KCNJ5

From Wikipedia, the free encyclopedia

Potassium inwardly-rectifying channel, subfamily J, member 5

Identifiers

KCNJ5; CIR; GIRK4; KATP1; KIR3.4

External IDs

OMIM: 600734 MGI: 104755 HomoloGene: 20248

Gene ontology
Molecular Function:	• voltage-gated ion channel activity • G-protein enhanced inward rectifier potassium 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

Orthologs

Human

Mouse

Refseq

NM_000890 (mRNA)
NP_000881 (protein)

NM_010605 (mRNA)
NP_034735 (protein)

Location

Chr 11: 128.27 - 128.29 Mb

Chr 9: 32.06 - 32.09 Mb

Pubmed search

[1]

[2]

Potassium inwardly-rectifying channel, subfamily J, member 5, also known as KCNJ5 or K_ir3.4, 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. It may associate 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: KCNJ5 potassium inwardly-rectifying channel, subfamily J, member 5.

[edit] Further reading

Zhuo ML, Huang Y, Liu DP, Liang CC (2005). "KATP channel: relation with cell metabolism and role in the cardiovascular system.". Int. J. Biochem. Cell Biol. 37 (4): 751–64. doi:10.1016/j.biocel.2004.10.008. PMID 15694835.
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.
Tucker SJ, James MR, Adelman JP (1995). "Assignment of KATP-1, the cardiac ATP-sensitive potassium channel gene (KCNJ5), to human chromosome 11q24.". Genomics 28 (1): 127–8. doi:10.1006/geno.1995.1121. PMID 7590741.
Ashford ML, Bond CT, Blair TA, Adelman JP (1994). "Cloning and functional expression of a rat heart KATP channel.". Nature 370 (6489): 456–9. doi:10.1038/370456a0. PMID 8047164.
Ashford ML, Bond CT, Blair TA, Adelman JP (1996). "Cloning and functional expression of a rat heart KATP channel.". Nature 378 (6559): 792. doi:10.1038/378792a0. PMID 8524415.
Spauschus A, Lentes KU, Wischmeyer E, et al. (1996). "A G-protein-activated inwardly rectifying K+ channel (GIRK4) from human hippocampus associates with other GIRK channels.". J. Neurosci. 16 (3): 930–8. PMID 8558261.
Iizuka M, Kubo Y, Tsunenari I, et al. (1996). "Functional characterization and localization of a cardiac-type inwardly rectifying K+ channel.". Recept. Channels 3 (4): 299–315. PMID 8834003.
Chan KW, Langan MN, Sui JL, et al. (1996). "A recombinant inwardly rectifying potassium channel coupled to GTP-binding proteins.". J. Gen. Physiol. 107 (3): 381–97. PMID 8868049.
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.
Kanzaki M, Lindorfer MA, Garrison JC, Kojima I (1997). "Activation of the calcium-permeable cation channel CD20 by alpha subunits of the Gi protein.". J. Biol. Chem. 272 (23): 14733–9. PMID 9169438.
Wischmeyer E, Döring F, Wischmeyer E, et al. (1997). "Subunit interactions in the assembly of neuronal Kir3.0 inwardly rectifying K+ channels.". Mol. Cell. Neurosci. 9 (3): 194–206. doi:10.1006/mcne.1997.0614. PMID 9245502.
Krapivinsky G, Kennedy ME, Nemec J, et al. (1998). "Gbeta binding to GIRK4 subunit is critical for G protein-gated K+ channel activation.". J. Biol. Chem. 273 (27): 16946–52. PMID 9642257.
Corey S, Clapham DE (1998). "Identification of native atrial G-protein-regulated inwardly rectifying K+ (GIRK4) channel homomultimers.". J. Biol. Chem. 273 (42): 27499–504. PMID 9765280.
Kennedy ME, Nemec J, Corey S, et al. (1999). "GIRK4 confers appropriate processing and cell surface localization to G-protein-gated potassium channels.". J. Biol. Chem. 274 (4): 2571–82. PMID 9891030.
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.
He C, Yan X, Zhang H, et al. (2002). "Identification of critical residues controlling G protein-gated inwardly rectifying K(+) channel activity through interactions with the beta gamma subunits of G proteins.". J. Biol. Chem. 277 (8): 6088–96. doi:10.1074/jbc.M104851200. PMID 11741896.
Ma D, Zerangue N, Raab-Graham K, et al. (2002). "Diverse trafficking patterns due to multiple traffic motifs in G protein-activated inwardly rectifying potassium channels from brain and heart.". Neuron 33 (5): 715–29. PMID 11879649.
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.
Shankar H, Murugappan S, Kim S, et al. (2004). "Role of G protein-gated inwardly rectifying potassium channels in P2Y12 receptor-mediated platelet functional responses.". Blood 104 (5): 1335–43. doi:10.1182/blood-2004-01-0069. PMID 15142872.

[edit] External links

MeSH KCNJ5+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