Neutrophil cytosolic factor 1

PDB rendering based on 1gd5.

Available structures
PDB	1GD5, 1K4U, 1KQ6, 1NG2, 1O7K, 1OV3, 1UEC, 1W70, 1WLP

Identifiers

Symbols

NCF1; FLJ79451; NCF1A; NOXO2; SH3PXD1A; p47phox

External IDs

OMIM: 608512 MGI: 97283 HomoloGene: 30964 GeneCards: NCF1 Gene

Gene Ontology
Molecular function	• GTPase activity • protein binding • GTP binding • electron carrier activity • superoxide-generating NADPH oxidase activity • SH3 domain binding • phosphatidylinositol binding
Cellular component	• soluble fraction • cytoplasm • cytosol • NADPH oxidase complex
Biological process	• GTP catabolic process • protein targeting to membrane • superoxide metabolic process • cellular defense response • cell communication • superoxide anion generation • innate immune response • respiratory burst

Orthologs

Species

Human

Mouse

n/a

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 7:
74.19 – 74.2 Mb

Chr 5:
134.7 – 134.71 Mb

PubMed search

[1]

[2]

Neutrophil cytosol factor 1 is a protein that in humans is encoded by the NCF1 gene.

The protein encoded by this gene is a 47 kDa cytosolic subunit of neutrophil NADPH oxidase. This oxidase is a multicomponent enzyme that is activated to produce superoxide anion. Mutations in this gene have been associated with chronic granulomatous disease.^[1] p47 is vital to the activation of NADPH oxidase. P47 becomes heavily phosphorylated

Interactions

Neutrophil cytosolic factor 1 has been shown to interact with Moesin,^[2] RELA^[3] and Neutrophil cytosolic factor 4.^[4]^[5]^[6]

References

^ "Entrez Gene: NCF1 neutrophil cytosolic factor 1, (chronic granulomatous disease, autosomal 1)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=653361.
^ Wientjes, F B; Reeves E P, Soskic V, Furthmayr H, Segal A W (Nov. 2001). "The NADPH oxidase components p47(phox) and p40(phox) bind to moesin through their PX domain". Biochem. Biophys. Res. Commun. (United States) 289 (2): 382–8. doi:10.1006/bbrc.2001.5982. ISSN 0006-291X. PMID 11716484.
^ Gu, Ying; Xu You Cheng, Wu Ru Feng, Nwariaku Fiemu E, Souza Rhonda F, Flores Sonia C, Terada Lance S (May. 2003). "p47phox participates in activation of RelA in endothelial cells". J. Biol. Chem. (United States) 278 (19): 17210–7. doi:10.1074/jbc.M210314200. ISSN 0021-9258. PMID 12618429.
^ Lapouge, Karine; Smith Susan J M, Groemping Yvonne, Rittinger Katrin (Mar. 2002). "Architecture of the p40-p47-p67phox complex in the resting state of the NADPH oxidase. A central role for p67phox". J. Biol. Chem. (United States) 277 (12): 10121–8. doi:10.1074/jbc.M112065200. ISSN 0021-9258. PMID 11796733.
^ Grizot, S; Grandvaux N, Fieschi F, Fauré J, Massenet C, Andrieu J P, Fuchs A, Vignais P V, Timmins P A, Dagher M C, Pebay-Peyroula E (Mar. 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 (United States) 40 (10): 3127–33. doi:10.1021/bi0028439. ISSN 0006-2960. PMID 11258927.
^ Sathyamoorthy, M; de Mendez I, Adams A G, Leto T L (Apr. 1997). "p40(phox) down-regulates NADPH oxidase activity through interactions with its SH3 domain". J. Biol. Chem. (UNITED STATES) 272 (14): 9141–6. doi:10.1074/jbc.272.14.9141. ISSN 0021-9258. PMID 9083043.

Dorseuil O, Gacon G (1997). "[Signal transduction by Rac small G proteins in phagocytes]". C. R. Seances Soc. Biol. Fil. 191 (2): 237–46. PMID 9255350.
Casimir CM, Bu-Ghanim HN, Rodaway AR, et al. (1991). "Autosomal recessive chronic granulomatous disease caused by deletion at a dinucleotide repeat.". Proc. Natl. Acad. Sci. U.S.A. 88 (7): 2753–7. doi:10.1073/pnas.88.7.2753. PMC 51317. PMID 2011585. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=51317.
Rodaway AR, Teahan CG, Casimir CM, et al. (1990). "Characterization of the 47-kilodalton autosomal chronic granulomatous disease protein: tissue-specific expression and transcriptional control by retinoic acid.". Mol. Cell. Biol. 10 (10): 5388–96. PMC 361238. PMID 2398896. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=361238.
Lomax KJ, Leto TL, Nunoi H, et al. (1989). "Recombinant 47-kilodalton cytosol factor restores NADPH oxidase in chronic granulomatous disease.". Science 245 (4916): 409–12. doi:10.1126/science.2547247. PMID 2547247.
Volpp BD, Nauseef WM, Donelson JE, et al. (1989). "Cloning of the cDNA and functional expression of the 47-kilodalton cytosolic component of human neutrophil respiratory burst oxidase.". Proc. Natl. Acad. Sci. U.S.A. 86 (18): 7195–9. doi:10.1073/pnas.86.18.7195. PMC 298023. PMID 2550933. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=298023.
Volpp BD, Nauseef WM, Clark RA (1989). "Two cytosolic neutrophil oxidase components absent in autosomal chronic granulomatous disease.". Science 242 (4883): 1295–7. doi:10.1126/science.2848318. PMID 2848318.
Miki Y, Swensen J, Shattuck-Eidens D, et al. (1994). "A strong candidate for the breast and ovarian cancer susceptibility gene BRCA1.". Science 266 (5182): 66–71. doi:10.1126/science.7545954. PMID 7545954.
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. doi:10.1073/pnas.91.22.10650. PMC 45079. PMID 7938008. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=45079.
el Benna J, Faust LP, Babior BM (1994). "The phosphorylation of the respiratory burst oxidase component p47phox during neutrophil activation. Phosphorylation of sites recognized by protein kinase C and by proline-directed kinases.". J. Biol. Chem. 269 (38): 23431–6. PMID 8089108.
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. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Finan PM, Hall A, Kellie S (1996). "Sam68 from an immortalised B-cell line associates with a subset of SH3 domains.". FEBS Lett. 389 (2): 141–4. doi:10.1016/0014-5793(96)00552-2. PMID 8766817.
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. doi:10.1074/jbc.272.14.9141. PMID 9083043.
Görlach A, Lee PL, Roesler J, et al. (1997). "A p47-phox pseudogene carries the most common mutation causing p47-phox- deficient chronic granulomatous disease.". J. Clin. Invest. 100 (8): 1907–18. doi:10.1172/JCI119721. PMC 508379. PMID 9329953. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=508379.
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. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Izuhara K, Arinobu Y, Sumimoto H, et al. (1999). "Association of the interleukin-4 receptor alpha chain with p47phox, an activator of the phagocyte NADPH oxidase in B cells.". Mol. Immunol. 36 (1): 45–52. doi:10.1016/S0161-5890(98)00111-4. PMID 10369419.
Nakamura F, Huang L, Pestonjamasp K, et al. (1999). "Regulation of F-actin binding to platelet moesin in vitro by both phosphorylation of threonine 558 and polyphosphatidylinositides.". Mol. Biol. Cell 10 (8): 2669–85. PMC 25498. PMID 10436021. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=25498.
Rinckel LA, Faris SL, Hitt ND, Kleinberg ME (1999). "Rac1 disrupts p67phox/p40phox binding: a novel role for Rac in NADPH oxidase activation.". Biochem. Biophys. Res. Commun. 263 (1): 118–22. doi:10.1006/bbrc.1999.1334. PMID 10486263.
Chanock SJ, Roesler J, Zhan S, et al. (2000). "Genomic structure of the human p47-phox (NCF1) gene.". Blood Cells Mol. Dis. 26 (1): 37–46. doi:10.1006/bcmd.2000.0274. PMID 10772875.
Onofri F, Giovedi S, Kao HT, et al. (2000). "Specificity of the binding of synapsin I to Src homology 3 domains.". J. Biol. Chem. 275 (38): 29857–67. doi:10.1074/jbc.M006018200. PMID 10899172.

PDB gallery

1gd5: SOLUTION STRUCTURE OF THE PX DOMAIN FROM HUMAN P47PHOX NADPH OXIDASE

1k4u: Solution structure of the C-terminal SH3 domain of p67phox complexed with the C-terminal tail region of p47phox

1kq6: p47phox PX domain

1ng2: Structure of autoinhibited p47phox

1o7k: HUMAN P47 PX DOMAIN COMPLEX WITH SULPHATES

1ov3: Structure of the p22phox-p47phox complex

1uec: Crystal structure of autoinhibited form of tandem SH3 domain of p47phox

1wlp: Solution Structure Of The P22Phox-P47Phox Complex

Oxidoreductases: NADH or NADPH (EC 1.6)

1.6.1: NAD/NADP	NAD(P)+ transhydrogenase (B-specific)

1.6.2: Heme	Methemoglobin reductase · NADPH-hemoprotein reductase/Cytochrome P450 reductase · NADPH-cytochrome-c2 reductase · Leghemoglobin reductase

1.6.3: Oxygen	NADPH oxidase (P91-PHOX, Neutrophil cytosolic factor 1, Neutrophil cytosolic factor 2, Neutrophil cytosolic factor 4) · dual oxidase (Dual oxidase 1, Dual oxidase 2)

1.6.5: Quinone or similar	NADH dehydrogenase

1.6.6: Nitrogenous group	Trimethylamine-N-oxide reductase

1.6.99: other	NADH dehydrogenase (quinone)

B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6

Neutrophil cytosolic factor 1

Interactions

References

Further reading