Aliases for KCNT2 Gene
- Potassium Channel, Sodium Activated Subfamily T, Member 2 2 3
- SLICK 3 4 6
- Sodium And Chloride-Activated ATP-Sensitive Potassium Channel Slo2.1 3 4
- Sequence Like An Intermediate Conductance Potassium Channel Subunit 3 4
- Potassium Channel, Subfamily T, Member 2 2 3
- Sodium-And Chloride-Activated ATP-Sensitive Potassium Channel (SLICK) 3
External Ids for KCNT2 Gene
GeneCards Summary for KCNT2 Gene
KCNT2 (Potassium Channel, Sodium Activated Subfamily T, Member 2) is a Protein Coding gene. Among its related pathways are Activation of cAMP-Dependent PKA and Activation of cAMP-Dependent PKA. GO annotations related to this gene include voltage-gated potassium channel activity and calcium-activated potassium channel activity. An important paralog of this gene is KCNU1.
UniProtKB/Swiss-Prot for KCNT2 Gene
Outward rectifying potassium channel. Produces rapidly activating outward rectifier K(+) currents. Activated by high intracellular sodium and chloride levels. Channel activity is inhibited by ATP and by inhalation anesthetics, such as isoflurane (By similarity). Inhibited upon stimulation of G-protein coupled receptors, such as CHRM1 and GRIA1.
Ca2+-activated potassium channels (KCa) are a group of 6/7-TM ion channels that selectively transport K+ ions across biological membranes. They are broadly classified into three subtypes, SK, IK and BK channels, based on their conductance (small, intermediate and big conductance respectively). The small conductance KCa channels (KCa2.1, 2.2 and 2.3, also known as SK1, SK2 and SK3 respectively) and the intermediate conductance KCa channel (KCa3.1, also known as SK4) are voltage-insensitive and are activated by Ca2+-calmodulin. Both play important roles in many processes involving Ca2+-dependent signalling in both electrically excitable and non-excitable cells. The BK family of KCa channels (also known as Slo or Maxi-K channels) are also voltage-sensitive and include KCa1.1 (Slo1), KCa4.1 (Slo2.2), KCa4.2 (Slo2.1) and KCa5.1 (Slo3). These channels do not require calmodulin for activation as they contain three direct bivalent cation binding sites.