ASIC3

From Wikipedia, the free encyclopedia
  (Redirected from ACCN3)
Jump to: navigation, search
ASIC3
Identifiers
Aliases ASIC3, ACCN3, DRASIC, SLNAC1, TNaC1, acid sensing ion channel subunit 3
External IDs MGI: 2159339 HomoloGene: 20999 GeneCards: ASIC3
Targeted by Drug
agmatine, Hydron, amiloride, aspirin, diclofenac, nafamostat, salicylic acid[1]
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_004769
NM_020321
NM_020322

NM_183000
NM_001310474

RefSeq (protein)

NP_004760
NP_064717
NP_064718

NP_001297403.1
NP_892045.2
NP_001297403
NP_892045

Location (UCSC) Chr 7: 151.05 – 151.05 Mb Chr 5: 24.41 – 24.42 Mb
PubMed search [2] [3]
Wikidata
View/Edit Human View/Edit Mouse

Acid-sensing ion channel 3 (ASIC3) also known as amiloride-sensitive cation channel 3 (ACCN3) or testis sodium channel 1 (TNaC1) is a protein that in humans is encoded by the ASIC3 gene. The ASIC3 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 1998.[4][5] 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.[6]

Structure and function[edit]

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[edit]

ASIC3 has been shown to interact with LIN7B,[9] GOPC[9] and MAGI1.[9]

References[edit]

  1. ^ "Drugs that physically interact with Acid sensing ion channel subunit 3 view/edit references on wikidata". 
  2. ^ "Human PubMed Reference:". 
  3. ^ "Mouse PubMed Reference:". 
  4. ^ Ishibashi K, Marumo F (June 1998). "Molecular cloning of a DEG/ENaC sodium channel cDNA from human testis". Biochem. Biophys. Res. Commun. 245 (2): 589–93. doi:10.1006/bbrc.1998.8483. PMID 9571199. 
  5. ^ de Weille JR, Bassilana F, Lazdunski M, Waldmann R (October 1998). "Identification, functional expression and chromosomal localisation of a sustained human proton-gated cation channel". FEBS Lett. 433 (3): 257–60. doi:10.1016/S0014-5793(98)00916-8. PMID 9744806. 
  6. ^ 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. 
  7. ^ 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 4756657Freely accessible. PMID 26772908. 
  8. ^ 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. 
  9. ^ a b c Hruska-Hageman AM, Benson CJ, Leonard AS, Price MP, Welsh MJ (November 2004). "PSD-95 and Lin-7b interact with acid-sensing ion channel-3 and have opposite effects on H+- gated current". J. Biol. Chem. 279 (45): 46962–8. doi:10.1074/jbc.M405874200. PMID 15317815. 

External links[edit]

Further reading[edit]