Target Information

General Information of This Target
Target ID
BTDT00232
Target Name
Acid-sensing ion channel 2 (Asic2);Acid-sensing ion channel 3 (Asic3)
Target Bioclass
Transporter and channel
Uniprot ID
Q62962 ; O35240
3D Structure
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2D Sequence
3D Structure
Source
Predict by Alphafold2
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Alphafold Parameters: msa_mode: mmseqs2_uniref_env model_type: auto num_recycles: auto
Gene Name
Asic2;Asic3
Gene ID
25364 ; 286920
Synonym 1
Amiloride-sensitive brain sodium channel; Amiloride-sensitive brain sodium channel 2; Amiloride-sensitive cation channel 1, neuronal; Amiloride-sensitive cation channel neuronal 1; Brain sodium channel 1; Mammalian degenerin homolog
Synonym 2
Accn3; Drasic; Amiloride-sensitive cation channel 3; Dorsal root ASIC
Sequence 1
MDLKESPSEGSLQPSSIQIFANTSTLHGIRHIFVYGPLTIRRVLWAVAFVGSLGLLLVES
SERVSYYFSYQHVTKVDEVVAQSLVFPAVTLCNLNGFRFSRLTTNDLYHAGELLALLDVN
LQIPDPHLADPTVLEALRQKANFKHYKPKQFSMLEFLHRVGHDLKDMMLYCKFKGQECGH
QDFTTVFTKYGKCYMFNSGEDGKPLLTTVKGGTGNGLEIMLDIQQDEYLPIWGETEETTF
EAGVKVQIHSQSEPPFIQELGFGVAPGFQTFVATQEQRLTYLPPPWGECRSSEMGLDFFP
VYSITACRIDCETRYIVENCNCRMVHMPGDAPFCTPEQHKECAEPALGLLAEKDSNYCLC
RTPCNLTRYNKELSMVKIPSKTSAKYLEKKFNKSEKYISENILVLDIFFEALNYETIEQK
KAYEVAALLGDIGGQMGLFIGASLLTILELFDYIYELIKEKLLDLLGKEEEEGSHDENMS
TCDTMPNHSETISHTVNVPLQTALGTLEEIAC

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Sequence 2
MKPRSGLEEAQRRQASDIRVFASSCTMHGLGHIFGPGGLTLRRGLWATAVLLSLAAFLYQ
VAERVRYYGEFHHKTTLDERESHQLTFPAVTLCNINPLRRSRLTPNDLHWAGTALLGLDP
AEHAAYLRALGQPPAPPGFMPSPTFDMAQLYARAGHSLEDMLLDCRYRGQPCGPENFTVI
FTRMGQCYTFNSGAHGAELLTTPKGGAGNGLEIMLDVQQEEYLPIWKDMEETPFEVGIRV
QIHSQDEPPAIDQLGFGAAPGHQTFVSCQQQQLSFLPPPWGDCNTASLDPDDFDPEPSDP
LGSPRPRPSPPYSLIGCRLACESRYVARKCGCRMMHMPGNSPVCSPQQYKDCASPALDAM
LRKDTCVCPNPCATTRYAKELSMVRIPSRASARYLARKYNRSESYITENVLVLDIFFEAL
NYEAVEQKAAYEVSELLGDIGGQMGLFIGASLLTILEILDYLCEVFQDRVLGYFWNRRSA
QKRSGNTLLQEELNGHRTHVPHLSLGPRPPTTPCAVTKTLSASHRTCYLVTRL

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Family1
the amiloride-sensitive sodium channel (TC 1.A.6) family.
Family2
the amiloride-sensitive sodium channel family
Function 1
Cation channel with high affinity for sodium, which is gated; by extracellular protons and inhibited by the diuretic amiloride. Also; permeable for Li(+) and K(+). Activation by an extracellular pH drop is; followed by a rapid pH-independent inactivation. Heteromeric channel; assembly seems to modulate channel properties.

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Function 2
Cation channel with high affinity for sodium, which is gated by extracellular protons and inhibited by the diuretic amiloride. Generates a biphasic current with a fast inactivating and a slow sustained phase. In sensory neurons is proposed to mediate the pain induced by acidosis that occurs in ischemic, damaged or inflamed tissue. May be involved in hyperalgesia. May play a role in mechanoreception. Heteromeric channel assembly seems to modulate channel properties.

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Taxonomy ID
10116
TCDB ID
1.A.6.1.2 ; 1.A.6.1.2
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Kingdom: Metazoa
Phylum: Chordata
Class: Mammalia
Order: Rodentia
Family: Muridae
Genus: Rattus
Species: Rattus norvegicus
Toxin Information Related to This Target
                           Toxin Name Activity Data Type Activity Data Reference
 Toxin Info    APETx2 IC50
117 nM
 [1- 10]
References
Ref 1 A new sea anemone peptide, APETx2, inhibits ASIC3, a major acid-sensitive channel in sensory neurons. EMBO J. 2004 Apr 7;23(7):1516-25. doi: 10.1038/sj.emboj.7600177. Epub 2004 Mar 25.
Ref 2 ASIC3, a sensor of acidic and primary inflammatory pain. EMBO J. 2008 Nov 19;27(22):3047-55. doi: 10.1038/emboj.2008.213. Epub 2008 Oct 16.
Ref 3 Chemical synthesis and folding of APETx2, a potent and selective inhibitor of acid sensing ion channel 3. Toxicon. 2009 Jul;54(1):56-61. doi: 10.1016/j.toxicon.2009.03.014. Epub 2009 Mar 21.
Ref 4 Expression in Pichia pastoris and characterization of APETx2, a specific inhibitor of acid sensing ion channel 3. Toxicon. 2010 Dec;56(8):1388-97. doi: 10.1016/j.toxicon.2010.08.004. Epub 2010 Sep 9.
Ref 5 Inhibition of voltage-gated Na(+) currents in sensory neurones by the sea anemone toxin APETx2. Br J Pharmacol. 2012 Apr;165(7):2167-77. doi: 10.1111/j.1476-5381.2011.01674.x.
Ref 6 A natural point mutation changes both target selectivity and mechanism of action of sea anemone toxins. FASEB J. 2012 Dec;26(12):5141-51. doi: 10.1096/fj.12-218479. Epub 2012 Sep 12.
Ref 7 Cyclisation increases the stability of the sea anemone peptide APETx2 but decreases its activity at acid-sensing ion channel 3. Mar Drugs. 2012 Jul;10(7):1511-1527. doi: 10.3390/md10071511. Epub 2012 Jul 16.
Ref 8 Functional expression in Escherichia coli of the disulfide-rich sea anemone peptide APETx2, a potent blocker of acid-sensing ion channel 3. Mar Drugs. 2012 Jul;10(7):1605-1618. doi: 10.3390/md10071605. Epub 2012 Jul 23.
Ref 9 Solution structure of APETx2, a specific peptide inhibitor of ASIC3 proton-gated channels. Protein Sci. 2005 Aug;14(8):2003-10. doi: 10.1110/ps.051378905. Epub 2005 Jun 29.
Ref 10 Understanding the molecular basis of toxin promiscuity: the analgesic sea anemone peptide APETx2 interacts with acid-sensing ion channel 3 and hERG channels via overlapping pharmacophores. J Med Chem. 2014 Nov 13;57(21):9195-203. doi: 10.1021/jm501400p. Epub 2014 Nov 4.
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