KCNJ3

From Wikipedia, the free encyclopedia


Potassium inwardly-rectifying channel, subfamily J, member 3
PDB rendering based on 1n9p.
Available structures: 1n9p, 1u4e
Identifiers
Symbol(s) KCNJ3; GIRK1; KGA; KIR3.1
External IDs OMIM: 601534 MGI: 104742 HomoloGene: 1687
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 3760 16519
Ensembl ENSG00000162989 ENSMUSG00000026824
Uniprot P48549 Q3ZAT1
Refseq NM_002239 (mRNA)
NP_002230 (protein)		 NM_008426 (mRNA)
NP_032452 (protein)
Location Chr 2: 155.26 - 155.42 Mb Chr 2: 55.25 - 55.41 Mb
Pubmed search [1] [2]

Potassium inwardly-rectifying channel, subfamily J, member 3, also known as KCNJ3 or Kir3.1, 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 plays an important role in regulating heartbeat. It associates with three other G-protein-activated potassium channels to form a hetero-tetrameric pore-forming complex.[1]

Contents

[edit] See also

[edit] References

  1. ^ a b Entrez Gene: KCNJ3 potassium inwardly-rectifying channel, subfamily J, member 3.

[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. 
  • Stoffel M, Espinosa R, Powell KL, et al. (1994). "Human G-protein-coupled inwardly rectifying potassium channel (GIRK1) gene (KCNJ3): localization to chromosome 2 and identification of a simple tandem repeat polymorphism.". Genomics 21 (1): 254-6. doi:10.1006/geno.1994.1253. PMID 8088798. 
  • Schoots O, Yue KT, MacDonald JF, et al. (1996). "Cloning of a G protein-activated inwardly rectifying potassium channel from human cerebellum.". Brain Res. Mol. Brain Res. 39 (1-2): 23-30. PMID 8804710. 
  • 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. 
  • 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. 
  • 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. 
  • Schoots O, Voskoglou T, Van Tol HH (1997). "Genomic organization and promoter analysis of the human G-protein-coupled K+ channel Kir3.1 (KCNJ3/HGIRK1).". Genomics 39 (3): 279-88. doi:10.1006/geno.1996.4495. PMID 9119365. 
  • 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. 
  • Pabon A, Chan KW, Sui JL, et al. (2000). "Glycosylation of GIRK1 at Asn119 and ROMK1 at Asn117 has different consequences in potassium channel function.". J. Biol. Chem. 275 (39): 30677-82. doi:10.1074/jbc.M005338200. PMID 10889209. 
  • 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. 
  • 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. 
  • 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. 
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121-7. doi:10.1101/gr.2596504. PMID 15489334. 
  • Plummer HK, Dhar MS, Cekanova M, Schuller HM (2006). "Expression of G-protein inwardly rectifying potassium channels (GIRKs) in lung cancer cell lines.". BMC Cancer 5: 104. doi:10.1186/1471-2407-5-104. PMID 16109170. 

[edit] External links

 This membrane protein-related article is a stub. You can help Wikipedia by expanding it.

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

v • d • e
Membrane transport protein: ion channels
Ca2+: Calcium channel
Na+: Sodium channel
Navα (1.1, 1.2, 1.3, 1.4, 1.5, 1.6, 1.7, 1.9, 7A) • Navβ (1, 2, 3, 4) • Epithelial sodium channel
K+: Potassium channel
Cl-: Chloride channel
Porin
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