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potassium voltage-gated channel, subfamily G, member 1
Kcng1 : potassium voltage-gated channel, subfamily G, member 1
The sparsely populated Kv channel subfamilies Kv5 and Kv6 each contain one member, Kv5.1 and Kv6.1 (see Chandy, K.G. and Gutman, G.A. (1995) In: (R.A. North, ed.), Handbook of Receptors and Channels. Ligand- and Voltage- Gated Ion Channels. CRC Press, Ann Arbor, MI, pp. 1-71) referred to as IK8 and K13, . No function has yet been demonstrated for either of these proteins alone . Comparisons of predicted amino acid sequences strongly indicate that both Kv5.1 and Kv6.1 are members of the Kv family , exhibiting hallmarks such as the conserved GYGD sequence in H5 , six hydrophobic transmembrane domains including the positively charged S4 ,, and amino terminal Tl  or NA and Nn , domains.
EXPRESSION OF KV6.1
Unlike kH1, 2.4 kb of kH2 was expressed predominantly in the brain, placenta, and the skeletal muscle where it shared a differently spliced form of the kH2 mRNA, approximately 2.0 kb 
Expression in heart
All three known members of the Kv4 family are expressed in the ferret heart, with Kv4.2 being the most abundant (P≤.01). The transcript of Kv5.1 was most common in the right atrium (46.4%) and rarest in the atrial septum (21.5%). Kv6.1 was less abundant. It was present in 28.4% of SA nodal cells and in <16% of cells in the other anatomic regions 
Kv6.1 regulates the kinetics of Kv2.2 channels: It was much less effective in speeding inactivation at intermediate potentials than Kv5.1, had a slowing effect on inactivation at strong depolarizations, and had no effect on cumulative inactivation. Kv6.1 had profound effects on activation, including a negative shift of the steadystate activation curve and marked slowing of deactivation tail currents. 
Regulation of gating by electrically silent alpha-subunits, such as Kv6.1, is not restricted to the Kv2 subfamily. They interact with members of the Shal  and Kv3 (Shaw)  subfamilies as well.
Amino terminal portions of Kv6.1 were unable to form homomultimers but interacted specifically with amino termini of Kv2.1. Xenopus oocytes co-injected with Kv6.1 and Kv2.1 cRNAs exhibited a novel current with decreased rates of deactivation, decreased sensitivity to TEA block, and a hyperpolarizing shift of the half maximal activation potential when compared to Kv2.1. Our results indicate that Kv channel subfamilies can form heteromultimeric channels and, for the first time, suggest a possible functional role for the Kv6 subfamily.
KV6.1 Kinetics with Kv2
We previously showed that coexpression of Kv2.1 and Kv6.1 resulted in currents that deactivated extremely slowly upon depolarization 
Human Kv6.1/ Kv6.3/ Kv6.4 Expressed with human Kv2.1 in CHO-K1 Cells
Currents were measured using whole cells patch clamp techniques. The cells were superfused with symmetrical high K+ solutions and depolarizing voltage steps were applied from the holding potential of -80 mV to potentials between -70 and +40 mV (10 mV increments)
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Contributors : Rajnish Ranjan, Michael Schartner
To cite : [Editor], [Contributors]. Accessed on [Date] Channelpedia , http://channelpedia.epfl.ch/ionchannels/19