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

 ASIC1_HUMAN             Reviewed;         528 AA.
P78348; A3KN86; E5KBL7; P78349; Q96CV2;
05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 3.
27-SEP-2017, entry version 159.
RecName: Full=Acid-sensing ion channel 1 {ECO:0000303|PubMed:10798398};
Short=ASIC1 {ECO:0000303|PubMed:10798398};
AltName: Full=Amiloride-sensitive cation channel 2, neuronal;
AltName: Full=Brain sodium channel 2 {ECO:0000303|PubMed:9037075};
Short=BNaC2 {ECO:0000303|PubMed:9037075};
Name=ASIC1; Synonyms=ACCN2, BNAC2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain;
PubMed=9037075; DOI=10.1073/pnas.94.4.1459;
Garcia-Anoveros J., Derfler B.H., Neville-Golden J., Hyman B.T.,
Corey D.P.;
"BNaC1 and BNaC2 constitute a new family of human neuronal sodium
channels related to degenerins and epithelial sodium channels.";
Proc. Natl. Acad. Sci. U.S.A. 94:1459-1464(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION (ISOFORMS 1; 2 AND
3), AND SUBCELLULAR LOCATION.
TISSUE=Spinal ganglion;
PubMed=21036899; DOI=10.1074/jbc.M110.171330;
Hoagland E.N., Sherwood T.W., Lee K.G., Walker C.J., Askwith C.C.;
"Identification of a calcium permeable human acid-sensing ion channel
1 transcript variant.";
J. Biol. Chem. 285:41852-41862(2010).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Huque T., Cao J., Lischka F.W., Spielman A.I., Feldman R.S.,
Cowart B.J., Wise P.M., Pribitkin E.A., Mackler S.A., Brand J.G.;
"Acid sensing ion channels in human taste tissue.";
Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 231-528 (ISOFORM 1).
TISSUE=Ovary;
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).
[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]
INTERACTION WITH PRKCABP.
PubMed=11802773; DOI=10.1042/0264-6021:3610443;
Hruska-Hageman A.M., Wemmie J.A., Price M.P., Welsh M.J.;
"Interaction of the synaptic protein PICK1 (protein interacting with C
kinase 1) with the non-voltage gated sodium channels BNC1 (brain Na+
channel 1) and ASIC (acid-sensing ion channel).";
Biochem. J. 361:443-450(2002).
[9]
PHOSPHORYLATION BY PKC.
PubMed=12244121; DOI=10.1074/jbc.M208995200;
Berdiev B.K., Xia J., Jovov B., Markert J.M., Mapstone T.B.,
Gillespie G.Y., Fuller C.M., Bubien J.K., Benos D.J.;
"Protein kinase C isoform antagonism controls BNaC2 (ASIC1)
function.";
J. Biol. Chem. 277:45734-45740(2002).
[10]
PHOSPHORYLATION BY PKA, MUTAGENESIS OF SER-478 AND SER-479,
PHOSPHORYLATION AT SER-479, INTERACTION WITH PRKCABP, AND SUBCELLULAR
LOCATION.
PubMed=12578970; DOI=10.1073/pnas.252782799;
Leonard A.S., Yermolaieva O., Hruska-Hageman A., Askwith C.C.,
Price M.P., Wemmie J.A., Welsh M.J.;
"cAMP-dependent protein kinase phosphorylation of the acid-sensing ion
channel-1 regulates its binding to the protein interacting with C-
kinase-1.";
Proc. Natl. Acad. Sci. U.S.A. 100:2029-2034(2003).
[11]
REGULATION BY SERINE PROTEASES.
PubMed=15247234; DOI=10.1074/jbc.M407381200;
Poirot O., Vukicevic M., Boesch A., Kellenberger S.;
"Selective regulation of acid-sensing ion channel 1 by serine
proteases.";
J. Biol. Chem. 279:38448-38457(2004).
[12]
MUTAGENESIS OF PHE-352 AND ASP-357, SITES PHE-352 AND ASP-357,
INTERACTION WITH THE SPIDER VENOM PSALMOTOXIN-1, AND SUBUNIT.
PubMed=19654327; DOI=10.1074/jbc.M109.029009;
Sherwood T., Franke R., Conneely S., Joyner J., Arumugan P.,
Askwith C.;
"Identification of protein domains that control proton and calcium
sensitivity of ASIC1a.";
J. Biol. Chem. 284:27899-27907(2009).
[13]
INTERACTION WITH SNAKE VENOM MAMBALGIN-1, 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).
[14]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SPIDER VENOM
PSALMOTOXIN-1, SUBUNIT, AND ENZYME REGULATION.
PubMed=22760635; DOI=10.1038/ncomms1917;
Dawson R.J., Benz J., Stohler P., Tetaz T., Joseph C., Huber S.,
Schmid G., Hugin D., Pflimlin P., Trube G., Rudolph M.G., Hennig M.,
Ruf A.;
"Structure of the acid-sensing ion channel 1 in complex with the
gating modifier Psalmotoxin 1.";
Nat. Commun. 3:936-943(2012).
[15]
SUBUNIT, AND INTERACTION WITH PI-THERAPHOTOXIN-HM3A.
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).
-!- FUNCTION: Isoform 2 and isoform 3 function as proton-gated sodium
channels; they are activated by a drop of the extracellular pH and
then become rapidly desensitized. The channel 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. Isoform 2 can also transport potassium,
but with lower efficiency. It is nearly impermeable to the larger
rubidium and cesium ions. Isoform 3 can also transport calcium
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:22760635}.
-!- FUNCTION: Isoform 1 does not display proton-gated cation channel
activity. {ECO:0000269|PubMed:22760635}.
-!- ENZYME REGULATION: Inhibited by the diuretic amiloride. Inhibited
by Cs(1+) ions. Inhibited by spider venom psalmotoxin-1; this
locks the channel into its desensitized conformation.
{ECO:0000269|PubMed:22760635}.
-!- SUBUNIT: Homotrimer or heterotrimer with other ASIC proteins (By
similarity). Interacts with STOM and ASIC2 (By similarity).
Interacts with PRKCABP. Homotrimer of Asic1a (ASIC1 isoform 1)
interacts with spider venom psalmotoxin-1 (PubMed:19654327,
PubMed:22760635). Homotrimer of Asic1a (ASIC1 isoform 1) and
Asic1b (ASIC1 isoform 3) interacts with the spider venom pi-
theraphotoxin-Hm3a (PubMed:28327374). Homotrimer of Asic1a (ASIC1
isoform 1) interacts with the snake venom mambalgin-1
(PubMed:23034652). Heterotrimer of Asic1a-Asic2a (ASIC1 isoform 1-
ASIC2 isoform 1) interacts with the snake venom mambalgin-1
(PubMed:23034652). {ECO:0000250, ECO:0000269|PubMed:11802773,
ECO:0000269|PubMed:12578970, ECO:0000269|PubMed:22760635,
ECO:0000269|PubMed:23034652}.
-!- INTERACTION:
Q9NRD5:PICK1; NbExp=3; IntAct=EBI-79189, EBI-79165;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12578970,
ECO:0000269|PubMed:21036899, ECO:0000269|PubMed:22760635}; Multi-
pass membrane protein {ECO:0000269|PubMed:12578970,
ECO:0000269|PubMed:21036899, ECO:0000269|PubMed:22760635}.
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=2; Synonyms=Asic1a;
IsoId=P78348-2; Sequence=Displayed;
Name=1; Synonyms=Asic1b;
IsoId=P78348-1; Sequence=VSP_015596;
Name=3;
IsoId=P78348-3; Sequence=VSP_045298;
-!- TISSUE SPECIFICITY: Expressed in most or all neurons.
-!- 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. {ECO:0000269|PubMed:12244121,
ECO:0000269|PubMed:12578970}.
-!- MISCELLANEOUS: Potentiated by Ca(2+), Mg(2+), Ba(2+) and
multivalent cations. Inhibited by anti-inflammatory drugs like
salicylic acid (By similarity). Potentiated by FMRFamide-related
neuropeptides. PH dependence may be regulated by serine proteases.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
1.A.6) family. ASIC1 subfamily. {ECO:0000305}.
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EMBL; U78180; AAB48980.1; -; mRNA.
EMBL; U78181; AAB48981.1; -; mRNA.
EMBL; HM991481; ADP44689.1; -; mRNA.
EMBL; EU078959; ABU48925.1; -; mRNA.
EMBL; AC025154; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471111; EAW58118.1; -; Genomic_DNA.
EMBL; BC013891; AAH13891.2; -; mRNA.
EMBL; BC133707; AAI33708.1; -; mRNA.
CCDS; CCDS44876.1; -. [P78348-2]
CCDS; CCDS58228.1; -. [P78348-3]
CCDS; CCDS8796.1; -. [P78348-1]
RefSeq; NP_001086.2; NM_001095.3. [P78348-2]
RefSeq; NP_001243759.1; NM_001256830.1. [P78348-3]
RefSeq; NP_064423.2; NM_020039.3. [P78348-1]
UniGene; Hs.274361; -.
ProteinModelPortal; P78348; -.
SMR; P78348; -.
BioGrid; 106559; 22.
IntAct; P78348; 2.
BindingDB; P78348; -.
ChEMBL; CHEMBL1628477; -.
DrugBank; DB00594; Amiloride.
DrugBank; DB00586; Diclofenac.
GuidetoPHARMACOLOGY; 684; -.
iPTMnet; P78348; -.
PhosphoSitePlus; P78348; -.
SwissPalm; P78348; -.
BioMuta; ASIC1; -.
DMDM; 296439456; -.
PeptideAtlas; P78348; -.
PRIDE; P78348; -.
Ensembl; ENST00000228468; ENSP00000228468; ENSG00000110881. [P78348-1]
Ensembl; ENST00000447966; ENSP00000400228; ENSG00000110881. [P78348-2]
Ensembl; ENST00000552438; ENSP00000450247; ENSG00000110881. [P78348-3]
GeneID; 41; -.
KEGG; hsa:41; -.
UCSC; uc001rvv.5; human. [P78348-2]
CTD; 41; -.
DisGeNET; 41; -.
EuPathDB; HostDB:ENSG00000110881.11; -.
GeneCards; ASIC1; -.
HGNC; HGNC:100; ASIC1.
HPA; HPA058870; -.
MIM; 602866; gene.
neXtProt; NX_P78348; -.
OpenTargets; ENSG00000110881; -.
PharmGKB; PA24434; -.
GeneTree; ENSGT00760000119120; -.
HOGENOM; HOG000247010; -.
HOVERGEN; HBG004150; -.
InParanoid; P78348; -.
KO; K04829; -.
OMA; ANFQMIN; -.
OrthoDB; EOG091G053J; -.
PhylomeDB; P78348; -.
TreeFam; TF330663; -.
Reactome; R-HSA-2672351; Stimuli-sensing channels.
SignaLink; P78348; -.
SIGNOR; P78348; -.
GeneWiki; ACCN2; -.
GenomeRNAi; 41; -.
PRO; PR:P78348; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000110881; -.
CleanEx; HS_ACCN2; -.
ExpressionAtlas; P78348; baseline and differential.
Genevisible; P78348; HS.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0045202; C:synapse; IEA:Ensembl.
GO; GO:0044736; F:acid-sensing ion channel activity; IDA:UniProtKB.
GO; GO:0022839; F:ion gated channel activity; IEA:Ensembl.
GO; GO:0015280; F:ligand-gated sodium channel activity; TAS:ProtInc.
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; IDA:UniProtKB.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
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:0009268; P:response to pH; TAS:ProtInc.
GO; GO:0050915; P:sensory perception of sour taste; IMP:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0035725; P:sodium ion transmembrane transport; IDA:UniProtKB.
GO; GO:0006814; P:sodium ion transport; NAS:UniProtKB.
GO; GO:0006810; P:transport; TAS:ProtInc.
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 1 528 Acid-sensing ion channel 1.
/FTId=PRO_0000181294.
TOPO_DOM 1 45 Cytoplasmic. {ECO:0000250}.
TRANSMEM 46 69 Helical. {ECO:0000250}.
TOPO_DOM 70 427 Extracellular. {ECO:0000250}.
TRANSMEM 428 454 Discontinuously helical. {ECO:0000250}.
TOPO_DOM 455 528 Cytoplasmic. {ECO:0000250}.
MOTIF 444 446 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}.
SITE 352 352 Important for interaction with the spider
venom psalmotoxin-1.
{ECO:0000269|PubMed:19654327}.
SITE 357 357 Key residue for defining the pH
sensitivity of ASIC1 (isoform 1).
{ECO:0000269|PubMed:19654327}.
MOD_RES 479 479 Phosphoserine; by PKA.
{ECO:0000269|PubMed:12578970}.
MOD_RES 499 499 Phosphoserine.
{ECO:0000250|UniProtKB:Q6NXK8}.
CARBOHYD 368 368 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 395 395 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 93 194 {ECO:0000250|UniProtKB:Q1XA76}.
DISULFID 172 179 {ECO:0000250|UniProtKB:Q1XA76}.
DISULFID 290 367 {ECO:0000250|UniProtKB:Q1XA76}.
DISULFID 310 363 {ECO:0000250|UniProtKB:Q1XA76}.
DISULFID 314 361 {ECO:0000250|UniProtKB:Q1XA76}.
DISULFID 323 345 {ECO:0000250|UniProtKB:Q1XA76}.
DISULFID 325 337 {ECO:0000250|UniProtKB:Q1XA76}.
VAR_SEQ 1 185 MELKAEEEEVGGVQPVSIQAFASSSTLHGLAHIFSYERLSL
KRALWALCFLGSLAVLLCVCTERVQYYFHYHHVTKLDEVAA
SQLTFPAVTLCNLNEFRFSQVSKNDLYHAGELLALLNNRYE
IPDTQMADEKQLEILQDKANFRSFKPKPFNMREFYDRAGHD
IRDMLLSCHFRGEVCSAEDFK -> MPIQIFCSMSFSSGEE
APGPLGDIWGPHHHQQQQDISESEEEEEEKEKEAVRKEASE
GHSPMDLVAFANSCTLHGTNHIFVEGGPGPRQVLWAVAFVL
ALGAFLCQVGDRVAYYLSYPHVTLLNEVATTELAFPAVTLC
NTNAVRLSQLSYPDLLYLAPMLGLDESDDPGVPLAPPGPEA
FSGEPFNLHRFYNRSCHRLEDMLLYCSYQGGPCGPHNFS
(in isoform 3).
{ECO:0000303|PubMed:21036899}.
/FTId=VSP_045298.
VAR_SEQ 433 433 G -> GELLMTPVPFSCHGHGVAPYHPKAGCSLLSHEGPPP
QRPFPKPCCLG (in isoform 1).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9037075,
ECO:0000303|Ref.3}.
/FTId=VSP_015596.
MUTAGEN 352 352 F->L: Complete loss in the shift of pH
for both activation and desensitization
by the spider venom psalmotoxin-1.
{ECO:0000269|PubMed:19654327}.
MUTAGEN 357 357 D->A,N: Large decrease in response to pH
6.5 solutions.
{ECO:0000269|PubMed:19654327}.
MUTAGEN 478 478 S->A: No effect on phosphorylation.
{ECO:0000269|PubMed:12578970}.
MUTAGEN 479 479 S->A: Loss of phosphorylation.
{ECO:0000269|PubMed:12578970}.
CONFLICT 212 212 G -> D (in Ref. 1; AAB48980/AAB48981).
{ECO:0000305}.
SEQUENCE 528 AA; 59909 MW; 9E998F711C208450 CRC64;
MELKAEEEEV GGVQPVSIQA FASSSTLHGL AHIFSYERLS LKRALWALCF LGSLAVLLCV
CTERVQYYFH YHHVTKLDEV AASQLTFPAV TLCNLNEFRF SQVSKNDLYH AGELLALLNN
RYEIPDTQMA DEKQLEILQD KANFRSFKPK PFNMREFYDR AGHDIRDMLL SCHFRGEVCS
AEDFKVVFTR YGKCYTFNSG RDGRPRLKTM KGGTGNGLEI MLDIQQDEYL PVWGETDETS
FEAGIKVQIH SQDEPPFIDQ LGFGVAPGFQ TFVACQEQRL IYLPPPWGTC KAVTMDSDLD
FFDSYSITAC RIDCETRYLV ENCNCRMVHM PGDAPYCTPE QYKECADPAL DFLVEKDQEY
CVCEMPCNLT RYGKELSMVK IPSKASAKYL AKKFNKSEQY IGENILVLDI FFEVLNYETI
EQKKAYEIAG LLGDIGGQMG LFIGASILTV LELFDYAYEV IKHKLCRRGK CQKEAKRSSA
DKGVALSLDD VKRHNPCESL RGHPAGMTYA ANILPHHPAR GTFEDFTC


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