; ASP-432 AND GLN-436.
PubMed=15452199; DOI=10.1085/jgp.200308973;
Paukert M., Babini E., Pusch M., Grunder S.;
"Identification of the Ca2+ blocking site of acid-sensing ion channel
(ASIC) 1: implications for channel gating.";
J. Gen. Physiol. 124:383-394(2004).
[14]
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).
[15]
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).
[16]
MUTAGENESIS OF PHE-350, INTERACTION WITH MAMBALGIN-2, AND SUBUNIT.
PubMed=24323786; DOI=10.1002/anie.201308898;
Schroeder C.I., Rash L.D., Vila-Farres X., Rosengren K.J., Mobli M.,
King G.F., Alewood P.F., Craik D.J., Durek T.;
"Chemical synthesis, 3D structure, and ASIC binding site of the toxin
mambalgin-2.";
Angew. Chem. Int. Ed. 53:1017-1020(2014).
[17]
MUTAGENESIS OF ARG-190; 259-ASP-GLN-260; 349-ASP-PHE-350; ASP-349;
PHE-350; VAL-352; GLN-356 AND GLU-357, INTERACTION WITH MAMBALGIN-2,
AND SUBUNIT.
PubMed=24695733; DOI=10.1074/jbc.M114.561076;
Salinas M., Besson T., Delettre Q., Diochot S., Boulakirba S.,
Douguet D., Lingueglia E.;
"Binding site and inhibitory mechanism of the mambalgin-2 pain-
relieving peptide on acid-sensing ion channel 1a.";
J. Biol. Chem. 289:13363-13373(2014).
[18]
MUTAGENESIS OF GLU-235; TYR-316; PHE-350 AND LYS-354, INTERACTION WITH
THE SPIDER VENOM PSALMOTOXIN-1 TOXIN, AND SUBUNIT.
PubMed=26248594; DOI=10.1111/bph.13267;
Saez N.J., Deplazes E., Cristofori-Armstrong B., Chassagnon I.R.,
Lin X., Mobli M., Mark A.E., Rash L.D., King G.F.;
"Molecular dynamics and functional studies define a hot spot of
crystal contacts essential for psalmotoxin-1 inhibition of acid-
sensing ion channel 1a.";
Br. J. Pharmacol. 172:4985-4995(2015).
[19]
MUTAGENESIS OF PHE-350, INTERACTION WITH MAMBALGIN-1, AND SUBUNIT.
PubMed=26680001; DOI=10.1074/jbc.M115.702373;
Mourier G., Salinas M., Kessler P., Stura E.A., Leblanc M., Tepshi L.,
Besson T., Diochot S., Baron A., Douguet D., Lingueglia E.,
Servent D.;
"Mambalgin-1 pain-relieving peptide, stepwise solid-phase synthesis,
crystal structure, and functional domain for acid-sensing ion channel
1a inhibition.";
J. Biol. Chem. 291:2616-2629(2016).
[20]
MUTAGENESIS OF HIS-173; PHE-174; ARG-175; GLU-177; ALA-178 AND
PHE-350, INTERACTION WITH THE SPIDER VENOM PI-THERAPHOTOXIN-HM3A, AND
SUBUNIT.
TISSUE=Venom;
PubMed=28327374; DOI=10.1016/j.neuropharm.2017.03.020;
Er S.Y., Cristofori-Armstrong B., Escoubas P., Rash L.D.;
"Discovery and molecular interaction studies of a highly stable,
tarantula peptide modulator of acid-sensing ion channel 1.";
Neuropharmacology 114:3750-3755(2017).
[21]
MUTAGENESIS OF PHE-350, INTERACTION WITH THE SPIDER PI-HEXATOXIN-HI1A,
AND SUBUNIT.
PubMed=28320941; DOI=10.1073/pnas.1614728114;
Chassagnon I.R., McCarthy C.A., Chin Y.K., Pineda S.S., Keramidas A.,
Mobli M., Pham V., De Silva T.M., Lynch J.W., Widdop R.E., Rash L.D.,
King G.F.;
"Potent neuroprotection after stroke afforded by a double-knot spider-
venom peptide that inhibits acid-sensing ion channel 1a.";
Proc. Natl. Acad. Sci. U.S.A. 114:3750-3755(2017).
-!- 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. Isoform 3
discrimates stronger than isoform 1 between monovalent cations.
Isoform 3 can flux Ca(2+) while isoform 1 cannot. Heteromeric
channels composed of isoform 2 and isoform 3 are active but have a
lower pH-sensitivity. 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. {ECO:0000269|PubMed:11448963,
ECO:0000269|PubMed:11588592, ECO:0000269|PubMed:12198124,
ECO:0000269|PubMed:15369669, ECO:0000269|PubMed:9062189,
ECO:0000269|PubMed:9360943, ECO:0000269|PubMed:9707631}.
-!- ENZYME REGULATION: Inhibited by the diuretic amiloride.
{ECO:0000269|PubMed:9062189}.
-!- SUBUNIT: Homotrimer or heterotrimer with other ASIC proteins (By
similarity). Interacts with STOM and PRKCABP (By similarity).
Interacts with ASIC2. Interacts with the spider venom Pi-
hexatoxin-Hi1a (PubMed:28320941). Homotrimer of Asic1a interacts
with the spider venom psalmotoxin-1 (PubMed:10829030,
PubMed:26248594). Homotrimer of Asic1a and Asic1b and heterotrimer
of Asic1a/Asic1b interact with the spider venom Pi-theraphotoxin-
Hm3a (PubMed:28327374). Homotrimer of Asic1a interacts with the
snake venom mambalgin-1, mambalgin-2 and mambalgin-3
(PubMed:23034652, PubMed:23624383, PubMed:24323786,
PubMed:24695733, PubMed:26680001). Homotrimer of Asic1b interacts
with the snake venom mambalgin-1, mambalgin-2 and mambalgin-3
(PubMed:23034652, PubMed:23624383, PubMed:24323786,
PubMed:26680001). Heterotrimer of Asic1a-Asic1b interacts with the
snake venom mambalgin-1 and mambalgin-2 (PubMed:23034652).
Heterotrimer of Asic1a-Asic2a interacts with the snake venom
mambalgin-1, mambalgin-2 and mambalgin-3 (PubMed:23034652,
PubMed:23624383, PubMed:26680001). Heterotrimer of Asic1a-Asic2b
interacts with the snake venom mambalgin-1 and mambalgin-2
(PubMed:23034652). {ECO:0000250, ECO:0000269|PubMed:10829030,
ECO:0000269|PubMed:23034652, ECO:0000269|PubMed:23624383,
ECO:0000269|PubMed:24323786, ECO:0000269|PubMed:24695733,
ECO:0000269|PubMed:26248594, ECO:0000269|PubMed:26680001,
ECO:0000269|PubMed:28320941, ECO:0000269|PubMed:28327374,
ECO:0000269|PubMed:9360943}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11842212,
ECO:0000269|PubMed:9062189, ECO:0000269|PubMed:9707631}; Multi-
pass membrane protein {ECO:0000269|PubMed:11842212,
ECO:0000269|PubMed:9062189, ECO:0000269|PubMed:9707631}.
Note=Localizes in synaptosomes at dendritic synapses of neurons.
Colocalizes with DLG4 (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=ASIC-alpha, asic1alpha;
IsoId=P55926-1; Sequence=Displayed;
Name=2; Synonyms=ASIC-beta2;
IsoId=P55926-2; Sequence=VSP_015597, VSP_015598;
Note=Inactive.;
Name=3; Synonyms=ASIC-beta, ASIC1b;
IsoId=P55926-3; Sequence=VSP_015597, VSP_015599;
Note=Blocked by Ca(2+). Mutagenesis of Asp-465 to Asn reduces
Ca(2+) block. Ref.2 (CAA07080) sequence differs from that shown
due to frameshifts in positions 7 and 14. Ref.2 (CAA07080)
sequence is in conflict in position: 128:T->S. {ECO:0000305};
-!- TISSUE SPECIFICITY: Expressed in dorsal root ganglia and sciatic
nerve (at protein level). Widely distributed throughout the brain.
Expressed in olfactory bulb, neo and allocortical regions, dentate
granule cells, pyramidal cells of CA1-CA3 subfields of the
hippocampal formation, habenula, basolateral amygdaloid nuclei,
and in the Purkinje and granule cells of the cerebellum. Diffusely
detected over most other regions of the basal ganglia, including
thalamic nuclei, substantia nigra, striatum and globus pallidus,
hypothalamus, midbrain, pons, medulla and choroid plexus. Isoform
3 is expressed only in dorsal root ganglion (DRG) while isoform 1
is expressed in DRG, spinal chord, trigeminal ganglia and the
trigeminal mesencephalic nucleus. {ECO:0000269|PubMed:11588592,
ECO:0000269|PubMed:11842212, ECO:0000269|PubMed:9360943,
ECO:0000269|PubMed:9707631}.
-!- INDUCTION: Up-regulation upon tissues inflammation is abolished by
anti-inflammatory drugs. {ECO:0000269|PubMed:11588175}.
-!- 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}.
-!- 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. Isoform 1
homomultimeric channel is specifically and reversibly inhibited by
psalmotoxin-1, a spider venom toxin, while isoform 2 and other
ASICs are insensitive.
-!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
1.A.6) family. ASIC1 subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA07080.1; Type=Frameshift; Positions=119, 122, 142; Evidence={ECO:0000305};
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EMBL; U94403; AAB53002.1; -; mRNA.
EMBL; AJ006519; CAA07080.1; ALT_FRAME; mRNA.
EMBL; AJ309926; CAC44267.1; -; mRNA.
EMBL; AB049451; BAB39864.1; -; mRNA.
RefSeq; NP_077068.1; NM_024154.2. [P55926-1]
RefSeq; XP_006257440.1; XM_006257378.3. [P55926-3]
UniGene; Rn.37385; -.
ProteinModelPortal; P55926; -.
SMR; P55926; -.
IntAct; P55926; 1.
MINT; MINT-223538; -.
ChEMBL; CHEMBL3562170; -.
GuidetoPHARMACOLOGY; 684; -.
TCDB; 1.A.6.1.2; the epithelial na(+) channel (enac) family.
iPTMnet; P55926; -.
PhosphoSitePlus; P55926; -.
SwissPalm; P55926; -.
PRIDE; P55926; -.
Ensembl; ENSRNOT00000077175; ENSRNOP00000072206; ENSRNOG00000059765. [P55926-2]
Ensembl; ENSRNOT00000088191; ENSRNOP00000068902; ENSRNOG00000059765. [P55926-1]
GeneID; 79123; -.
KEGG; rno:79123; -.
CTD; 41; -.
RGD; 71062; Asic1.
GeneTree; ENSGT00760000119120; -.
HOGENOM; HOG000247010; -.
HOVERGEN; HBG004150; -.
InParanoid; P55926; -.
KO; K04829; -.
OMA; ANFQMIN; -.
OrthoDB; EOG091G053J; -.
PhylomeDB; P55926; -.
TreeFam; TF330663; -.
Reactome; R-RNO-2672351; Stimuli-sensing channels.
PRO; PR:P55926; -.
Proteomes; UP000002494; Chromosome 7.
Bgee; ENSRNOG00000059765; -.
ExpressionAtlas; P55926; differential.
Genevisible; P55926; RN.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0045202; C:synapse; IEA:Ensembl.
GO; GO:0044736; F:acid-sensing ion channel activity; ISS:UniProtKB.
GO; GO:0005216; F:ion channel activity; IDA:RGD.
GO; GO:0022839; F:ion gated channel activity; IEA:Ensembl.
GO; GO:0008306; P:associative learning; IEA:Ensembl.
GO; GO:0070588; P:calcium ion transmembrane transport; IEA:Ensembl.
GO; GO:0071467; P:cellular response to pH; ISS:UniProtKB.
GO; GO:0034220; P:ion transmembrane transport; IMP:RGD.
GO; GO:0007613; P:memory; IEA:Ensembl.
GO; GO:0046929; P:negative regulation of neurotransmitter secretion; IEA:Ensembl.
GO; GO:0070207; P:protein homotrimerization; ISS:UniProtKB.
GO; GO:0042391; P:regulation of membrane potential; IEA:Ensembl.
GO; GO:0010447; P:response to acidic pH; IEA:Ensembl.
GO; GO:0019233; P:sensory perception of pain; NAS:RGD.
GO; GO:0050915; P:sensory perception of sour taste; IEA:Ensembl.
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_0000181300.
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}.
REGION 20 25 Involved in divalent cations
permeability.
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 175 175 Important residue in interaction with the
spider venom Pi-theraphotoxin-Hm3a, which
can explain functional difference between
ASIC1a and ASIC1b.
{ECO:0000269|PubMed:28327374}.
SITE 177 177 Important residue for interaction with
the spider venom Pi-theraphotoxin-Hm3a,
which can explain functional difference
between ASIC1a and ASIC1b.
{ECO:0000269|PubMed:28327374}.
SITE 287 287 Important for channel gating.
{ECO:0000250}.
SITE 349 349 Important for interaction with the snake
venom mambalgin-2.
{ECO:0000269|PubMed:24695733}.
SITE 350 350 Important for interaction with the snake
venom mambalgin-1 and mambalgin-2 toxins,
probably binds to its residue L-53;
Important for interaction with the spider
venom Pi-hexatoxin-Hi1a and psalmotoxin-
1. {ECO:0000269|PubMed:24323786,
ECO:0000269|PubMed:24695733,
ECO:0000269|PubMed:26248594,
ECO:0000269|PubMed:26680001,
ECO:0000269|PubMed:28320941}.
MOD_RES 477 477 Phosphoserine.
{ECO:0000250|UniProtKB:P78348}.
MOD_RES 497 497 Phosphoserine.
{ECO:0000250|UniProtKB:Q6NXK8}.
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 1 185 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:11448963,
ECO:0000303|PubMed:11588592,
ECO:0000303|PubMed:9707631}.
/FTId=VSP_015597.
VAR_SEQ 186 186 V -> MADIWGPHHHRQQQDSSESEEEEEKEMEAGSELDEG
DDSPRDLVAFANSCTLHGASHVFVEGGPGPRQALWAVAFVI
ALGAFLCQ (in isoform 2).
{ECO:0000303|PubMed:11588592}.
/FTId=VSP_015598.
VAR_SEQ 186 186 V -> MPIQIFCSVSFSSGEEAPGSMADIWGPHHHRQQQDS
SESEEEEEKEMEAGSELDEGDDSPRDLVAFANSCTLHGASH
VFVEGGPGPRQALWAVAFVIALGAFLCQVGDRVAYYLSYPH
VTLLDEVATTELVFPAVTFCNTNAVRLSQLSYPDLLYLAPM
LGLDESDDPGVPLAPPGPEAFSGEPFNLHRFYNRSCHRLED
MLLYCSYCGGPCGPHNFSV (in isoform 3).
{ECO:0000303|PubMed:11448963,
ECO:0000303|PubMed:9707631}.
/FTId=VSP_015599.
MUTAGEN 83 83 S->P: No effect. Increases
desensitization rates; when associated
with L-84 and M-85.
{ECO:0000269|PubMed:12947112}.
MUTAGEN 84 84 Q->L: No effect. Increases
desensitization rates; when associated
with P-83 and M-85.
{ECO:0000269|PubMed:12947112}.
MUTAGEN 85 85 L->M: No effect. Increases
desensitization rates; when associated
with P-83 and L-84.
{ECO:0000269|PubMed:12947112}.
MUTAGEN 100 100 F->L: No effect on channel activation and
inactivation.
{ECO:0000269|PubMed:12198124}.
MUTAGEN 103 103 V->L: No effect on channel activation and
inactivation.
{ECO:0000269|PubMed:12198124}.
MUTAGEN 105 105 K->Y: Activated and inactivated at lower
pH. {ECO:0000269|PubMed:12198124}.
MUTAGEN 106 106 N->P: Activated and inactivated at lower
pH. {ECO:0000269|PubMed:12198124}.
MUTAGEN 128 131 QMAD->HLVE: No effect on desensitization
rates. {ECO:0000269|PubMed:12947112}.
MUTAGEN 173 173 H->S: No significant decrease in
inhibition by the spider pi-
theraphotoxin-Hm3a.
{ECO:0000269|PubMed:28327374}.
MUTAGEN 174 174 F->Y: No significant decrease in
inhibition by the spider pi-
theraphotoxin-Hm3a.
{ECO:0000269|PubMed:28327374}.
MUTAGEN 175 175 R->C: 18-fold decrease in inhibition by
the spider pi-theraphotoxin-Hm3a.
{ECO:0000269|PubMed:28327374}.
MUTAGEN 177 177 E->G: 10-fold decrease in inhibition by
the spider pi-theraphotoxin-Hm3a.
{ECO:0000269|PubMed:28327374}.
MUTAGEN 178 178 A->P: No significant decrease in
inhibition by the spider pi-
theraphotoxin-Hm3a.
{ECO:0000269|PubMed:28327374}.
MUTAGEN 178 178 A->V: No significant decrease in
inhibition by the spider pi-
theraphotoxin-Hm3a.
{ECO:0000269|PubMed:28327374}.
MUTAGEN 190 190 R->K: Small decrease in inhibition by the
snake mambalgin-2 toxin; RDQ-KQE mutant.
{ECO:0000269|PubMed:24695733}.
MUTAGEN 235 235 E->A: No change in the shift of pH for
both activation and desensitization by
the spider venom psalmotoxin-1.
{ECO:0000269|PubMed:26248594}.
MUTAGEN 259 260 DQ->QE: Small decrease in inhibition by
the snake mambalgin-2 toxin; RDQ-KQE
mutant. {ECO:0000269|PubMed:24695733}.
MUTAGEN 316 316 Y->A: No change in the shift of pH for
both activation and desensitization by
the spider venom psalmotoxin-1.
{ECO:0000269|PubMed:26248594}.
MUTAGEN 349 350 DF->GL: Complete loss in inhibition by
200 nM of the snake mambalgin-2 toxin.
{ECO:0000269|PubMed:24695733}.
MUTAGEN 349 349 D->G: High decrease in inhibition by the
snake mambalgin-2 toxin.
{ECO:0000269|PubMed:24695733}.
MUTAGEN 350 350 F->A: Complete loss of inhibition by the
spider Pi-hexatoxin-Hi1a, and by the
snake mambalgin-2 toxin. Potentiated by
the spider pi-theraphotoxin-Hm3a (at both
pH 7.35 and 7.45) and inhibited at higher
toxin concentration at pH 7.35. Complete
loss in the shift of pH for both
activation and desensitization by the
spider venom psalmotoxin-1.
{ECO:0000269|PubMed:24323786,
ECO:0000269|PubMed:26248594,
ECO:0000269|PubMed:28320941,
ECO:0000269|PubMed:28327374}.
MUTAGEN 350 350 F->L: 37-fold decrease in inbibition by
the snake mambalgin-1 toxin. Very high
decrease in inhibition by the snake
mambalgin-2 toxin.
{ECO:0000269|PubMed:24695733,
ECO:0000269|PubMed:26680001}.
MUTAGEN 352 352 V->A: Moderate decrease in inhibition by
the snake mambalgin-2 toxin.
{ECO:0000269|PubMed:24695733}.
MUTAGEN 354 354 K->A: No change in the shift of pH for
both activation and desensitization by
the spider venom psalmotoxin-1.
{ECO:0000269|PubMed:26248594}.
MUTAGEN 356 356 Q->S: Moderate decrease in inhibition by
the snake mambalgin-2 toxin.
{ECO:0000269|PubMed:24695733}.
MUTAGEN 357 357 E->N: Moderate decrease in inhibition by
the snake mambalgin-2 toxin.
{ECO:0000269|PubMed:24695733}.
MUTAGEN 425 425 E->G: Reduction of Ca(2+) block. Loss of
Ca(2+) block; when associated with C-432.
{ECO:0000269|PubMed:15452199}.
MUTAGEN 431 431 G->V,F: Constitutive channel activity.
{ECO:0000269|PubMed:9360943}.
MUTAGEN 432 432 D->A: Reduction of Ca(2+) block.
{ECO:0000269|PubMed:15452199}.
MUTAGEN 432 432 D->C: Reduction of Ca(2+) block. Loss of
Ca(2+) block; when associated with G-425.
{ECO:0000269|PubMed:15452199}.
MUTAGEN 436 436 Q->N: No effect on Ca(2+) block.
{ECO:0000269|PubMed:15452199}.
SEQUENCE 526 AA; 59641 MW; 5462A7786E2A1726 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 KEAKRSSADK
GVALSLDDVK RHNPCESLRG HPAGMTYAAN ILPHHPARGT FEDFTC


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