General Information of This Target
Target ID
BTDT00154
Target Name
Potassium voltage-gated channel subfamily B member 2 (Kcnb2)
Target Bioclass
Transporter and channel
Uniprot ID
Q63099
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
Kcnb2
Synonym
CDRK; Voltage-gated potassium channel subunit Kv2.2
Sequence
MAEKAPPGLNRKTSRSTLSLPPEPVDIIRSKTCSRRVKINVGGLNHEVLWRTLDRLPRTR
LGKLRDCNTHESLLEVCDDYNLNENEYFFDRHPGAFTSILNFYRTGKLHMMEEMCALSFG
QELDYWGIDEIYLESCCQARYHQKKEQMNEELRREAETMRDGEGEEFDNTCCPEKRKKLW
DLLEKPNSSVAAKILAIVSILFIVLSTIALSLNTLPELQENDEFGQPSDNRKLAHVEAVC
IAWFTMEYLLRFLSSPNKWKFFKGPLNVIDLLAILPYYVTIFLTESNKSVLQFQNVRRVV
QIFRIMRILRILKLARHSTGLQSLGFTLRRSYNELGLLILFLAMGIMIFSSLVFFAEKDE
DATKFTSIPASFWWATITMTTVGYGDIYPKTLLGKIVGGLCCIAGVLVIALPIPIIVNNF
SEFYKEQKRQEKAIKRREALERAKRNGSIVSMNLKDAFARSMELIDVAVEKAGESANIKD
SVDDNHLSPSRWKWARKALSETSSNKSYENKYQEVSQKDSHEQLNNTSSSSPQHLSAQKL
EMLYNEITKTQTHSHPNPDCQEQPERPSAYEEEIEMEEVVCPQEQLAVAQTEVIVDMKST
SSIDSFTSCATDFTETERSPLPPPSASHLQMKFPTDLPGMDEHQRVRAPPFLTLSRDKGP
AAREAALDYAPIDITVNLDAGASHGPLQPDSASDSPKSSLKGSNPLKSRSLKVNFQENRG
SAPQTPPSTARPLPVTTADFPLTTPQHMSTILLEESPPPGTETLPGADVSAHCQGPSKGL
SPRVPKQKLFPFSSRERRSFTEIDTGEDEDFLDLQRPRPDKQADPSPNCLADKPGEARDP
LREEGCVGSSSPQNTDHNCRQDIYQAVGEVKKDSSQEGYKMENHLFAPEIHSNPGDTGYC
PTRETSM

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Family
the potassium channel family
Function
Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain and smooth muscle cells. Channels open or close in response to the voltage difference across the membrane, letting potassium ions pass in accordance with their electrochemical gradient. Homotetrameric channels mediate a delayed-rectifier voltage-dependent outward potassium current that display rapid activation and slow inactivation in response to membrane depolarization. Can form functional homotetrameric and heterotetrameric channels that contain variable proportions of KCNB1; channel properties depend on the type of alpha subunits that are part of the channel. Can also form functional heterotetrameric channels with other alpha subunits that are non-conducting when expressed alone, such as KCNS1 and KCNS2, creating a functionally diverse range of channel complexes. In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Contributes to the delayed-rectifier voltage-gated potassium current in cortical pyramidal neurons and smooth muscle cells.

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Taxonomy ID
10116
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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    Mu-theraphotoxin-Pspp1 Inhibition rate . [1]
 Toxin Info    APETx2 Inhibition rate . [2- 11]
References
Ref 1 Chemical Synthesis, Proper Folding, Na(v) Channel Selectivity Profile and Analgesic Properties of the Spider Peptide Phlotoxin 1. Toxins (Basel). 2019 Jun 21;11(6):367. doi: 10.3390/toxins11060367.
Ref 2 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 3 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 4 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 5 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 6 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 7 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 8 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 9 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 10 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 11 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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