Two-pore-domain potassium channel

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Tandem pore domain potassium channel
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The two-pore-domain or tandem pore domain potassium channels are a family of 15 members that form what is known as leak channels which possess

G-proteins.[2] Two-pore-domain potassium channels correspond structurally to a inward-rectifier potassium channel α-subunits. Each inward-rectifier potassium channel α-subunit is composed of two transmembrane α-helices, a pore helix and a potassium ion selectivity filter sequence and assembles into a tetramer forming the complete channel.[3] The two-pore domain potassium channels instead are dimers where each subunit is essentially two α-subunits joined together.[4]

Each single channel does not have two pores; the name of the channel comes from the fact that each subunit has two P (pore) domains in its primary sequence.[5] To quote Rang and Dale (2015), "The nomenclature is misleading, especially when they are incorrectly referred to as two-pore channels".[6]

Below is a list of the 15 known two-pore-domain human potassium channels:[1]

Gene Channel[7] Family Aliases
KCNK1 K2p1.1 TWIK[2][8] TWIK-1
KCNK2 K2p2.1 TREK[2][8] TREK-1
KCNK3 K2p3.1 TASK[2][8] TASK-1
KCNK4 K2p4.1 TREK[2][8] TRAAK[9]
KCNK5 K2p5.1 TASK[2][8] TASK-2[10]
KCNK6 K2p6.1 TWIK[2][8] TWIK-2
KCNK7 K2p7.1 TWIK[2][8]
KCNK9 K2p9.1 TASK[2][8] TASK-3
KCNK10 K2p10.1 TREK[2][8] TREK-2
KCNK12 K2p12.1 THIK THIK-2
KCNK13 K2p13.1 THIK THIK-1
KCNK15 K2p15.1 TASK[2][8] TASK-5
KCNK16 K2p16.1 TALK[2][8] TALK-1
KCNK17 K2p17.1 TALK[2][8] TALK-2, TASK-4
KCNK18 K2p18.1 TRIK, TRESK[2][8][11][12]
K2P1
UniProt
O00180
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StructuresSwiss-model
DomainsInterPro
K2P2
UniProt
O95069
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StructuresSwiss-model
DomainsInterPro
K2P3
UniProt
O14649
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StructuresSwiss-model
DomainsInterPro

See also

References

  1. ^
    S2CID 7356601
    .
  2. ^ .
  3. .
  4. .
  5. ^ Baggetta AM, Bayliss DA, Czirják G, Enyedi P, Goldstein SA, Lesage F, Minor Jr DL, Plant LD, Sepúlveda F. "Two P domain potassium channels". GtoPdb v.2023.1. IUPHAR/BPS Guide to Pharmacology. Retrieved 2019-05-28.
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External links