KChIP1

Description: Kv channel-interacting protein 1
Gene: kcnip1
Alias: kchip1, kcnip1

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Introduction

KCNIP1 (also known as VABP; MGC95; KCHIP1) encodes a member of the family of voltage-gated potassium (Kv) channel-interacting proteins (KCNIPs), which belong to the recoverin branch of the EF-hand superfamily. Members of the KCNIP family are small calcium binding proteins. They all have EF-hand-like domains, and differ from each other in the N-terminus. They are integral subunit components of native Kv4 channel complexes. They may regulate A-type currents, and hence neuronal excitability, in response to changes in intracellular calcium. Alternative splicing results in multiple transcript variant encoding different isoforms.

http://www.ncbi.nlm.nih.gov/gene/30820

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Gene

Species	NCBI gene ID	Chromosome	Position
Human	30820	5	383145
Mouse	70357	11	364515
Rat	65023	10	369314

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Transcript

Species	NCBI accession	Length (nt)
Human	NM_001034837.3	2063
Mouse	NM_001190885.2	2392
Rat	NM_001261387.1	1653

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Protein Isoforms

Species	Uniprot ID	Length (aa)
Human	Q9NZI2	227
Mouse	Q9JJ57	227
Rat	Q8R426	227

Isoforms

Transcript

Length (nt)

Protein

Length (aa)

Variant

Isoform

Known

NM_001034838.3

1894

NP_001030010.1

225

transcript variant 3

isoform 3

NM_001278340.2

2192

NP_001265269.1

188

transcript variant 4

isoform 4

NM_001034837.3

2063

NP_001030009.1

227

transcript variant 1

isoform 1

NM_001278339.2

2105

NP_001265268.1

241

transcript variant 5

isoform 5

NM_014592.4

2030

NP_055407.1

216

transcript variant 2

isoform 2

Predicted

XM_017009407.2

1732

XP_016864896.1

225

transcript variant X1

isoform X1

XM_017009408.2

1902

XP_016864897.1

137

transcript variant X2

isoform X2

XM_054352477.1

1869

XP_054208452.1

225

transcript variant X1

isoform X1

XM_054352478.1

1902

XP_054208453.1

137

transcript variant X2

isoform X2

Known

NM_001190886.1

2247

NP_001177815.1

225

transcript variant C

isoform C

NM_027398.4

2359

NP_081674.2

216

transcript variant B

isoform B

NM_001290690.2

2547

NP_001277619.1

188

transcript variant D

isoform D

NM_001190885.2

2392

NP_001177814.1

227

transcript variant A

isoform A

NM_001363115.1

2022

NP_001350044.1

245

transcript variant E

isoform E

Predicted

XM_017314753.3

2479

XP_017170242.1

229

transcript variant X3

isoform X3

XM_036156977.1

2242

XP_036012870.1

188

transcript variant X10

isoform X6

XM_036156976.1

1707

XP_036012869.1

188

transcript variant X7

isoform X6

XM_017314754.2

1925

XP_017170243.1

220

transcript variant X4

isoform X4

XM_017314752.2

1958

XP_017170241.1

231

transcript variant X2

isoform X2

XM_030246299.1

1945

XP_030102159.1

188

transcript variant X8

isoform X6

XM_030246297.1

1978

XP_030102157.1

188

transcript variant X6

isoform X6

XM_017314755.3

2061

XP_017170244.1

192

transcript variant X5

isoform X5

XM_030246298.2

2078

XP_030102158.1

188

transcript variant X9

isoform X6

XM_017314751.3

1619

XP_017170240.1

249

transcript variant X1

isoform X1

XM_036156978.1

1440

XP_036012871.1

188

transcript variant X11

isoform X6

Known

NM_001261388.1

1620

NP_001248317.1

225

transcript variant 2

isoform 2

NM_001261387.1

1653

NP_001248316.1

236

transcript variant 1

isoform 1

NM_022929.2

1456

NP_075218.2

216

transcript variant 4

isoform 4

NM_001261389.1

1489

NP_001248318.1

227

transcript variant 3

isoform 3

Predicted

XM_006246105.4

3456

XP_006246167.1

245

transcript variant X1

isoform X1

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Post-Translational Modifications

PTM

Position

Type

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Structure

The KCNIPs differ from other proteins in the family of neuronal calcium binding proteins because they contain a variable N-terminal sequence that shares no homology with other calcium-binding protein domains (reviewed in Borgoyne [1196]). The N-termini among the KCNIPs themselves are also unique and share no homology (An [1195]).

KChIP1 predicted AlphaFold size

Species	Area (Å²)	Reference
Human	1965.84	source
Mouse	1758.65	source
Rat	1781.09	source

Methodology for AlphaFold size prediction and disclaimer are available here

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Kinetics

KChIPs slow rapid inactivation and accelerate recovery from inactivation. (Beck [25])

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Expression and Distribution

KChIP1 is predominantly expressed in brain (An [1195]).

In the septum, lateral septal nuclei showed moderate and high signal for KCNIP1. KCNIP1 was expressed at high levels, in the reticular thalamic nuclei and medial habenular nuclei and were not expressed in most of the other thalamic nuclei. The olfactory system KCNIP1 was highly expressed in the granular layer. KCNIP1 mRNA was detected in the scattered neurons, most possibly interneurons, of all layers of the cerebral cortex. KCNIP1 was expressed at high levels in scattered neurons that are most likely interneurons, around the CA regions, the dentate gyrus, and the molecular layer. From fig 4 in Pruunsild [1194]

All three KChIPs co-localize and co-immunoprecipitate with brain Kv4 a-subunits, and are thus integral components of native Kv4 channel complexes. (An [1195])

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Function

KChIPs (Kv-Channel-Interacting-Proteins) (An et al. 2000 [1195]) are related to known calcium-binding proteins, including frequenin, recoverin and calsenilin-DREAM (a transcriptional factor) (Pawlowski et al. 1996). KChIP1, KChIP2 and KChIP3 interact specifically with Kv4 channels in situ, upregulate current expression and modulate various aspects of inactivation gating (An et al. 2000 [1195]; Bähring et al. 2001b [1197]).

Inactivation of Kv4.1 and Kv4.3 channels expressed in Xenopus oocytes appears to happen by distinct methods when expressed alone, but when coexpressed with KChIP1, Kv4.1 and Kv4.3 currents are nearly indistinguishable. (Beck [25])

KChIP1 slows fast inactivation of Kv4.1 and Kv4.3 from the open state and facilitates closed-state inactivation. Additionally, KChIP1 favours inactivation from the preopen closed state by accelerating channel closing. (Beck [25])

References

Beck EJ et al. Remodelling inactivation gating of Kv4 channels by KChIP1, a small-molecular-weight calcium-binding protein.
J. Physiol. (Lond.), 2002 Feb 1 , 538 (691-706).

126

Van Hoorick D et al. Differential modulation of Kv4 kinetics by KCHIP1 splice variants.
Mol. Cell. Neurosci., 2003 Oct , 24 (357-66).

1191

Bourdeau ML et al. KChIP1 modulation of Kv4.3-mediated A-type K(+) currents and repetitive firing in hippocampal interneurons.
Neuroscience, 2011 Mar 10 , 176 (173-87).

1192

Liao YS et al. Functional role of EF-hands 3 and 4 in membrane-binding of KChIP1.
J. Biosci., 2009 Jun , 34 (203-11).

1193

Pioletti M et al. Three-dimensional structure of the KChIP1-Kv4.3 T1 complex reveals a cross-shaped octamer.
Nat. Struct. Mol. Biol., 2006 Nov , 13 (987-95).

1194

Pruunsild P et al. Structure, alternative splicing, and expression of the human and mouse KCNIP gene family.
Genomics, 2005 Nov , 86 (581-93).

1195

An WF et al. Modulation of A-type potassium channels by a family of calcium sensors.
Nature, 2000 Feb 3 , 403 (553-6).

1196

Burgoyne RD et al. The neuronal calcium sensor family of Ca2+-binding proteins.
Biochem. J., 2001 Jan 1 , 353 (1-12).

1197

Bähring R et al. Conserved Kv4 N-terminal domain critical for effects of Kv channel-interacting protein 2.2 on channel expression and gating.
J. Biol. Chem., 2001 Jun 29 , 276 (23888-94).

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Credits

To cite this page: [Contributors] Channelpedia https://channelpedia.epfl.ch/wikipages/76/ , accessed on 2024 Apr 25

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