ASIC1

Identifiers

ASIC1, ACCN2, ASIC, BNaC2, acid sensing ion channel subunit 1

External IDs

MGI: 1194915 HomoloGene: 121755 GeneCards: ASIC1

Targeted by Drug

Hydron, amiloride, benzamil, ibuprofen, nafamostat^[1]

Gene ontology
Molecular function	• ion gated channel activity • sodium channel activity • ion channel activity • protein binding • cation channel activity • ligand-gated sodium channel activity • acid-sensing ion channel activity
Cellular component	• integral component of membrane • membrane • plasma membrane • synapse • integral component of plasma membrane • cell surface
Biological process	• negative regulation of neurotransmitter secretion • associative learning • sodium ion transmembrane transport • sodium ion transport • regulation of membrane potential • cation transport • memory • sensory perception of sour taste • ion transport • protein homotrimerization • ion transmembrane transport • cellular response to pH • calcium ion transmembrane transport • transport • response to pH • signal transduction • response to acidic pH • calcium ion transport
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


41


11419

Ensembl


ENSG00000110881


ENSMUSG00000023017

UniProt


P78348


Q6NXK8

RefSeq (mRNA)


NM_001095 NM_001256830 NM_020039


NM_001289791 NM_009597

RefSeq (protein)


NP_001086.2 NP_001243759.1 NP_064423.2


NP_001276720.1 NP_033727.1

Location (UCSC)

Chr 12: 50.06 – 50.08 Mb

Chr 15: 99.67 – 99.7 Mb

PubMed search

^[2]

^[3]

Wikidata

View/Edit Human

View/Edit Mouse

Acid-sensing ion channel 1 (ASIC1) also known as amiloride-sensitive cation channel 2, neuronal (ACCN2) or brain sodium channel 2 (BNaC2) is a protein that in humans is encoded by the ASIC1 gene. The ASIC1 gene is one of the five paralogous genes that encode proteins that form trimeric acid-sensing ion channels (ASICs) in mammals. The cDNA of this gene was first cloned in 1996.^[4] The ASIC genes have splicing variants that encode different proteins that are called isoforms.

These genes are mainly expressed in the central and peripheral nervous system.

ASICs can form both homotrimeric (meaning composed of three identical subunits) and heterotrimeric channels.^[5]^[6]

Structure and function

This gene encodes a member of the ASIC/ENaC superfamily of proteins.^[7] The members of this family are amiloride-sensitive sodium channels that contain intracellular N and C termini, 2 hydrophobic transmembrane (TM) regions, and a large extracellular loop, which has many cysteine residues with conserved spacing. The TM regions are generally symbolized as TM1 (clone to N-terminus) and TM2 (close to C-terminus).

The pore of the channel through which ions selectively flow from the extracellular side into the cytoplasm is formed by the three TM2 regions of the trimer.^[8]

Interactions

ASIC1 has been shown to interact with PICK1.^[9]^[10]

References

↑ "Drugs that physically interact with Acid-sensing ion channel 1 view/edit references on wikidata".
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ García-Añoveros J, Derfler B, Neville-Golden J, Hyman BT, Corey DP (March 1997). "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 (4): 1459–64. doi:10.1073/pnas.94.4.1459. PMC 19813. PMID 9037075.
↑ Babinski K, Catarsi S, Biagini G, Séguéla P (Sep 2000). "Mammalian ASIC2a and ASIC3 subunits co-assemble into heteromeric proton-gated channels sensitive to Gd3+". The Journal of Biological Chemistry. 275 (37): 28519–25. doi:10.1074/jbc.M004114200. PMID 10842183.
↑ Bassilana F, Champigny G, Waldmann R, de Weille JR, Heurteaux C, Lazdunski M (Nov 1997). "The acid-sensitive ionic channel subunit ASIC and the mammalian degenerin MDEG form a heteromultimeric H+-gated Na+ channel with novel properties". The Journal of Biological Chemistry. 272 (46): 28819–22. doi:10.1074/jbc.272.46.28819. PMID 9360943.
↑ Hanukoglu I, Hanukoglu A (Jan 2016). "Epithelial sodium channel (ENaC) family: Phylogeny, structure-function, tissue distribution, and associated inherited diseases.". Gene. 579 (2): 95–132. doi:10.1016/j.gene.2015.12.061. PMC 4756657. PMID 26772908.
↑ Hanukoglu I (2016). "ASIC and ENaC type sodium channels: Conformational states and the structures of the ion selectivity filters". FEBS Journal. doi:10.1111/febs.13840. PMID 27580245.
↑ Leonard AS, Yermolaieva O, Hruska-Hageman A, Askwith CC, Price MP, Wemmie JA, Welsh MJ (February 2003). "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 (4): 2029–34. doi:10.1073/pnas.252782799. PMC 149953. PMID 12578970.
↑ Hruska-Hageman AM, Wemmie JA, Price MP, Welsh MJ (February 2002). "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 (Pt 3): 443–50. doi:10.1042/0264-6021:3610443. PMC 1222326. PMID 11802773.

External links

Human ASIC1 genome location and ASIC1 gene details page in the UCSC Genome Browser.

Corey DP, García-Añoveros J (1996). "Mechanosensation and the DEG/ENaC ion channels". Science. 273 (5273): 323–4. doi:10.1126/science.273.5273.323. PMID 8685718.
Waldmann R, Champigny G, Bassilana F, Heurteaux C, Lazdunski M (1997). "A proton-gated cation channel involved in acid-sensing". Nature. 386 (6621): 173–7. doi:10.1038/386173a0. PMID 9062189.
Bubien JK, Keeton DA, Fuller CM, Gillespie GY, Reddy AT, Mapstone TB, Benos DJ (1999). "Malignant human gliomas express an amiloride-sensitive Na+ conductance". Am. J. Physiol. 276 (6 Pt 1): C1405–10. PMID 10362604.
Askwith CC, Cheng C, Ikuma M, Benson C, Price MP, Welsh MJ (2000). "Neuropeptide FF and FMRFamide potentiate acid-evoked currents from sensory neurons and proton-gated DEG/ENaC channels". Neuron. 26 (1): 133–41. doi:10.1016/S0896-6273(00)81144-7. PMID 10798398.
Bässler EL, Ngo-Anh TJ, Geisler HS, Ruppersberg JP, Gründer S (2001). "Molecular and functional characterization of acid-sensing ion channel (ASIC) 1b". J. Biol. Chem. 276 (36): 33782–7. doi:10.1074/jbc.M104030200. PMID 11448963.
Gunthorpe MJ, Smith GD, Davis JB, Randall AD (2001). "Characterisation of a human acid-sensing ion channel (hASIC1a) endogenously expressed in HEK293 cells". Pflugers Arch. 442 (5): 668–74. doi:10.1007/s004240100584. PMID 11512022.
Duggan A, Garcia-Anoveros J, Corey DP (2002). "The PDZ domain protein PICK1 and the sodium channel BNaC1 interact and localize at mechanosensory terminals of dorsal root ganglion neurons and dendrites of central neurons". J. Biol. Chem. 277 (7): 5203–8. doi:10.1074/jbc.M104748200. PMID 11739374.
Ji HL, Jovov B, Fu J, Bishop LR, Mebane HC, Fuller CM, Stanton BA, Benos DJ (2002). "Up-regulation of acid-gated Na(+) channels (ASICs) by cystic fibrosis transmembrane conductance regulator co-expression in Xenopus oocytes". J. Biol. Chem. 277 (10): 8395–405. doi:10.1074/jbc.M109465200. PMID 11748227.
Hruska-Hageman AM, Wemmie JA, Price MP, Welsh MJ (2002). "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 (Pt 3): 443–50. doi:10.1042/0264-6021:3610443. PMC 1222326. PMID 11802773.
Wemmie JA, Chen J, Askwith CC, Hruska-Hageman AM, Price MP, Nolan BC, Yoder PG, Lamani E, Hoshi T, Freeman JH, Welsh MJ (2002). "The acid-activated ion channel ASIC contributes to synaptic plasticity, learning, and memory". Neuron. 34 (3): 463–77. doi:10.1016/S0896-6273(02)00661-X. PMID 11988176.
Berdiev BK, Xia J, Jovov B, Markert JM, Mapstone TB, Gillespie GY, Fuller CM, Bubien JK, Benos DJ (2003). "Protein kinase C isoform antagonism controls BNaC2 (ASIC1) function". J. Biol. Chem. 277 (48): 45734–40. doi:10.1074/jbc.M208995200. PMID 12244121.
Ugawa S, Ueda T, Ishida Y, Nishigaki M, Shibata Y, Shimada S (2002). "Amiloride-blockable acid-sensing ion channels are leading acid sensors expressed in human nociceptors". J. Clin. Invest. 110 (8): 1185–90. doi:10.1172/JCI15709. PMC 150796. PMID 12393854.
Leonard AS, Yermolaieva O, Hruska-Hageman A, Askwith CC, Price MP, Wemmie JA, Welsh MJ (2003). "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 (4): 2029–34. doi:10.1073/pnas.252782799. PMC 149953. PMID 12578970.
Wemmie JA, Coryell MW, Askwith CC, Lamani E, Leonard AS, Sigmund CD, Welsh MJ (2004). "Overexpression of acid-sensing ion channel 1a in transgenic mice increases acquired fear-related behavior". Proc. Natl. Acad. Sci. U.S.A. 101 (10): 3621–6. doi:10.1073/pnas.0308753101. PMC 373512. PMID 14988500.
Poirot O, Vukicevic M, Boesch A, Kellenberger S (2004). "Selective regulation of acid-sensing ion channel 1 by serine proteases". J. Biol. Chem. 279 (37): 38448–57. doi:10.1074/jbc.M407381200. PMID 15247234.
Price MP, Thompson RJ, Eshcol JO, Wemmie JA, Benson CJ (2005). "Stomatin modulates gating of acid-sensing ion channels". J. Biol. Chem. 279 (51): 53886–91. doi:10.1074/jbc.M407708200. PMID 15471860.

Membrane transport protein: ion channels (TC 1A)

Ca²⁺: Calcium channel

Ligand-gated	Inositol trisphosphate receptor 1 2 3 Ryanodine receptor 1 2 3

Voltage-gated	L-type/Ca_vα 1.1 1.2 1.3 1.4 N-type/Ca_vα2.2 P-type/Ca_vα 2.1 Q-type/Ca_vα2.1 R-type/Ca_vα2.3 T-type/Ca_vα 3.1 3.2 3.3 α₂δ-subunits 1 2 β-subunits β1 β2 β3 β4 γ-subunits γ1 γ2 γ3 γ4 Cation channels of sperm 1 2 3 4 Two-pore channel 1 2

Na⁺: Sodium channel

Constitutively active	Epithelial sodium channel α β γ δ

Proton-gated	Amiloride-sensitive cation channel 1 2 3 4

Voltage-gated	Na_vα 1.1 1.2 1.3 1.4 1.5 1.6 1.7 1.8 1.9 7A Na_vβ 1 2 3 4

K⁺: Potassium channel

Calcium-activated	BK channel α1 β1 β2 β3 β4 SK channel SK1 SK2 SK3 IK channel IK1 K_Ca 1.1 2.1 2.2 2.3 3.1 4.1 4.2 5.1

Inward-rectifier	K_ATP K_ir 1.1 2.1 2.2 2.3 2.4 2.6 GIRK/K_ir 3.1 3.2 3.3 3.4 K_ir 4.1 4.2 5.1 6.1 6.2 7.1

Tandem pore domain	K2P 1 2 3 4 5 6 7 9 10 12 13 15 16 17 18

Voltage-gated	K_vα1-6 1.1 1.2 1.3 1.4 1.5 1.6 1.7 1.8 2.1 2.2 3.1 3.2 3.3 3.4 4.1 4.2 4.3 5.1 6.1 6.2 6.3 6.4 K_vα7-12 7.1 7.2 7.3 7.4 7.5 8.1 8.2 9.1 9.2 9.3 10.1 10.2 11.1/hERG 11.2 11.3 12.1 12.2 12.3 K_vβ 1 2 3 KCNIP 1 2 3 4 minK/ISK minK/ISK-like MiRP 1 2 3 Shaker gene

Miscellaneous

Cl⁻: Chloride channel	Calcium-activated chloride channels Anoctamin ANO1 Bestrophin 1 2 Chloride Channel Accessory 1 2 3 4 CFTR CLCN 1 2 3 4 5 6 7 KA KB CLIC 1 2 3 4 5 6 L1 CLNS 1A 1B

H⁺: Proton channel	HVCN1

M⁺: CNG cation channel	α 1 2 3 4 β 1 2 3 HCN FC 1 2 3 4

M⁺: TRP cation channel	TRPA (1) TRPC 1 2 3 4 4AP 5 6 7 TRPM 1 2 3 4 5 6 7 8 TRPML 1 2 3 TRPN TRPP 1 2 TRPV 1 2 3 4 5 6

H₂O (+ solutes): Porin	Aquaporin 0 1 2 3 4 5 6 7 8 9 Voltage-dependent anion channel 1 2 3 General bacterial porin family

Cytoplasm: Gap junction	Connexin: A GJA1 GJA3 GJA4 GJA5 GJA8 GJA9 GJA10 B GJB1 GJB2 GJB3 GJB4 GJB5 GJB6 GJB7 C GJC1 GJC2 GJC3 D GJD2 GJD3 GJD4) Innexin

By gating mechanism

Ion channel class	Ligand-gated Light-gated Voltage-gated Stretch-activated

see also disorders

This article is issued from Wikipedia - version of the 11/30/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.

ASIC1

Structure and function

Interactions

References

External links

Further reading