[1]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain;
DOI=10.1073/pnas.94.4.1459; PubMed=9037075 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[2]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 231-528 (ISOFORM 1).
TISSUE=Ovary;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[3]
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REGULATION BY FMRFAMIDE-RELATED PEPTIDES.
DOI=10.1016/S0896-6273(00)81144-7; PubMed=10798398 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[4]
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INTERACTION WITH PRKCABP.
DOI=10.1042/0264-6021:3610443; PubMed=11802773 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[5]
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PHOSPHORYLATION BY PKC.
DOI=10.1074/jbc.M208995200; PubMed=12244121 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[6]
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PHOSPHORYLATION BY PKA, MUTAGENESIS OF SER-478 AND SER-479, PHOSPHORYLATION AT SER-479, INTERACTION WITH PRKCABP, AND SUBCELLULAR LOCATION.
DOI=10.1073/pnas.252782799; PubMed=12578970 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[7]
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REGULATION BY SERINE PROTEASES.
DOI=10.1074/jbc.M407381200; PubMed=15247234 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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- FUNCTION: Cation channel with high affinity for sodium, which is gated by extracellular protons and inhibited by the diuretic amiloride. Also permeable for Ca(2+), Li(+) and K(+). Generates a biphasic current with a fast inactivating and a slow sustained phase. 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 (By similarity).
- SUBUNIT: Homotetramer or heterotetramer with other ASIC proteins (Probable). Interacts with STOM and ACCN1 (By similarity). Interacts with PRKCABP.
- INTERACTION:
Q9NRD5:PICK1; NbExp=1; IntAct=EBI-79189, EBI-79165;
- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein (By similarity). Note=Localizes in synaptosomes at dendritic synapses of neurons. Colocalizes with DLG4 (By similarity).
- ALTERNATIVE PRODUCTS:
2 named isoforms [FASTA] produced by alternative splicing. The splice variant from ASIC1a described in mouse and rat, which gives rise to an isoform with different N-termini (Asic1b), does not seem to exist in human.
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| Name | 1 |
| Isoform ID | P78348-1 |
| Features which should be applied to build the isoform sequence: VSP_015596. |
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- TISSUE SPECIFICITY: Expressed in most or all neurons.
- PTM: Phosphorylation by PKA regulates interaction with PRKCABP and subcellular location. Phosphorylation by PKC may regulate the channel.
- 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.
- SIMILARITY: Belongs to the amiloride-sensitive sodium channel family.
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