Neutrophil cytosolic factor 1

PDB rendering based on 1gd5.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1GD5, 1K4U, 1KQ6, 1NG2, 1O7K, 1OV3, 1UEC, 1W70, 1WLP

Identifiers

Symbols

NCF1 ; NCF1A; NOXO2; SH3PXD1A; p47phox

External IDs

OMIM: 608512 MGI: 97283 HomoloGene: 30964 ChEMBL: 1613743 GeneCards: NCF1 Gene

Gene ontology
Molecular function	• protein binding • electron carrier activity • superoxide-generating NADPH oxidase activity • SH3 domain binding • phosphatidylinositol binding • phosphatidylinositol-3,4-bisphosphate binding
Cellular component	• cytosol • extrinsic component of membrane • phagolysosome • NADPH oxidase complex
Biological process	• response to yeast • antigen processing and presentation of peptide antigen via MHC class I • antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent • respiratory burst involved in defense response • protein targeting to membrane • leukotriene metabolic process • superoxide metabolic process • inflammatory response • cellular defense response • small GTPase mediated signal transduction • cell proliferation • superoxide anion generation • antigen processing and presentation of exogenous peptide antigen via MHC class I • innate immune response • respiratory burst • negative regulation of smooth muscle contraction • vascular endothelial growth factor receptor signaling pathway • hydrogen peroxide biosynthetic process • interaction with host • oxidation-reduction process • neutrophil mediated killing of gram-positive bacterium • neutrophil mediated killing of fungus • phagosome maturation
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 7:
74.77 – 74.79 Mb

Chr 5:
134.22 – 134.23 Mb

PubMed search

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

Function

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]
Neutrophil cytosolic factor 4,^[3]^[4]^[5] and
RELA.^[6]

References

↑ "Entrez Gene: NCF1 neutrophil cytosolic factor 1, (chronic granulomatous disease, autosomal 1)".
↑ Wientjes FB, Reeves EP, Soskic V, Furthmayr H, Segal AW (Nov 2001). "The NADPH oxidase components p47(phox) and p40(phox) bind to moesin through their PX domain". Biochem. Biophys. Res. Commun. 289 (2): 382–8. doi:10.1006/bbrc.2001.5982. PMID 11716484.
↑ Lapouge K, Smith SJ, Groemping Y, Rittinger K (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. 277 (12): 10121–8. doi:10.1074/jbc.M112065200. PMID 11796733.
↑ Grizot S, Grandvaux N, Fieschi F, Fauré J, Massenet C, Andrieu JP, Fuchs A, Vignais PV, Timmins PA, Dagher MC, 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 40 (10): 3127–33. doi:10.1021/bi0028439. PMID 11258927.
↑ Sathyamoorthy M, de Mendez I, Adams AG, Leto TL (Apr 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.
↑ Gu Y, Xu YC, Wu RF, Nwariaku FE, Souza RF, Flores SC, Terada LS (May 2003). "p47phox participates in activation of RelA in endothelial cells". J. Biol. Chem. 278 (19): 17210–7. doi:10.1074/jbc.M210314200. PMID 12618429.

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, Bentley DL, Rowe P, Segal AW (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.
Rodaway AR, Teahan CG, Casimir CM, Segal AW, Bentley DL (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. doi:10.1128/mcb.10.10.5388. PMC 361238. PMID 2398896.
Lomax KJ, Leto TL, Nunoi H, Gallin JI, Malech HL (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, Moser DR, Clark RA (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.
Volpp BD, Nauseef WM, Clark RA (1988). "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, Futreal PA, Harshman K, Tavtigian S, Liu Q, Cochran C, Bennett LM, Ding W (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.
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, Hopkins PJ, Christensen B, Green ED, Chanock SJ, Curnutte JT (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.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (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, Nunoi H, Takeya R, Higuchi K, Takeshige K, Hamasaki N, Harada N (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, Luna EJ, Furthmayr H (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. doi:10.1091/mbc.10.8.2669. PMC 25498. PMID 10436021.
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, Hopkins P, Lee P, Barrett DT, Christensen BL, Curnutte JT, Görlach A (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, Valtorta F, Bongiorno Borbone L, De Camilli P, Greengard P, Benfenati F (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 (Si-specific) NAD(P)⁺ transhydrogenase (Re/Si-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)

This article is issued from Wikipedia - version of the Tuesday, January 26, 2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.

Neutrophil cytosolic factor 1

Function

Interactions

References

Further reading