KCND2

Protein-coding gene in the species Homo sapiens
KCND2
Identifiers
AliasesKCND2, KV4.2, RK5, potassium voltage-gated channel subfamily D member 2
External IDsOMIM: 605410; MGI: 102663; HomoloGene: 40828; GeneCards: KCND2; OMA:KCND2 - orthologs
Gene location (Human)
Chromosome 7 (human)
Chr.Chromosome 7 (human)[1]
Chromosome 7 (human)
Genomic location for KCND2
Genomic location for KCND2
Band7q31.31Start120,273,175 bp[1]
End120,750,337 bp[1]
Gene location (Mouse)
Chromosome 6 (mouse)
Chr.Chromosome 6 (mouse)[2]
Chromosome 6 (mouse)
Genomic location for KCND2
Genomic location for KCND2
Band6 A2- A3.1|6 8.49 cMStart21,215,502 bp[2]
End21,729,804 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • cerebellar vermis

  • pons

  • stromal cell of endometrium

  • Brodmann area 23

  • prefrontal cortex

  • ganglionic eminence

  • Region I of hippocampus proper

  • endothelial cell

  • caudate nucleus

  • dorsolateral prefrontal cortex
Top expressed in
  • habenula

  • cerebellar vermis

  • toe

  • medial geniculate nucleus

  • medial dorsal nucleus

  • third toe

  • olfactory tubercle

  • nucleus accumbens

  • lateral geniculate nucleus

  • globus pallidus
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • potassium channel activity
  • metal ion binding
  • voltage-gated ion channel activity
  • ion channel activity
  • protein binding
  • A-type (transient outward) potassium channel activity
  • voltage-gated potassium channel activity
  • voltage-gated ion channel activity involved in regulation of postsynaptic membrane potential
Cellular component
  • integral component of membrane
  • perikaryon
  • postsynaptic membrane
  • cell projection
  • membrane
  • plasma membrane raft
  • intrinsic component of plasma membrane
  • voltage-gated potassium channel complex
  • plasma membrane
  • dendritic spine
  • synapse
  • integral component of plasma membrane
  • neuronal cell body membrane
  • cell junction
  • neuronal cell body
  • dendrite
  • glutamatergic synapse
  • GABA-ergic synapse
  • integral component of postsynaptic membrane
  • integral component of postsynaptic specialization membrane
  • postsynaptic density
Biological process
  • chemical synaptic transmission
  • regulation of ion transmembrane transport
  • ion transport
  • potassium ion transport
  • transmembrane transport
  • potassium ion transmembrane transport
  • action potential
  • sensory perception of pain
  • protein homooligomerization
  • cellular response to hypoxia
  • neuronal action potential
  • locomotor rhythm
  • regulation of postsynaptic membrane potential
  • cardiac conduction
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

3751

16508

Ensembl

ENSG00000184408

ENSMUSG00000060882

UniProt

Q9NZV8

Q9Z0V2

RefSeq (mRNA)

NM_012281

NM_019697

RefSeq (protein)

NP_036413

NP_062671

Location (UCSC)Chr 7: 120.27 – 120.75 MbChr 6: 21.22 – 21.73 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Potassium voltage-gated channel subfamily D member 2 is a protein that in humans is encoded by the KCND2 gene.[5][6][7] It contributes to the cardiac transient outward potassium current (Ito1), the main contributing current to the repolarizing phase 1 of the cardiac action potential.[8]

Description

Voltage-gated potassium (Kv) channels represent the most complex class of voltage-gated ion channels from both functional and structural standpoints. Their diverse functions include regulating neurotransmitter release, heart rate, insulin secretion, neuronal excitability, epithelial electrolyte transport, smooth muscle contraction, and cell volume. Four sequence-related potassium channel genes - shaker, shaw, shab, and shal - have been identified in Drosophila, and each has been shown to have human homolog(s). This gene encodes a member of the potassium channel, voltage-gated, shal-related subfamily, members of which form voltage-activated A-type potassium ion channels and are prominent in the repolarization phase of the action potential. This member mediates a rapidly inactivating, A-type outward potassium current which is not under the control of the N terminus as it is in Shaker channels.[7]

Interactions

KCND2 has been shown to interact with FLNC.[9]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000184408 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000060882 – 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. ^ Zhu XR, Wulf A, Schwarz M, Isbrandt D, Pongs O (December 1999). "Characterization of human Kv4.2 mediating a rapidly-inactivating transient voltage-sensitive K+ current". Receptors Channels. 6 (5): 387–400. PMID 10551270.
  6. ^ Gutman GA, Chandy KG, Grissmer S, Lazdunski M, McKinnon D, Pardo LA, Robertson GA, Rudy B, Sanguinetti MC, Stuhmer W, Wang X (December 2005). "International Union of Pharmacology. LIII. Nomenclature and molecular relationships of voltage-gated potassium channels". Pharmacol Rev. 57 (4): 473–508. doi:10.1124/pr.57.4.10. PMID 16382104. S2CID 219195192.
  7. ^ a b "Entrez Gene: KCND2 potassium voltage-gated channel, Shal-related subfamily, member 2".
  8. ^ Oudit GY, Kassiri Z, Sah R, Ramirez RJ, Zobel C, Backx PH (May 2001). "The molecular physiology of the cardiac transient outward potassium current (I(to)) in normal and diseased myocardium". J. Mol. Cell. Cardiol. 33 (5): 851–872. doi:10.1006/jmcc.2001.1376. PMID 11343410. S2CID 829154.
  9. ^ Petrecca, K; Miller D M; Shrier A (December 2000). "Localization and enhanced current density of the Kv4.2 potassium channel by interaction with the actin-binding protein filamin". J. Neurosci. 20 (23): 8736–44. doi:10.1523/JNEUROSCI.20-23-08736.2000. PMC 6773047. PMID 11102480.

Further reading

  • Kong W, Po S, Yamagishi T, et al. (1999). "Isolation and characterization of the human gene encoding Ito: further diversity by alternative mRNA splicing". Am. J. Physiol. 275 (6 Pt 2): H1963–70. doi:10.1152/ajpheart.1998.275.6.H1963. PMID 9843794.
  • Kikuno R, Nagase T, Ishikawa K, et al. (1999). "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 6 (3): 197–205. doi:10.1093/dnares/6.3.197. PMID 10470851.
  • Kurschner C, Yuzaki M (1999). "Neuronal interleukin-16 (NIL-16): a dual function PDZ domain protein". J. Neurosci. 19 (18): 7770–80. doi:10.1523/JNEUROSCI.19-18-07770.1999. PMC 6782450. PMID 10479680.
  • An WF, Bowlby MR, Betty M, et al. (2000). "Modulation of A-type potassium channels by a family of calcium sensors". Nature. 403 (6769): 553–556. Bibcode:2000Natur.403..553A. doi:10.1038/35000592. PMID 10676964. S2CID 4419472.
  • Isbrandt D, Leicher T, Waldschütz R, et al. (2000). "Gene structures and expression profiles of three human KCND (Kv4) potassium channels mediating A-type currents I(TO) and I(SA)". Genomics. 64 (2): 144–154. doi:10.1006/geno.2000.6117. PMID 10729221. S2CID 1429910.
  • Postma AV, Bezzina CR, de Vries JF, et al. (2000). "Genomic organisation and chromosomal localisation of two members of the KCND ion channel family, KCND2 and KCND3". Hum. Genet. 106 (6): 614–619. doi:10.1007/s004390050033. PMID 10942109.
  • Petrecca K, Miller DM, Shrier A (2001). "Localization and enhanced current density of the Kv4.2 potassium channel by interaction with the actin-binding protein filamin". J. Neurosci. 20 (23): 8736–44. doi:10.1523/JNEUROSCI.20-23-08736.2000. PMC 6773047. PMID 11102480.
  • Bähring R, Dannenberg J, Peters HC, et al. (2001). "Conserved Kv4 N-terminal domain critical for effects of Kv channel-interacting protein 2.2 on channel expression and gating". J. Biol. Chem. 276 (26): 23888–23894. doi:10.1074/jbc.M101320200. PMID 11287421.
  • Nakamura TY, Pountney DJ, Ozaita A, et al. (2001). "A role for frequenin, a Ca2+-binding protein, as a regulator of Kv4 K+-currents". Proc. Natl. Acad. Sci. U.S.A. 98 (22): 12808–12813. Bibcode:2001PNAS...9812808N. doi:10.1073/pnas.221168498. PMC 60135. PMID 11606724.
  • Morohashi Y, Hatano N, Ohya S, et al. (2002). "Molecular cloning and characterization of CALP/KChIP4, a novel EF-hand protein interacting with presenilin 2 and voltage-gated potassium channel subunit Kv4". J. Biol. Chem. 277 (17): 14965–14975. doi:10.1074/jbc.M200897200. PMID 11847232.
  • Eldstrom J, Doerksen KW, Steele DF, Fedida D (2002). "N-terminal PDZ-binding domain in Kv1 potassium channels". FEBS Lett. 531 (3): 529–537. doi:10.1016/S0014-5793(02)03572-X. PMID 12435606. S2CID 40689829.
  • Schrader LA, Anderson AE, Mayne A, et al. (2002). "PKA modulation of Kv4.2-encoded A-type potassium channels requires formation of a supramolecular complex". J. Neurosci. 22 (23): 10123–33. doi:10.1523/JNEUROSCI.22-23-10123.2002. PMC 6758737. PMID 12451113.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–16903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Shin BK, Wang H, Yim AM, et al. (2003). "Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function". J. Biol. Chem. 278 (9): 7607–7616. doi:10.1074/jbc.M210455200. PMID 12493773.
  • Scherer SW, Cheung J, MacDonald JR, et al. (2003). "Human chromosome 7: DNA sequence and biology". Science. 300 (5620): 767–772. Bibcode:2003Sci...300..767S. doi:10.1126/science.1083423. PMC 2882961. PMID 12690205.
  • Hillier LW, Fulton RS, Fulton LA, et al. (2003). "The DNA sequence of human chromosome 7". Nature. 424 (6945): 157–164. Bibcode:2003Natur.424..157H. doi:10.1038/nature01782. PMID 12853948.
  • Wong W, Schlichter LC (2004). "Differential recruitment of Kv1.4 and Kv4.2 to lipid rafts by PSD-95". J. Biol. Chem. 279 (1): 444–452. doi:10.1074/jbc.M304675200. PMID 14559911.
  • Kim LA, Furst J, Butler MH, et al. (2004). "Ito channels are octomeric complexes with four subunits of each Kv4.2 and K+ channel-interacting protein 2". J. Biol. Chem. 279 (7): 5549–5554. doi:10.1074/jbc.M311332200. PMID 14623880.

External links

  • v
  • t
  • e
  • 1nn7: Crystal Structure Of The Tetramerization Domain Of The Shal Voltage-Gated Potassium Channel
    1nn7: Crystal Structure Of The Tetramerization Domain Of The Shal Voltage-Gated Potassium Channel
  • 1s6c: Crystal structure of the complex between KChIP1 and Kv4.2 N1-30
    1s6c: Crystal structure of the complex between KChIP1 and Kv4.2 N1-30
  • 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

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