KCNIP2

Protein-coding gene in the species Homo sapiens
KCNIP2
Identifiers
AliasesKCNIP2, KCHIP2, potassium voltage-gated channel interacting protein 2
External IDsOMIM: 604661; MGI: 2135916; HomoloGene: 23710; GeneCards: KCNIP2; OMA:KCNIP2 - orthologs
Gene location (Human)
Chromosome 10 (human)
Chr.Chromosome 10 (human)[1]
Chromosome 10 (human)
Genomic location for KCNIP2
Genomic location for KCNIP2
Band10q24.32Start101,825,974 bp[1]
End101,843,920 bp[1]
Gene location (Mouse)
Chromosome 19 (mouse)
Chr.Chromosome 19 (mouse)[2]
Chromosome 19 (mouse)
Genomic location for KCNIP2
Genomic location for KCNIP2
Band19 C3|19 38.75 cMStart45,780,278 bp[2]
End45,804,500 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • nucleus accumbens

  • caudate nucleus

  • putamen

  • left ventricle

  • amygdala

  • adipose tissue

  • abdominal fat

  • subcutaneous adipose tissue

  • prefrontal cortex

  • dorsolateral prefrontal cortex
Top expressed in
  • interventricular septum

  • olfactory tubercle

  • dentate gyrus

  • superior frontal gyrus

  • nucleus accumbens

  • myocardium of ventricle

  • globus pallidus

  • inferior colliculus

  • subiculum

  • hippocampus proper
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • calcium ion binding
  • potassium channel activity
  • ER retention sequence binding
  • transmembrane transporter binding
  • protein N-terminus binding
  • metal ion binding
  • voltage-gated ion channel activity
  • protein binding
  • A-type (transient outward) potassium channel activity
  • identical protein binding
  • voltage-gated potassium channel activity involved in cardiac muscle cell action potential repolarization
  • potassium channel regulator activity
Cellular component
  • cytoplasm
  • membrane
  • plasma membrane
  • potassium channel complex
  • voltage-gated potassium channel complex
Biological process
  • clustering of voltage-gated potassium channels
  • muscle contraction
  • regulation of heart contraction
  • regulation of ion transmembrane transport
  • ion transport
  • detection of calcium ion
  • potassium ion transport
  • membrane repolarization
  • regulation of cation channel activity
  • potassium ion transmembrane transport
  • regulation of potassium ion transmembrane transport
  • signal transduction
  • chemical synaptic transmission
  • membrane repolarization during cardiac muscle cell action potential
  • potassium ion export across plasma membrane
  • positive regulation of potassium ion export across plasma membrane
  • positive regulation of voltage-gated potassium channel activity
  • cardiac conduction
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

30819

80906

Ensembl

ENSG00000120049

ENSMUSG00000025221

UniProt

Q9NS61

Q9JJ69

RefSeq (mRNA)
NM_014591
NM_173191
NM_173192
NM_173193
NM_173194

NM_173195
NM_173197
NM_173342

NM_001276358
NM_030716
NM_145703
NM_145704

RefSeq (protein)
NP_055406
NP_775283
NP_775284
NP_775285
NP_775286

NP_775287
NP_775289

NP_001263287
NP_109641
NP_663749
NP_663750

Location (UCSC)Chr 10: 101.83 – 101.84 MbChr 19: 45.78 – 45.8 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Kv channel-interacting protein 2 also known as KChIP2 is a protein that in humans is encoded by the KCNIP2 gene.[5][6]

Function

This gene encodes a member of the family of voltage-gated potassium (Kv) channel-interacting proteins (KCNIPs, also frequently called "KChIP"), which belong to the recoverin branch of the EF-hand superfamily.[7] 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.[6]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000120049 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000025221 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ An WF, Bowlby MR, Betty M, Cao J, Ling HP, Mendoza G, Hinson JW, Mattsson KI, Strassle BW, Trimmer JS, Rhodes KJ (Feb 2000). "Modulation of A-type potassium channels by a family of calcium sensors". Nature. 403 (6769): 553–6. Bibcode:2000Natur.403..553A. doi:10.1038/35000592. PMID 10676964. S2CID 4419472.
  6. ^ a b "Entrez Gene: KCNIP2 Kv channel interacting protein 2".
  7. ^ Burgoyne RD (Mar 2007). "Neuronal calcium sensor proteins: generating diversity in neuronal Ca2+ signalling". Nature Reviews. Neuroscience. 8 (3): 182–93. doi:10.1038/nrn2093. PMC 1887812. PMID 17311005.

Further reading

  • Hartley JL, Temple GF, Brasch MA (Nov 2000). "DNA cloning using in vitro site-specific recombination". Genome Research. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
  • Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Böcher M, Blöcker H, Bauersachs S, Blum H, Lauber J, Düsterhöft A, Beyer A, Köhrer K, Strack N, Mewes HW, Ottenwälder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A (Mar 2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Research. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
  • Ohya S, Morohashi Y, Muraki K, Tomita T, Watanabe M, Iwatsubo T, Imaizumi Y (Mar 2001). "Molecular cloning and expression of the novel splice variants of K(+) channel-interacting protein 2". Biochemical and Biophysical Research Communications. 282 (1): 96–102. doi:10.1006/bbrc.2001.4558. PMID 11263977.
  • Bähring R, Dannenberg J, Peters HC, Leicher T, Pongs O, Isbrandt D (Jun 2001). "Conserved Kv4 N-terminal domain critical for effects of Kv channel-interacting protein 2.2 on channel expression and gating". The Journal of Biological Chemistry. 276 (26): 23888–94. doi:10.1074/jbc.M101320200. PMID 11287421.
  • Rosati B, Pan Z, Lypen S, Wang HS, Cohen I, Dixon JE, McKinnon D (May 2001). "Regulation of KChIP2 potassium channel beta subunit gene expression underlies the gradient of transient outward current in canine and human ventricle". The Journal of Physiology. 533 (Pt 1): 119–25. doi:10.1111/j.1469-7793.2001.0119b.x. PMC 2278594. PMID 11351020.
  • Decher N, Uyguner O, Scherer CR, Karaman B, Yüksel-Apak M, Busch AE, Steinmeyer K, Wollnik B (Nov 2001). "hKChIP2 is a functional modifier of hKv4.3 potassium channels: cloning and expression of a short hKChIP2 splice variant". Cardiovascular Research. 52 (2): 255–64. doi:10.1016/S0008-6363(01)00374-1. PMID 11684073.
  • Kuo HC, Cheng CF, Clark RB, Lin JJ, Lin JL, Hoshijima M, Nguyêñ-Trân VT, Gu Y, Ikeda Y, Chu PH, Ross J, Giles WR, Chien KR (Dec 2001). "A defect in the Kv channel-interacting protein 2 (KChIP2) gene leads to a complete loss of I(to) and confers susceptibility to ventricular tachycardia". Cell. 107 (6): 801–13. doi:10.1016/S0092-8674(01)00588-8. PMID 11747815. S2CID 18389247.
  • Deschênes I, DiSilvestre D, Juang GJ, Wu RC, An WF, Tomaselli GF (Jul 2002). "Regulation of Kv4.3 current by KChIP2 splice variants: a component of native cardiac I(to)?". Circulation. 106 (4): 423–9. doi:10.1161/01.CIR.0000025417.65658.B6. PMID 12135940.
  • Deschênes I, Tomaselli GF (Sep 2002). "Modulation of Kv4.3 current by accessory subunits". FEBS Letters. 528 (1–3): 183–8. doi:10.1016/S0014-5793(02)03296-9. PMID 12297301. S2CID 41910930.
  • Shibata R, Misonou H, Campomanes CR, Anderson AE, Schrader LA, Doliveira LC, Carroll KI, Sweatt JD, Rhodes KJ, Trimmer JS (Sep 2003). "A fundamental role for KChIPs in determining the molecular properties and trafficking of Kv4.2 potassium channels". The Journal of Biological Chemistry. 278 (38): 36445–54. doi:10.1074/jbc.M306142200. PMID 12829703.
  • Ren X, Shand SH, Takimoto K (Oct 2003). "Effective association of Kv channel-interacting proteins with Kv4 channel is mediated with their unique core peptide". The Journal of Biological Chemistry. 278 (44): 43564–70. doi:10.1074/jbc.M302337200. PMID 12928444.
  • Kim LA, Furst J, Butler MH, Xu S, Grigorieff N, Goldstein SA (Feb 2004). "Ito channels are octomeric complexes with four subunits of each Kv4.2 and K+ channel-interacting protein 2". The Journal of Biological Chemistry. 279 (7): 5549–54. doi:10.1074/jbc.M311332200. PMID 14623880.
  • Kim LA, Furst J, Gutierrez D, Butler MH, Xu S, Goldstein SA, Grigorieff N (Feb 2004). "Three-dimensional structure of I(to); Kv4.2-KChIP2 ion channels by electron microscopy at 21 Angstrom resolution". Neuron. 41 (4): 513–9. doi:10.1016/S0896-6273(04)00050-9. PMID 14980201. S2CID 18151379.
  • Lin YL, Lin SR, Wu TT, Chang LS (Jul 2004). "Evidence showing an intermolecular interaction between KChIP proteins and Taiwan cobra cardiotoxins". Biochemical and Biophysical Research Communications. 319 (3): 720–4. doi:10.1016/j.bbrc.2004.05.064. PMID 15184042.
  • Rhodes KJ, Carroll KI, Sung MA, Doliveira LC, Monaghan MM, Burke SL, Strassle BW, Buchwalder L, Menegola M, Cao J, An WF, Trimmer JS (Sep 2004). "KChIPs and Kv4 alpha subunits as integral components of A-type potassium channels in mammalian brain". The Journal of Neuroscience. 24 (36): 7903–15. doi:10.1523/JNEUROSCI.0776-04.2004. PMC 6729940. PMID 15356203.
  • Lin YL, Chen CY, Cheng CP, Chang LS (Aug 2004). "Protein-protein interactions of KChIP proteins and Kv4.2". Biochemical and Biophysical Research Communications. 321 (3): 606–10. doi:10.1016/j.bbrc.2004.07.006. PMID 15358149.

External links

  • v
  • t
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This article incorporates text from the United States National Library of Medicine, which is in the public domain.

  • v
  • t
  • e
Ligand-gated
Voltage-gated
Constitutively active
Proton-gated
Voltage-gated
Calcium-activated
Inward-rectifier
Tandem pore domain
Voltage-gated
Miscellaneous
Cl: Chloride channel
H+: Proton channel
M+: CNG cation channel
M+: TRP cation channel
H2O (+ solutes): Porin
Cytoplasm: Gap junction
By gating mechanism
Ion channel class
see also disorders