Close

KCNV2 Membrane Protein Introduction

Introduction of KCNV2

KCNV2, the full name of which is potassium voltage-gated channel subfamily V member 2, is encoded by the KCNV2 gene in humans. This potassium channel subunit does not form functional channels by itself. It modulates channel activity by shifting the threshold and the half-maximal activation to more negative values. Lots of researches have demonstrated that variations in KCNV2 have been reported to be associated with retinal dysfunction.

Basic Information of KCNV2
Protein Name Potassium voltage-gated channel subfamily V member 2
Gene Name KCNV2
Aliases Voltage-gated potassium channel subunit Kv8.2
Organism Homo sapiens (Human)
UniProt ID Q8TDN2
Transmembrane Times 6
Length (aa) 545
Sequence MLKQSERRRSWSYRPWNTTENEGSQHRRSICSLGARSGSQASIHGWTEGNYNYYIEEDEDGEEEDQWKDDLAEEDQQAGEVTTAKPEGPSDPPALLSTLNVNVGGHSYQLDYCELAGFPKTRLGRLATSTSRSRQLSLCDDYEEQTDEYFFDRDPAVFQLVYNFYLSGVLLVLDGLCPRRFLEELGYWGVRLKYTPRCCRICFEERRDELSERLKIQHELRAQAQVEEAEELFRDMRFYGPQRRRLWNLMEKPFSSVAAKAIGVASSTFVLVSVVALALNTVEEMQQHSGQGEGGPDLRPILEHVEMLCMGFFTLEYLLRLASTPDLRRFARSALNLVDLVAILPLYLQLLLECFTGEGHQRGQTVGSVGKVGQVLRVMRLMRIFRILKLARHSTGLRAFGFTLRQCYQQVGCLLLFIAMGIFTFSAAVYSVEHDVPSTNFTTIPHSWWWAAVSISTVGYGDMYPETHLGRFFAFLCIAFGIILNGMPISILYNKFSDYYSKLKAYEYTTIRRERGEVNFMQRARKKIAECLLGSNPQLTPRQEN

Function of KCNV2 Membrane Protein

KCNV2 is a potassium channel which is also known as Kv8.2. It belongs to electrically silent KvS subunits. The expression is restricted in testis. This potassium channel subunit does not form functional channels by itself. It can form functional heterotetrametric Kv2/KvS channels which possess unique biophysical properties and display a more tissue-specific expression pattern, making them more desirable pharmacological and therapeutic targets. It modulates channel activity by shifting the threshold and the half-maximal activation to more negative values. Common variations in KCNV2 have been reported to be associated with retinal dysfunction. The structure and function are both complicated for this channel. The various functions not only include neuronal excitability, regulating neurotransmitter release, but also include insulin secretion, heart rate, epithelial electrolyte transport, smooth muscle contraction, and cell volume. The subunit of this channel is known as a silent subunit. Furthermore, KCNV2 displays its role in function-altering effect on other K+ channel subunits.

Topological scheme of hKv8.2 Fig.1 Topological scheme of hKv8.2 (Smith, 2012)

Application of KCNV2 Membrane Protein in Literature

  1. Gayet-Primo J., et al. Heteromeric KV2/KV8.2 Channels Mediate Delayed Rectifier Potassium Currents in Primate Photoreceptors. J Neurosci. 2018, 38(14):3414-3427. PubMed ID: 29483285

    This article shows that Kv8.2 subunit interacts with different Kv2 channels to induce potassium currents with different functional properties. It also indicates that mutations in KCNV2 are the cause of retinal dysfunction in patients.

  2. Qu J., et al. Pharmacogenetic and case-control study on potassium channel related gene variants and genetic generalized epilepsy. Medicine (Baltimore). 2017, 96(26):e7321. PubMed ID: 28658141

    This article suggests that KCNA1, KCNA2, and KCNV2 variants may not be involved in the risk/drug resistance of GGEs.

  3. Smith K.E., et al. Functional analysis of missense mutations in Kv8.2 causing cone dystrophy with supernormal rod electroretinogram. J Biol Chem. 2012, 287(52):43972-83. PubMed ID: 23115240

    This study shows that two-pore mutations in KCNV2 can result in the formation of nonconducting heteromeric Kv2.1/Kv8.2 channels. The mutations prevent heteromer generation and lead to the formation of homomeric Kv2.1 channels only.

  4. Zobor D., et al. Rod and cone function in patients with KCNV2 retinopathy. PLoS One. 2012, 7(10):e46762. PubMed ID: 23077521

    This article shows that KCNV2 mutations cause a unique form of retinal disorder illustrating the importance of K(+)-channels for the resting potential, activation and deactivation of photoreceptors, while phototransduction remains unchanged.

  5. Hölter P., et al. The retinal clock drives the expression of Kcnv2, a channel essential for visual function and cone survival. Invest Ophthalmol Vis Sci. 2012, 53(11):6947-54. PubMed ID: 22969075

    This article demonstrates that the transcriptional regulation of Kcnv2 and Kv2.1 is a way through which the retinal clock system drives the functional adaptation of visual function to the marked daily changes in environmental lighting conditions.

KCNV2 Preparation Options

We provide custom membrane protein preparation services for worldwide customers. Leveraging by our advanced Magic™ membrane protein production platform, we are able to present target membrane protein in multiple active formats. Our professional scientists are happy to help you find an ideal method and make your project a success. Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-KCNV2 antibody development services.


Creative Biolabs provides high-quality membrane protein preparation service to facilitate the development of worldwide customer’s research. During the past years, we have successfully established a powerful Magic™ membrane protein platform which enables us to provide a series of membrane protein preparation services. For more detailed information, please feel free to contact us.

Reference

  1. Smith K E, et al. (2012). Functional analysis of missense mutations in Kv8.2 causing cone dystrophy with supernormal rod electroretinogram. J Biol Chem. 287(52):43972-83.

Online Inquiry

Verification code
Click image to refresh the verification code.

CONTACT US

45-1 Ramsey Road, Shirley, NY 11967, USA
Call us at:
USA: 1-631-381-2994
Europe: 44-207-097-1828
Fax: 1-631-207-8356
Email:
Our customer service representatives are available 24 hours a day, 7 days a week. Contact Us