Channelpedia

Kv5.1

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

Edit - History

Introduction

Kv5.1 (also known as K8; kH1; KCNF; MGC33316), encoded by the gene KCNF1, is a member of the voltage-gated, subfamily F. Kv5.1 channels cannot generate K+ channel activity by themselves, but modulate in a specific way the function of Kv2.1 and Kv2.2 subunits [400], [399]. NCBI


Experimental data

Edit - History

Gene

KCNF1 is intronless and expressed in all tissues tested, including the heart, skeletal muscle, brain, kidney, and pancreas. NCBI

Species NCBI gene ID Chromosome Position
Human 3754 2 2291
Mouse 382571 12 4788
Rat 298908 6 2678

Edit

Transcript

Species NCBI accession Length (nt)
Human NM_002236.5 2292
Mouse NM_201531.4 4789
Rat NM_001169104.1 2679

Edit

Protein Isoforms

Species Uniprot ID Length (aa)
Human Q9H3M0 494
Mouse Q7TSH7 493
Rat D4ADX7 505

Isoforms

Transcript
Length (nt)
Protein
Length (aa)
Variant
Isoform

Edit

Post-Translational Modifications

PTM
Position
Type

Edit - History

Structure

Kv5.1
Visual Representation of Kv5.1 Structure
Methodology for visual representation of structure available here

STRUCTURE AND COMPARISON OF HUMAN AND RAT KV5.1

kH1 and Kv5.1 (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 associated 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]

Kv5.1 predicted AlphaFold size

Species Area (Å2) Reference
Human 3969.18 source
Mouse 3203.21 source
Rat 3354.59 source

Methodology for AlphaFold size prediction and disclaimer are available here


Edit - History

Kinetics

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]


Edit - History

Expression and Distribution

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 (omim.org)

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

Function

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


Edit - History

Interaction

Kv2.1

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]

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


References

312

400

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

607

Strausberg RL 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).

648

649

650

Pongs O 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).

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


Edit - History

Credits

Contributors: Rajnish Ranjan, Michael Schartner, Nitin Khanna, Katherine Johnston

To cite this page: [Contributors] Channelpedia https://channelpedia.epfl.ch/wikipages/18/ , accessed on 2024 Dec 30



Add section