KCNJ15

Potassium channel, inwardly rectifying subfamily J, member 15

Identifiers

KCNJ15 ; IRKK; KIR1.3; KIR4.2

External IDs

OMIM: 602106 MGI: 1310000 HomoloGene: 1690 IUPHAR: 439 GeneCards: KCNJ15 Gene

Gene ontology
Molecular function	• inward rectifier potassium channel activity • protein binding
Cellular component	• plasma membrane • integral component of plasma membrane
Biological process	• potassium ion transport • synaptic transmission • potassium ion import • regulation of ion transmembrane transport
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 21:
38.16 – 38.31 Mb

Chr 16:
95.26 – 95.3 Mb

PubMed search

Potassium inwardly-rectifying channel, subfamily J, member 15, also known as KCNJ15 is a human gene, which encodes the K_ir4.2 protein.^[1]

Function

Potassium channels are present in most mammalian cells, where they participate in a wide range of physiologic responses. K_ir4.2 is an integral membrane protein and inward-rectifier type potassium channel. K_ir4.2 has a greater tendency to allow potassium to flow into a cell rather than out of a cell. Three transcript variants encoding the same protein have been found for this gene.^[1]

The existing literature describing KCNJ15 and K_ir4.2 is sparse. In spite of some initial channel nomenclature confusion, in which the gene was referred to as Kir1.3^[2] the channel was first cloned from human kidney by Shuck and coworkers in 1997.^[3] Shortly thereafter it was shown that mutation of an extracellular lysine residue resulted in 6-fold increase in K⁺ current.^[4] Two years later, in 1999, voltage clamp measurements in xenopus oocytes found that intracellular acidification decreased the potassium current of K_ir4.2. Also activation of protein kinase C decreased the current although in a non-reversible fashion. Furthermore it was found that coexpression with related potassium channel K_ir5.1, changed these results somewhat, which the authors concluded was likely to be a result of heterodimerization.^[2] Further voltage clamp investigations found the exact pH sensitivity (pK_a = 7.1), open probability (high) and conductance of ~25 pS.^[5] In 2007 the channel was found to interact with the Calcium-sensing receptor in human kidney, using a yeast-two-hybrid system. This co-localization was verified at the protein level using both immunofluorescence techniques and coimmunoprecipitation of K_ir4.2 and the Calcium-sensing receptor.^[6] Also a mutational study of K_ir4.2 has demonstrated that removal of a c-terminal tyrosine increased the K⁺ current more than 10-fold.^[7] Because the channel has a very high open probability, the authors of this last article conclude that this increase is mediated by increased trafficking of the protein to the membrane and not increased single-channel conductance. This same line of reasoning is applicable to the initial work of Derst and coworkers.^[4]

Interactions

KCNJ15 has been shown to interact with Interleukin 16.^[8]

References

1 2 "Entrez Gene: KCNJ15 potassium inwardly-rectifying channel, subfamily J, member 15".
1 2 Pearson WL, Dourado M, Schreiber M, Salkoff L, Nichols CG (1999). "Expression of a functional Kir4 family inward rectifier K+ channel from a gene cloned from mouse liver". J. Physiol. (Lond.). 514 ( Pt 3) (3): 639–653. doi:10.1111/j.1469-7793.1999.639ad.x. PMC 2269105. PMID 9882736.
↑ Shuck ME, Piser TM, Bock JH, Slightom JL, Lee KS, Bienkowski MJ (1997). "Cloning and characterization of two K+ inward rectifier (Kir) 1.1 potassium channel homologs from human kidney (Kir1.2 and Kir1.3)". J. Biol. Chem. 272 (1): 586–593. doi:10.1074/jbc.272.1.586. PMID 8995301.
1 2 Derst C, Wischmeyer E, Preisig-Müller R, et al. (1998). "A hyperprostaglandin E syndrome mutation in Kir1.1 (renal outer medullary potassium) channels reveals a crucial residue for channel function in Kir1.3 channels". J. Biol. Chem. 273 (37): 23884–23891. doi:10.1074/jbc.273.37.23884. PMID 9727001.
↑ Pessia M, Imbrici P, D'Adamo MC, Salvatore L, Tucker SJ (2001). "Differential pH sensitivity of Kir4.1 and Kir4.2 potassium channels and their modulation by heteropolymerisation with Kir5.1". J. Physiol. (Lond.) 532 (Pt 2): 359–367. doi:10.1111/j.1469-7793.2001.0359f.x. PMC 2278540. PMID 11306656.
↑ Huang C, Sindic A, Hill CE, et al. (2007). "Interaction of the Ca2+-sensing receptor with the inwardly rectifying potassium channels Kir4.1 and Kir4.2 results in inhibition of channel function". Am. J. Physiol. Renal Physiol. 292 (3): F1073–F1081. doi:10.1152/ajprenal.00269.2006. PMID 17122384.
↑ Pearson WL, Skatchkov SN, Eaton MJ, Nichols CG (2006). "C-terminal determinants of Kir4.2 channel expression". J. Membr. Biol. 213 (3): 187–193. doi:10.1007/s00232-006-0058-6. PMID 17468958.
↑ Kurschner, C; Yuzaki, M (Sep 1999). "Neuronal interleukin-16 (NIL-16): a dual function PDZ domain protein". J. Neurosci. 19 (18): 7770–80. PMID 10479680.

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

Protein: cell membrane proteins (other than Cell surface receptor, enzymes, and cytoskeleton)

Arrestin	SAG ARRB1 ARRB2 ARR3

Membrane-spanning 4A	MS4A1 MS4A2 MS4A3 MS4A4A MS4A4E MS4A5 MS4A6A MS4A6E MS4A7 MS4A8B MS4A9 MS4A10 MS4A12 MS4A13 MS4A14 MS4A15 MS4A18

Myelin	Myelin basic protein PMP2 Myelin proteolipid protein PLP1 Myelin oligodendrocyte glycoprotein Myelin-associated glycoprotein Myelin protein zero

Pulmonary surfactant	Pulmonary surfactant-associated protein B Pulmonary surfactant-associated protein C

Tetraspanin	TSPAN1 TSPAN2 TSPAN3 TSPAN4 TSPAN5 TSPAN6 TSPAN7 TSPAN8 TSPAN9 TSPAN10 TSPAN11 TSPAN12 TSPAN13 TSPAN14 TSPAN15 TSPAN16 TSPAN17 TSPAN18 TSPAN19 TSPAN20 TSPAN21 TSPAN22 TSPAN23 TSPAN24 TSPAN25 TSPAN26 TSPAN27 TSPAN28 TSPAN29 TSPAN30 TSPAN31 TSPAN32 TSPAN33 TSPAN34

Other/ungrouped	Calnexin LDL-receptor-related protein-associated protein Neurofibromin 2 Presenilin PSEN1 PSEN2 HFE Phospholipid transfer proteins Dysferlin STRC OTOF

see also other cell membrane protein disorders

Membrane transport protein: ion channels (TC 1A)

Ca²⁺: Calcium channel

Ligand-gated	Inositol trisphosphate receptor 1 2 3 Ryanodine receptor 1 2 3

Voltage-gated	L-type/Ca_vα 1.1 1.2 1.3 1.4 N-type/Ca_vα2.2 P-type/Ca_vα 2.1 Q-type/Ca_vα2.1 R-type/Ca_vα2.3 T-type/Ca_vα 3.1 3.2 3.3 α₂δ-subunits 1 2 β-subunits β1 β2 β3 β4 γ-subunits γ1 γ2 γ3 γ4 Cation channels of sperm 1 2 3 4 Two-pore channel 1 2

Na⁺: Sodium channel

Constitutively active	Epithelial sodium channel α β γ δ

Proton-gated	Amiloride-sensitive cation channel 1 2 3 4

Voltage-gated	Na_vα 1.1 1.2 1.3 1.4 1.5 1.6 1.7 1.8 1.9 7A Na_vβ 1 2 3 4

K⁺: Potassium channel

Calcium-activated	BK channel α1 β1 β2 β3 β4 SK channel SK1 SK2 SK3 IK channel IK1 K_Ca 1.1 2.1 2.2 2.3 3.1 4.1 4.2 5.1

Inward-rectifier	K_ATP K_ir 1.1 2.1 2.2 2.3 2.4 2.6 GIRK/K_ir 3.1 3.2 3.3 3.4 K_ir 4.1 4.2 5.1 6.1 6.2 7.1

Tandem pore domain	K2P 1 2 3 4 5 6 7 9 10 12 13 15 16 17 18

Voltage-gated	K_vα1-6 1.1 1.2 1.3 1.4 1.5 1.6 1.7 1.8 2.1 2.2 3.1 3.2 3.3 3.4 4.1 4.2 4.3 5.1 6.1 6.2 6.3 6.4 K_vα7-12 7.1 7.2 7.3 7.4 7.5 8.1 8.2 9.1 9.2 9.3 10.1 10.2 11.1/hERG 11.2 11.3 12.1 12.2 12.3 K_vβ 1 2 3 KCNIP 1 2 3 4 minK/ISK minK/ISK-like MiRP 1 2 3 Shaker gene

Miscellaneous

Cl⁻: Chloride channel	Calcium-activated chloride channels Anoctamin ANO1 Bestrophin 1 2 Chloride Channel Accessory 1 2 3 4 CFTR CLCN 1 2 3 4 5 6 7 KA KB CLIC 1 2 3 4 5 6 L1 CLNS 1A 1B

H⁺: Proton channel	HVCN1

M⁺: CNG cation channel	α 1 2 3 4 β 1 2 3 HCN FC 1 2 3 4

M⁺: TRP cation channel	TRPA (1) TRPC 1 2 3 4 4AP 5 6 7 TRPM 1 2 3 4 5 6 7 8 TRPML 1 2 3 TRPN TRPP 1 2 TRPV 1 2 3 4 5 6

H₂O (+ solutes): Porin	Aquaporin 0 1 2 3 4 5 6 7 8 9 Voltage-dependent anion channel 1 2 3 General bacterial porin family

Cytoplasm: Gap junction	Connexin: A GJA1 GJA3 GJA4 GJA5 GJA8 GJA9 GJA10 B GJB1 GJB2 GJB3 GJB4 GJB5 GJB6 GJB7 C GJC1 GJC2 GJC3 D GJD2 GJD3 GJD4) Innexin

By gating mechanism

Ion channel class	Ligand-gated Light-gated Voltage-gated Stretch-activated

see also disorders

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KCNJ15

Function

Interactions

See also

References