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KCNS1 Membrane Protein Introduction

Introduction of KCNS1

KCNS1, the full protein name of which is potassium voltage-gated channel subfamily S member 1, is encoded by the KCNS1 gene in humans. It is a voltage-gated potassium channel subunit and biased expressed in brain, gallbladder, and 3 other tissues. This potassium channel subunit does not form functional channels by itself, but it can form functional heteromeric channels with KCNB1 and KCNB2 to modulate the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1 and KCNB2.

Basic Information of KCNS1
Protein Name Potassium voltage-gated channel subfamily S member 1
Gene Name KCNS1
Aliases Delayed-rectifier K(+) channel alpha subunit 1, Voltage-gated potassium channel subunit Kv9.1
Organism Homo sapiens (Human)
UniProt ID Q96KK3
Transmembrane Times 6
Length (aa) 526
Sequence MLMLLVRGTHYENLRSKVVLPTPLGGRSTETFVSEFPGPDTGIRWRRSDEALRVNVGGVRRQLSARALARFPGTRLGRLQAAASEEQARRLCDDYDEAAREFYFDRHPGFFLSLLHFYRTGHLHVLDELCVFAFGQEADYWGLGENALAACCRARYLERRLTQPHAWDEDSDTPSSVDPCPDEISDVQRELARYGAARCGRLRRRLWLTMENPGYSLPSKLFSCVSISVVLASIAAMCIHSLPEYQAREAAAAVAAVAAGRSPEGVRDDPVLRRLEYFCIAWFSFEVSSRLLLAPSTRNFFCHPLNLIDIVSVLPFYLTLLAGVALGDQGGKEFGHLGKVVQVFRLMRIFRVLKLARHSTGLRSLGATLKHSYREVGILLLYLAVGVSVFSGVAYTAEKEEDVGFNTIPACWWWGTVSMTTVGYGDVVPVTVAGKLAASGCILGGILVVALPITIIFNKFSHFYRRQKALEAAVRNSNHQEFEDLLSSIDGVSEASLETSRETSQEGQSADLESQAPSEPPHPQMY

Function of KCNS1 Membrane Protein

KCNS1, it contributes to M-type current through associating with KCNQ3 to form a potassium channel. This slowly activating and deactivating potassium conductance plays a critical role in determining the subthreshold electrical excitability of neurons. It is important in the regulation of neuronal excitability. In addition, KCNS1 is associated with molecular diversity of a heterogeneous population of M-channels. They are various in kinetic and pharmacological properties, which can induce this physiologically important current. It’s insensitive to tetraethylammonium, but suppressed by barium, linopirdine and XE991. It can be activated by the anticonvulsant retigabine and niflumic acid. As the native M-channel, the potassium channel composed of KCNQ3 and KCNS1 is also suppressed by activation of the muscarinic acetylcholine receptor CHRM1. Except for these functions, KCNS1 can act as one of the first prognostic indicators of chronic pain risk. Moreover, KCNS1 in the periphery may play a functional role in ameliorating mechanical and cold pain in chronic states.

Peripheral Kcns1 deletion triggers exaggerated pain phenotypes after nerve injury. Fig.1 Peripheral Kcns1 deletion triggers exaggerated pain phenotypes after nerve injury. (Tsantoulas, 2018)

Application of KCNS1 Membrane Protein in Literature

  1. Tsantoulas C., et al. Mice lacking Kcns1 in peripheral neurons show increased basal and neuropathic pain sensitivity. Pain. 2018, 192:251-260. PubMed ID: 29697531

    This article suggests that restoring Kcns1 function in the periphery may be of some use in ameliorating mechanical and cold pain in chronic states.

  2. Hendry L., et al. KCNS1, but not GCH1, is associated with pain intensity in a black southern African population with HIV-associated sensory neuropathy: a genetic association study. J Acquir Immune Defic Syndr. 2013, 63(1):27-30. PubMed ID: 23314412

    This article shows that KCNS1 is associated with GCH1 with pain intensity in black Southern Africans with HIV-associated sensory neuropathy.

  3. Costigan M., et al. Multiple chronic pain states are associated with a common amino acid-changing allele in KCNS1. Brain. 2010, 133(9):2519-27. PubMed ID: 20724292

    This study shows the KCNS1 allele rs734784 as one of the first prognostic indicators of chronic pain risk.

  4. Stocker M., et al. Subunit assembly and domain analysis of electrically silent K+ channel alpha-subunits of the rat Kv9 subfamily. J Neurochem. 1999, 72(4):1725-34. PubMed ID: 10098883

    This article shows that specific inter-subfamily assembly between rKv3.4 with rKv9.3 or rKv9.1 is controlled by the hydrophobic core but not by the amino-terminal domain.

  5. Salinas M., et al. New modulatory alpha subunits for mammalian Shab K+ channels. J Biol Chem. 1997, 272(39):24371-9. PubMed ID: 9305895

    This article reveals that Kv9.1 and Kv9.2 are colocalized with Kv2.1 and/or Kv2.2 alpha subunits in several regions of the brain. Also, this article shows that neither Kv9.1 nor Kv9.2 have K+ channel activity by themselves, but both can modulate the activity of Kv2.1 and Kv2.2 channels by changing kinetics and levels of expression and by shifting the half-inactivation potential to more polarized values.

KCNS1 Preparation Options

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Reference

  1. Tsantoulas C, et al. (2018). Mice lacking Kcns1 in peripheral neurons show increased basal and neuropathic pain sensitivity. Pain. 192:251-260.

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