KCNJ6

From Wikipedia, the free encyclopedia

Potassium inwardly-rectifying channel, subfamily J, member 6

Identifiers

KCNJ6; BIR1; GIRK2; KATP2; KCNJ7; KIR3.2; MGC126596; hiGIRK2

External IDs

OMIM: 600877 MGI: 104781 HomoloGene: 1688

Gene ontology
Molecular Function:	• voltage-gated ion channel activity • G-protein activated inward rectifier potassium channel activity • potassium ion binding
Cellular Component:	• voltage-gated potassium channel complex • membrane • integral to membrane
Biological Process:	• ion transport • potassium ion transport

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002240 (mRNA)
NP_002231 (protein)

NM_001025584 (mRNA)
NP_001020755 (protein)

Location

Chr 21: 37.92 - 38.02 Mb

Chr 16: 94.87 - 95.11 Mb

Pubmed search

[1]

[2]

Potassium inwardly-rectifying channel, subfamily J, member 6, also known as KCNJ6 or K_ir3.2, is a human gene.^[1]

Potassium channels are present in most mammalian cells, where they participate in a wide range of physiologic responses. The protein encoded by this gene is an integral membrane protein and inward-rectifier type potassium channel. The encoded protein, which has a greater tendency to allow potassium to flow into a cell rather than out of a cell, is controlled by G-proteins and may be involved in the regulation of insulin secretion by glucose. It associates with two other G-protein-activated potassium channels to form a heteromultimeric pore-forming complex.^[1]

1 See also
2 References
3 Further reading
4 External links

[edit] See also

[edit] References

^ ^a ^b Entrez Gene: KCNJ6 potassium inwardly-rectifying channel, subfamily J, member 6.

[edit] Further reading

Kubo Y, Adelman JP, Clapham DE, et al. (2006). "International Union of Pharmacology. LIV. Nomenclature and molecular relationships of inwardly rectifying potassium channels.". Pharmacol. Rev. 57 (4): 509–26. doi:10.1124/pr.57.4.11. PMID 16382105.
Patil N, Cox DR, Bhat D, et al. (1995). "A potassium channel mutation in weaver mice implicates membrane excitability in granule cell differentiation.". Nat. Genet. 11 (2): 126–9. doi:10.1038/ng1095-126. PMID 7550338.
Ferrer J, Nichols CG, Makhina EN, et al. (1995). "Pancreatic islet cells express a family of inwardly rectifying K+ channel subunits which interact to form G-protein-activated channels.". J. Biol. Chem. 270 (44): 26086–91. PMID 7592809.
Tsaur ML, Menzel S, Lai FP, et al. (1995). "Isolation of a cDNA clone encoding a KATP channel-like protein expressed in insulin-secreting cells, localization of the human gene to chromosome band 21q22.1, and linkage studies with NIDDM.". Diabetes 44 (5): 592–6. PMID 7729621.
Sakura H, Bond C, Warren-Perry M, et al. (1995). "Characterization and variation of a human inwardly-rectifying-K-channel gene (KCNJ6): a putative ATP-sensitive K-channel subunit.". FEBS Lett. 367 (2): 193–7. PMID 7796919.
Lesage F, Duprat F, Fink M, et al. (1994). "Cloning provides evidence for a family of inward rectifier and G-protein coupled K+ channels in the brain.". FEBS Lett. 353 (1): 37–42. PMID 7926018.
Liao YJ, Jan YN, Jan LY (1996). "Heteromultimerization of G-protein-gated inwardly rectifying K+ channel proteins GIRK1 and GIRK2 and their altered expression in weaver brain.". J. Neurosci. 16 (22): 7137–50. PMID 8929423.
Signorini S, Liao YJ, Duncan SA, et al. (1997). "Normal cerebellar development but susceptibility to seizures in mice lacking G protein-coupled, inwardly rectifying K+ channel GIRK2.". Proc. Natl. Acad. Sci. U.S.A. 94 (3): 923–7. PMID 9023358.
Ohira M, Seki N, Nagase T, et al. (1997). "Gene identification in 1.6-Mb region of the Down syndrome region on chromosome 21.". Genome Res. 7 (1): 47–58. PMID 9037601.
Huang CL, Jan YN, Jan LY (1997). "Binding of the G protein betagamma subunit to multiple regions of G protein-gated inward-rectifying K+ channels.". FEBS Lett. 405 (3): 291–8. PMID 9108307.
Dahmane N, Ghezala GA, Gosset P, et al. (1998). "Transcriptional map of the 2.5-Mb CBR-ERG region of chromosome 21 involved in Down syndrome.". Genomics 48 (1): 12–23. doi:10.1006/geno.1997.5146. PMID 9503011.
Inanobe A, Horio Y, Fujita A, et al. (2000). "Molecular cloning and characterization of a novel splicing variant of the Kir3.2 subunit predominantly expressed in mouse testis.". J. Physiol. (Lond.) 521 Pt 1: 19–30. PMID 10562331.
Hibino H, Inanobe A, Tanemoto M, et al. (2000). "Anchoring proteins confer G protein sensitivity to an inward-rectifier K(+) channel through the GK domain.". EMBO J. 19 (1): 78–83. doi:10.1093/emboj/19.1.78. PMID 10619846.
Schoots O, Wilson JM, Ethier N, et al. (2000). "Co-expression of human Kir3 subunits can yield channels with different functional properties.". Cell. Signal. 11 (12): 871–83. PMID 10659995.
Hattori M, Fujiyama A, Taylor TD, et al. (2000). "The DNA sequence of human chromosome 21.". Nature 405 (6784): 311–9. doi:10.1038/35012518. PMID 10830953.
Jelacic TM, Kennedy ME, Wickman K, Clapham DE (2000). "Functional and biochemical evidence for G-protein-gated inwardly rectifying K+ (GIRK) channels composed of GIRK2 and GIRK3.". J. Biol. Chem. 275 (46): 36211–6. doi:10.1074/jbc.M007087200. PMID 10956667.
Chen L, Kawano T, Bajic S, et al. (2002). "A glutamate residue at the C terminus regulates activity of inward rectifier K+ channels: implication for Andersen's syndrome.". Proc. Natl. Acad. Sci. U.S.A. 99 (12): 8430–5. doi:10.1073/pnas.122682899. PMID 12034888.
Lavine N, Ethier N, Oak JN, et al. (2003). "G protein-coupled receptors form stable complexes with inwardly rectifying potassium channels and adenylyl cyclase.". J. Biol. Chem. 277 (48): 46010–9. doi:10.1074/jbc.M205035200. PMID 12297500.
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): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Ivanina T, Rishal I, Varon D, et al. (2003). "Mapping the Gbetagamma-binding sites in GIRK1 and GIRK2 subunits of the G protein-activated K+ channel.". J. Biol. Chem. 278 (31): 29174–83. doi:10.1074/jbc.M304518200. PMID 12743112.

[edit] External links

MeSH KCNJ6+protein,+human

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v • d • e Membrane transport protein: ion channels

Ca²⁺: Calcium channel	Voltage-dependent calcium channel (L-type/Ca_vα(1.1, 1.2, 1.3, 1.4), N-type, P-type/Ca_vα(2.1), Q-type, R-type, T-type, α₂δ-subunits (1, 2), β-subunits (β1, β2, β3, β4), γ-subunits (γ1, γ2, γ3, γ4) Inositol triphosphate receptor • Ryanodine receptor • Cation channels of sperm • Two-pore channel

Na⁺: Sodium channel	Na_vα (1.1, 1.2, 1.3, 1.4, 1.5, 1.6, 1.7, 1.9, 7A) • Na_vβ (1, 2, 3, 4) • Epithelial sodium channel

K⁺: Potassium channel	Voltage-gated (K_vα (1.1, 1.2, 1.3, 1.4, 1.5, 2.1, 3.1, 3.4, 4.1, 4.2, 4.3, 6.1, 7.1, 7.2, 7.3, 7.4, 7.5, 9.3, 10.1, 11.1/hERG) • K_vβ (1, 2), Shaker gene, KCNE1) Calcium-activated (BK channel: α1, β1, β2, β3, β4; SK channel: SK1, SK2, SK3, SK4) Inward-rectifier K_ir (1.1, 2.1, 2.2, 2.3, 2.4, GIRK, 3.1, 3.2, 3.3, 3.4, 4.1, 4.2, 5.1, 6.1, 6.2, 7.1) Tandem pore domain K2P (1, 2, 3, 4, 6, 9, 15, 17)

Cl^-: Chloride channel	Cystic fibrosis transmembrane conductance regulator

Porin	Aquaporin (1, 2, 3, 4, 5, 7, 8, 9) • Voltage-dependent anion channel (1)

Cations: TRP	TRPA (1) • TRPC (1, 2, 3, 4, 4AP, 5, 6, 7) • TRPM (1, 2, 3, 4, 5, 6, 7, 8) • TRPML (Mucolipin-1) • TRPP (1, 2) • TRPV (1, 2, 3, 4, 5, 6)

Other/general	Voltage-gated ion channel • Ligand-gated ion channel • Cyclic nucleotide-gated ion channel (α1, α2, α3, β1, β3, H1, H2, H3, H4) • Stretch-activated ion channel