KCNN1 Membrane Protein Introduction

Introduction of KCNN1

Small conductance calcium-activated potassium channel protein 1, also known as KCNN1, is encoded by the gene KCNN1,which is mapped to the chromosome 19p13.1. KCNN1 is a member of the KCNN family of potassium channels. As an integral membrane protein, KCNN1 contains 6 putative transmembrane domains and pore region. It also forms a voltage-independent calcium-activated channel with three other calmodulin-binding subunits.

Basic Information of KCNN1
Protein Name	Small conductance calcium-activated potassium channel protein 1
Gene Name	KCNN1
Aliases	KCa2.1, SK1, SKCa 1, SKCa1
Organism	Homo sapiens (Human)
UniProt ID	Q92952
Transmembrane Times	6
Length (aa)	543
Sequence	MNSHSYNGSVGRPLGSGPGALGRDPPDPEAGHPPQPPHSPGLQVVVAKSEPARPSPGSPRGQPQDQDDDEDDEEDEAGRQRASGKPSNVGHRLGHRRALFEKRKRLSDYALIFGMFGIVVMVTETELSWGVYTKESLYSFALKCLISLSTAILLGLVVLYHAREIQLFMVDNGADDWRIAMTCERVFLISLELAVCAIHPVPGHYRFTWTARLAFTYAPSVAEADVDVLLSIPMFLRLYLLGRVMLLHSKIFTDASSRSIGALNKITFNTRFVMKTLMTICPGTVLLVFSISSWIIAAWTVRVCERYHDKQEVTSNFLGAMWLISITFLSIGYGDMVPHTYCGKGVCLLTGIMGAGCTALVVAVVARKLELTKAEKHVHNFMMDTQLTKRVKNAAANVLRETWLIYKHTRLVKKPDQARVRKHQRKFLQAIHQAQKLRSVKIEQGKLNDQANTLTDLAKTQTVMYDLVSELHAQHEELEARLATLESRLDALGASLQALPGLIAQAIRPPPPPLPPRPGPGPQDQAARSSPCRWTPVAPSDCG

Function of KCNN1 Membrane Protein

The basic function of KCNN1 is regarded as a voltage-independent potassium channel which is activated by intracellular calcium. It is activated by an afterhyperpolarization (AHP) and regulates neuronal excitability by contributing to the slow component of synaptic AHP. Activation of KCNN1 is usually followed by membrane hyperpolarization. KCNN1 is also important regulators of many biological processes, including chemical synaptic transmission and potassium ion transport. In recent studies, KCNN1 is shown to play an important role in the pathophysiology of pain following nerve injury. It is reported to be blocked by apamin.

Fig.1 Mitochondrial K⁺ cycle. (Charles, 2017)

Application of KCNN1 Membrane Protein in Literature

Shmukler B.E., et al. Structure and complex transcription pattern of the mouse SK1 K(Ca) channel gene, KCNN1. Biochim Biophys Acta. 2001, 1518(1-2): 36-46. PubMed ID: 11267657

In this article, the authors suggest a possible role in the tuning of SK1 channel function via the evolutionary conservation of this complex transcription pattern.
Litt M., et al. Gene structure and chromosome mapping of the human small-conductance calcium-activated potassium channel SK1 gene (KCNN1). Cytogenet Cell Genet. 1999, 86(1): 70-3. PubMed ID: 10516439

This article figures out the gene structure of KCNN1 and its localization by the method of radiation hybrid mapping to chromosome 19p13.1.
Thompson C.R., et al. Sphingosine kinase 1 (SK1) is recruited to nascent phagosomes in human macrophages: inhibition of SK1 translocation by Mycobacterium tuberculosis. J Immunol. 2005, 174(6): 3551-61. PubMed ID: 15749892

The results in this article are agreed with a model in which Mtb inhibits both the activation and phagosomal translocation of SK1 and in further blocks the localized Ca²⁺ transients required for phagosome maturation.
Choi H.S., et al. A novel flavin-containing monooxygenase from Methylophaga sp strain SK1 and its indigo synthesis in Escherichia coli. Biochem Biophys Res Commun. 2003, 306(4): 930-6. PubMed ID: 12821131

This article suggests that the recombinant strain has the potential to be applied in microbial indigo production.
Boettger M.K., et al. Calcium-activated potassium channel SK1- and IK1-like immunoreactivity in injured human sensory neurons and its regulation by neurotrophic factors. Brain. 2002, 125(Pt 2): 252-63. PubMed ID: 11844726

In this article, they find that decreased retrograde transport of neurotrophic factors in injured sensory neurons may thus reduce expression of ion channels and increase excitability. Selective potassium channel openers are likely to represent novel therapies for pain following nerve injury.

KCNN1 Preparation Options

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Reference

Charles Owen Smith, et al. (2017). The Slo(w) path to identifying the mitochondrial channels responsible for ischemic protection. Biochem J. 474(12): 2067-2094.

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