Description: potassium voltage-gated channel, subfamily F, member 1
Gene: Kcnf1     Synonyms: Kv5.1, kcnf1, kh1, ik8, kcnf

Edit - History


The gene KCNF1 encodes Kv5.1, a member of the potassium channel, voltage-gated, subfamily F. Also known as K8; kH1; KCNF; MGC33316. This gene is intronless and expressed in all tissues tested, including the heart, skeletal muscle, brain, kidney, and pancreas.

The alpha subunits Kv5.1 (IK8) - like Kv6.1 (K13), and Kv8.1 - cannot generate K+ channel activity by themselves, but modulate in a specific way the function of Kv2.1 and Kv2.2 subunits [400], [399].

Experimental data

Rat Kv5.1 gene in CHO host cell       datasheet

15 °C
25 °C
35 °C

Edit - History


26 genes have been described encoding for different Kv alpha-subunits. These are divided into subfamilies by sequence similarities: within a subfamily members share 70% of sequence identity, whereas between different subfamilies this percentage drops to 40%, reflecting the homology in the core section S1–S6 [650].

RGD ID Chromosome Position Species
631414 6 40910390-40913068 Rat
1621180 12 17178906-17183694 Mouse
735852 2 11052063-11054351 Human

Kcnf1 : potassium voltage-gated channel, subfamily F, member 1



Acc No Sequence Length Source
NM_001169104 n/A n/A NCBI
NM_201531 n/A n/A NCBI
NM_002236 n/A n/A NCBI



Accession Name Definition Evidence
GO:0016020 membrane Double layer of lipid molecules that encloses all cells, and, in eukaryotes, many organelles; may be a single or double lipid bilayer; also includes associated proteins. IEA
GO:0008076 voltage-gated potassium channel complex A protein complex that forms a transmembrane channel through which potassium ions may cross a cell membrane in response to changes in membrane potential. IEA

Edit - History



the effects of coexpression of Kv2.1 with electrically silent Kv5.1 or Kv6.1 alpha-subunits in Xenopus oocytes on channel gating. Kv5.1 coexpression alsoslowed deactivation of Kv2.1. In contrast, Kv6.1 was much less effective in speeding inactivation at intermediate potentials, had a slowing effect on inactivation at strong depolarizations, and had no effect on cumulative inactivation



Edit - History



kH1 and IK8 are completely identical in S3, S4, S5, S6 and H5 domains. This probably underlines the importance of the core region for K/ channel function and it associ- ated properties. At the N-terminal tail, IK8 is 12 amino acid longer than kH1. At the beginning of 5'end, kH1 is followed by a 6 amino acid sequence which is mismatched. At the C-terminal cytoplasmic tail, kH1 and IK8 are distinguished by one gap and ten amino acids which are mismatched [1698]



Edit - History


Expression of Kv5.1

kH1 was expressed abundantly in tissues examined, including the heart, skeletal muscle, and less abundant in the brain, liver, kidney, and pancreas [1698]

Northern blot analysis revealed that KH1 was expressed as a 5-kb mRNA in all tissues tested, with the highest levels in heart. A 2.4-kb transcript was detected only in brain (

UBSM and mouse brain tissue

T-PCR for voltage-gated K+ channel (KV) subunits revealed the expression of Kv2.1, Kv5.1, Kv6.1, Kv6.2 and Kv6.3 in isolated urinary bladder smooth muscle myocytes as well as mouse brain. A comparison of the biophysical properties of UBSM IK(V) with those reported for Kv2.1 and Kv5.1 and/or Kv6 heteromultimeric channels demonstrated a marked similarity. We propose that heteromultimeric channel complexes composed of Kv2.1 and Kv5.1 and/or Kv6 subunits form the molecular basis of the mouse UBSM IK(V) [1699]

Edit - History


Kv5.1 coexpression slowed deactivation of Kv2.1, accelerated the rate of inactivation of Kv2.1 at intermediate potentials (-30 to 0 mV), without affecting the rate at strong depolarization (0 to 40 mV), and markedly accelerated the rate of cumulative inactivation evoked by high-frequency trains of short pulses.[400], [398]

KV5.1 has no function on its own, but has important modulatory actions on KV2 channels [399]

Edit - History


Kinetic interaction of Kv5.1 and Kv2

Kv5.1 kin

Kv5 and Kv6 are members of the electrically silent families that are capable of evoking a large negative shift in the steady-state inactivation of Kv2.1- and Kv2.2-containing channels. The half-maximal steady-state inactivation values reported for these heteromultimeric channels are consistent with the value of −61 mV reported here for the UBSM IK(V). Steady-state activation of the UBSM IK(V) demonstrates a half-maximal value of 1.1 mV, which is mid-range of that reported for Kv2.1 (between 10 mV and −1.7 mV), is more negative than Kv2.1/Kv5.1 (18 mV) and is more positive than Kv2.1/Kv6.1 (-9.4 mV). It seems possible that the half-maximal steady-state activation value of a given heteromultimeric channel will be dependent on the stoichiometry of Kv2.1, Kv5.1 and Kv6.1 channel subunits [1699]






. et al. Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.
Proc. Natl. Acad. Sci. U.S.A., 2002 Dec 24 , 99 (16899-903).


Lazdunski M. et al. New modulatory alpha subunits for mammalian Shab K+ channels.
J. Biol. Chem., 1997 Sep 26 , 272 (24371-9).


Pongs O. et al. Molecular biology of voltage-dependent potassium channels.
Physiol. Rev., 1992 Oct , 72 (S69-88).

Su K. et al. Isolation, characterization, and mapping of two human potassium channels.
Biochem. Biophys. Res. Commun., 1997 Dec 29 , 241 (675-81).

Nelson MT. et al. Properties and molecular basis of the mouse urinary bladder voltage-gated K+ current.
J. Physiol. (Lond.), 2003 May 15 , 549 (65-74).


Contributors: Rajnish Ranjan, Michael Schartner, Nitin Khanna

To cite this page: [Contributors] Channelpedia, accessed on [date]