Neutrophil cytosolic factor 4

From Wikipedia, the free encyclopedia

Neutrophil cytosolic factor 4, 40kDa

PDB rendering based on 1h6h.

Available structures: 1h6h, 1oey, 1w6x, 1w70, 1z9q, 2dyb

Identifiers

Symbol(s)

NCF4; MGC3810; NCF; P40PHOX; SH3PXD4

External IDs

OMIM: 601488 MGI: 109186 HomoloGene: 525

Gene ontology
Molecular Function:	• phosphoinositide binding • protein dimerization activity
Cellular Component:	• cytosol • membrane • NADPH oxidase complex
Biological Process:	• electron transport • immune response • cell communication

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_000631 (mRNA)
NP_000622 (protein)

NM_008677 (mRNA)
NP_032703 (protein)

Location

Chr 22: 35.59 - 35.6 Mb

Chr 15: 78.07 - 78.09 Mb

Pubmed search

[1]

[2]

Neutrophil cytosolic factor 4, 40kDa, also known as NCF4, is a human gene.^[1]

The protein encoded by this gene is a cytosolic regulatory component of the superoxide-producing phagocyte NADPH-oxidase, a multicomponent enzyme system important for host defense. This protein is preferentially expressed in cells of myeloid lineage. It interacts primarily with neutrophil cytosolic factor 2 (NCF2/p67-phox) to form a complex with neutrophil cytosolic factor 1 (NCF1/p47-phox), which further interacts with the small G protein RAC1 and translocates to the membrane upon cell stimulation. This complex then activates flavocytochrome b, the membrane-integrated catalytic core of the enzyme system. The PX domain of this protein can bind phospholipid products of the PI(3) kinase, which suggests its role in PI(3) kinase-mediated signaling events. The phosphorylation of this protein was found to negatively regulate the enzyme activity. Alternatively spliced transcript variants encoding distinct isoforms have been observed.^[1]

[edit] References

^ ^a ^b Entrez Gene: NCF4 neutrophil cytosolic factor 4, 40kDa.

[edit] Further reading

Matute JD, Arias AA, Dinauer MC, Patiño PJ (2006). "p40phox: the last NADPH oxidase subunit.". Blood Cells Mol. Dis. 35 (2): 291–302. doi:10.1016/j.bcmd.2005.06.010. PMID 16102984.
Jones JH (1977). "The essence of operating room nursing. Paramedical personnel.". The Australasian nurses journal 7 (1): 44–5, 63–4. PMID 243433.
Leto TL, Adams AG, de Mendez I (1994). "Assembly of the phagocyte NADPH oxidase: binding of Src homology 3 domains to proline-rich targets.". Proc. Natl. Acad. Sci. U.S.A. 91 (22): 10650–4. PMID 7938008.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298.
Tsunawaki S, Mizunari H, Nagata M, et al. (1994). "A novel cytosolic component, p40phox, of respiratory burst oxidase associates with p67phox and is absent in patients with chronic granulomatous disease who lack p67phox.". Biochem. Biophys. Res. Commun. 199 (3): 1378–87. doi:10.1006/bbrc.1994.1383. PMID 8147882.
Wientjes FB, Hsuan JJ, Totty NF, Segal AW (1994). "p40phox, a third cytosolic component of the activation complex of the NADPH oxidase to contain src homology 3 domains.". Biochem. J. 296 ( Pt 3): 557–61. PMID 8280052.
Dusi S, Donini M, Rossi F (1996). "Mechanisms of NADPH oxidase activation: translocation of p40phox, Rac1 and Rac2 from the cytosol to the membranes in human neutrophils lacking p47phox or p67phox.". Biochem. J. 314 ( Pt 2): 409–12. PMID 8670049.
Zhan S, Vazquez N, Zhan S, et al. (1996). "Genomic structure, chromosomal localization, start of transcription, and tissue expression of the human p40-phox, a new component of the nicotinamide adenine dinucleotide phosphate-oxidase complex.". Blood 88 (7): 2714–21. PMID 8839867.
Someya A, Nagaoka I, Nunoi H, Yamashita T (1997). "Translocation of guinea pig p40-phox during activation of NADPH oxidase.". Biochim. Biophys. Acta 1277 (3): 217–25. PMID 8982388.
Sathyamoorthy M, de Mendez I, Adams AG, Leto TL (1997). "p40(phox) down-regulates NADPH oxidase activity through interactions with its SH3 domain.". J. Biol. Chem. 272 (14): 9141–6. PMID 9083043.
Grogan A, Reeves E, Keep N, et al. (1998). "Cytosolic phox proteins interact with and regulate the assembly of coronin in neutrophils.". J. Cell. Sci. 110 ( Pt 24): 3071–81. PMID 9365277.
Fuchs A, Bouin AP, Rabilloud T, Vignais PV (1997). "The 40-kDa component of the phagocyte NADPH oxidase (p40phox) is phosphorylated during activation in differentiated HL60 cells.". Eur. J. Biochem. 249 (2): 531–9. PMID 9370364.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. PMID 9373149.
Bouin AP, Grandvaux N, Vignais PV, Fuchs A (1998). "p40(phox) is phosphorylated on threonine 154 and serine 315 during activation of the phagocyte NADPH oxidase. Implication of a protein kinase c-type kinase in the phosphorylation process.". J. Biol. Chem. 273 (46): 30097–103. PMID 9804763.
Grandvaux N, Grizot S, Vignais PV, Dagher MC (1999). "The Ku70 autoantigen interacts with p40phox in B lymphocytes.". J. Cell. Sci. 112 ( Pt 4): 503–13. PMID 9914162.
Nishiyama A, Ohno T, Iwata S, et al. (1999). "Demonstration of the interaction of thioredoxin with p40phox, a phagocyte oxidase component, using a yeast two-hybrid system.". Immunol. Lett. 68 (1): 155–9. PMID 10397171.
Hasebe T, Someya A, Nagaoka I (1999). "Identification of a splice variant mRNA of p40phox, an NADPH oxidase component of phagocytes.". FEBS Lett. 455 (3): 257–61. PMID 10437784.
Dunham I, Shimizu N, Roe BA, et al. (1999). "The DNA sequence of human chromosome 22.". Nature 402 (6761): 489–95. doi:10.1038/990031. PMID 10591208.
Vergnaud S, Paclet MH, El Benna J, et al. (2000). "Complementation of NADPH oxidase in p67-phox-deficient CGD patients p67-phox/p40-phox interaction.". Eur. J. Biochem. 267 (4): 1059–67. PMID 10672014.
Grizot S, Grandvaux N, Fieschi F, et al. (2001). "Small angle neutron scattering and gel filtration analyses of neutrophil NADPH oxidase cytosolic factors highlight the role of the C-terminal end of p47phox in the association with p40phox.". Biochemistry 40 (10): 3127–33. PMID 11258927.