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{{Infobox_gene}}
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'''NADPH oxidase, EF-hand calcium binding domain 5''', also known as '''NOX5''', is a [[protein]] which in humans is encoded by the ''NOX5'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NOX5 NADPH oxidase, EF-hand calcium binding domain 5| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=79400| accessdate = }}</ref><ref name="pmid11483596">{{cite journal | vauthors = Bánfi B, Molnár G, Maturana A, Steger K, Hegedûs B, Demaurex N, Krause KH | title = A Ca(2+)-activated NADPH oxidase in testis, spleen, and lymph nodes | journal = J. Biol. Chem. | volume = 276 | issue = 40 | pages = 37594–601 |date=October 2001 | pmid = 11483596 | doi = 10.1074/jbc.M103034200 | url = }}</ref>
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== Function ==
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
NOX5 is a novel [[NADPH oxidase]] that generates [[superoxide]].<ref name="entrez" />
{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = NADPH oxidase, EF-hand calcium binding domain 5
| HGNCid = 14874
| Symbol = NOX5
| AltSymbols =; MGC149776; MGC149777; NOX5A; NOX5B
| OMIM = 606572
| ECnumber = 
| Homologene = 41568
| MGIid = 
| GeneAtlas_image1 = PBB_GE_NOX5_220641_at_tn.png
| Function = {{GNF_GO|id=GO:0005216 |text = ion channel activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0015252 |text = hydrogen ion channel activity}} {{GNF_GO|id=GO:0016175 |text = superoxide-generating NADPH oxidase activity}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0020037 |text = heme binding}} {{GNF_GO|id=GO:0050660 |text = FAD binding}} {{GNF_GO|id=GO:0050661 |text = NADP binding}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0000910 |text = cytokinesis}} {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0010155 |text = regulation of proton transport}} {{GNF_GO|id=GO:0042554 |text = superoxide release}} {{GNF_GO|id=GO:0043012 |text = regulation of fusion of sperm to egg plasma membrane}} {{GNF_GO|id=GO:0050663 |text = cytokine secretion}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 79400
    | Hs_Ensembl = ENSG00000137808
    | Hs_RefseqProtein = NP_078781
    | Hs_RefseqmRNA = NM_024505
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 15
    | Hs_GenLoc_start = 67094125
    | Hs_GenLoc_end = 67136516
    | Hs_Uniprot = Q96PH1
    | Mm_EntrezGene = 
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = 
    | Mm_RefseqProtein = 
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
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  }}
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'''NADPH oxidase, EF-hand calcium binding domain 5''', also known as '''NOX5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NOX5 NADPH oxidase, EF-hand calcium binding domain 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=79400| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
Nox5 interacts with [[Abl gene|c-abl]], superoxide production leads to [[phosphorylation]] of c-abl, while inhibition of c-abl kinase activity inhibits Nox5 superoxide production.<ref name="pmid18160052">{{cite journal | vauthors = El Jamali A, Valente AJ, Lechleiter JD, Gamez MJ, Pearson DW, Nauseef WM, Clark RA | title = NOVEL REDOX-DEPENDENT REGULATION OF NOX5 BY THE TYROSINE KINASE C-ABL | journal = Free Radic. Biol. Med. | volume = 44 | issue = 5 | pages = 868–81 |date=March 2008 | pmid = 18160052 | pmc = 2278123 | doi = 10.1016/j.freeradbiomed.2007.11.020 | url = }}</ref>
{{PBB_Summary
| section_title =
| summary_text = NOX5 is a novel NADPH oxidase that generates superoxide and functions as a H+ channel in a Ca(2+)-dependent manner.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: NOX5 NADPH oxidase, EF-hand calcium binding domain 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=79400| accessdate = }}</ref>
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal | author=Lachgar A, Sojic N, Arbault S, ''et al.'' |title=Amplification of the inflammatory cellular redox state by human immunodeficiency virus type 1-immunosuppressive tat and gp160 proteins. |journal=J. Virol. |volume=73 |issue= 2 |pages= 1447-52 |year= 1999 |pmid= 9882350 |doi=  }}
*{{cite journal   |vauthors=Lachgar A, Sojic N, Arbault S, etal |title=Amplification of the Inflammatory Cellular Redox State by Human Immunodeficiency Virus Type 1-Immunosuppressive Tat and gp160 Proteins |journal=J. Virol. |volume=73 |issue= 2 |pages= 1447–52 |year= 1999 |pmid= 9882350 |doi= | pmc=103969 }}
*{{cite journal | author=Cheng G, Cao Z, Xu X, ''et al.'' |title=Homologs of gp91phox: cloning and tissue expression of Nox3, Nox4, and Nox5. |journal=Gene |volume=269 |issue= 1-2 |pages= 131-40 |year= 2001 |pmid= 11376945 |doi= }}
*{{cite journal   |vauthors=Cheng G, Cao Z, Xu X, etal |title=Homologs of gp91phox: cloning and tissue expression of Nox3, Nox4, and Nox5 |journal=Gene |volume=269 |issue= 1–2 |pages= 131–40 |year= 2001 |pmid= 11376945 |doi=10.1016/S0378-1119(01)00449-8  }}
*{{cite journal | author=Bánfi B, Molnár G, Maturana A, ''et al.'' |title=A Ca(2+)-activated NADPH oxidase in testis, spleen, and lymph nodes. |journal=J. Biol. Chem. |volume=276 |issue= 40 |pages= 37594-601 |year= 2001 |pmid= 11483596 |doi= 10.1074/jbc.M103034200 }}
*{{cite journal   |vauthors=Bánfi B, Molnár G, Maturana A, etal |title=A Ca(2+)-activated NADPH oxidase in testis, spleen, and lymph nodes |journal=J. Biol. Chem. |volume=276 |issue= 40 |pages= 37594–601 |year= 2001 |pmid= 11483596 |doi= 10.1074/jbc.M103034200 }}
*{{cite journal | author=Armstrong JS, Bivalacqua TJ, Chamulitrat W, ''et al.'' |title=A comparison of the NADPH oxidase in human sperm and white blood cells. |journal=Int. J. Androl. |volume=25 |issue= 4 |pages= 223-9 |year= 2002 |pmid= 12121572 |doi= }}
*{{cite journal   |vauthors=Armstrong JS, Bivalacqua TJ, Chamulitrat W, etal |title=A comparison of the NADPH oxidase in human sperm and white blood cells |journal=Int. J. Androl. |volume=25 |issue= 4 |pages= 223–9 |year= 2002 |pmid= 12121572 |doi=10.1046/j.1365-2605.2002.00351.x  }}
*{{cite journal | author=Moskwa P, Dagher MC, Paclet MH, ''et al.'' |title=Participation of Rac GTPase activating proteins in the deactivation of the phagocytic NADPH oxidase. |journal=Biochemistry |volume=41 |issue= 34 |pages= 10710-6 |year= 2002 |pmid= 12186557 |doi=  }}
*{{cite journal   |vauthors=Moskwa P, Dagher MC, Paclet MH, etal |title=Participation of Rac GTPase activating proteins in the deactivation of the phagocytic NADPH oxidase |journal=Biochemistry |volume=41 |issue= 34 |pages= 10710–6 |year= 2002 |pmid= 12186557 |doi=10.1021/bi0257033 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal   |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal | author=Bánfi B, Tirone F, Durussel I, ''et al.'' |title=Mechanism of Ca2+ activation of the NADPH oxidase 5 (NOX5). |journal=J. Biol. Chem. |volume=279 |issue= 18 |pages= 18583-91 |year= 2004 |pmid= 14982937 |doi= 10.1074/jbc.M310268200 }}
*{{cite journal   |vauthors=Bánfi B, Tirone F, Durussel I, etal |title=Mechanism of Ca2+ activation of the NADPH oxidase 5 (NOX5) |journal=J. Biol. Chem. |volume=279 |issue= 18 |pages= 18583–91 |year= 2004 |pmid= 14982937 |doi= 10.1074/jbc.M310268200 }}
*{{cite journal  | author=Jana A, Pahan K |title=Human immunodeficiency virus type 1 gp120 induces apoptosis in human primary neurons through redox-regulated activation of neutral sphingomyelinase. |journal=J. Neurosci. |volume=24 |issue= 43 |pages= 9531-40 |year= 2005 |pmid= 15509740 |doi= 10.1523/JNEUROSCI.3085-04.2004 }}
*{{cite journal  | vauthors=Jana A, Pahan K |title=Human Immunodeficiency Virus Type 1 gp120 Induces Apoptosis in Human Primary Neurons through Redox-Regulated Activation of Neutral Sphingomyelinase |journal=J. Neurosci. |volume=24 |issue= 43 |pages= 9531–40 |year= 2005 |pmid= 15509740 |doi= 10.1523/JNEUROSCI.3085-04.2004 | pmc=1955476 }}
*{{cite journal  | author=Kawahara T, Ritsick D, Cheng G, Lambeth JD |title=Point mutations in the proline-rich region of p22phox are dominant inhibitors of Nox1- and Nox2-dependent reactive oxygen generation. |journal=J. Biol. Chem. |volume=280 |issue= 36 |pages= 31859-69 |year= 2005 |pmid= 15994299 |doi= 10.1074/jbc.M501882200 }}
*{{cite journal  | vauthors=Kawahara T, Ritsick D, Cheng G, Lambeth JD |title=Point mutations in the proline-rich region of p22phox are dominant inhibitors of Nox1- and Nox2-dependent reactive oxygen generation |journal=J. Biol. Chem. |volume=280 |issue= 36 |pages= 31859–69 |year= 2005 |pmid= 15994299 |doi= 10.1074/jbc.M501882200 }}
*{{cite journal  | author=Femling JK, Nauseef WM, Weiss JP |title=Synergy between extracellular group IIA phospholipase A2 and phagocyte NADPH oxidase in digestion of phospholipids of Staphylococcus aureus ingested by human neutrophils. |journal=J. Immunol. |volume=175 |issue= 7 |pages= 4653-61 |year= 2005 |pmid= 16177112 |doi=  }}
*{{cite journal  | vauthors=Femling JK, Nauseef WM, Weiss JP |title=Synergy between extracellular group IIA phospholipase A2 and phagocyte NADPH oxidase in digestion of phospholipids of Staphylococcus aureus ingested by human neutrophils |journal=J. Immunol. |volume=175 |issue= 7 |pages= 4653–61 |year= 2005 |pmid= 16177112 |doi=  10.4049/jimmunol.175.7.4653}}
*{{cite journal | author=Cucoranu I, Clempus R, Dikalova A, ''et al.'' |title=NAD(P)H oxidase 4 mediates transforming growth factor-beta1-induced differentiation of cardiac fibroblasts into myofibroblasts. |journal=Circ. Res. |volume=97 |issue= 9 |pages= 900-7 |year= 2005 |pmid= 16179589 |doi= 10.1161/01.RES.0000187457.24338.3D }}
*{{cite journal   |vauthors=Cucoranu I, Clempus R, Dikalova A, etal |title=NAD(P)H oxidase 4 mediates transforming growth factor-beta1-induced differentiation of cardiac fibroblasts into myofibroblasts |journal=Circ. Res. |volume=97 |issue= 9 |pages= 900–7 |year= 2005 |pmid= 16179589 |doi= 10.1161/01.RES.0000187457.24338.3D }}
*{{cite journal | author=Kamiguti AS, Serrander L, Lin K, ''et al.'' |title=Expression and activity of NOX5 in the circulating malignant B cells of hairy cell leukemia. |journal=J. Immunol. |volume=175 |issue= 12 |pages= 8424-30 |year= 2006 |pmid= 16339585 |doi=  }}
*{{cite journal   |vauthors=Kamiguti AS, Serrander L, Lin K, etal |title=Expression and activity of NOX5 in the circulating malignant B cells of hairy cell leukemia |journal=J. Immunol. |volume=175 |issue= 12 |pages= 8424–30 |year= 2006 |pmid= 16339585 |doi=  10.4049/jimmunol.175.12.8424}}
*{{cite journal | author=Fu X, Beer DG, Behar J, ''et al.'' |title=cAMP-response element-binding protein mediates acid-induced NADPH oxidase NOX5-S expression in Barrett esophageal adenocarcinoma cells. |journal=J. Biol. Chem. |volume=281 |issue= 29 |pages= 20368-82 |year= 2006 |pmid= 16707484 |doi= 10.1074/jbc.M603353200 }}
*{{cite journal   |vauthors=Fu X, Beer DG, Behar J, etal |title=cAMP-response element-binding protein mediates acid-induced NADPH oxidase NOX5-S expression in Barrett esophageal adenocarcinoma cells |journal=J. Biol. Chem. |volume=281 |issue= 29 |pages= 20368–82 |year= 2006 |pmid= 16707484 |doi= 10.1074/jbc.M603353200 }}
*{{cite journal | author=Duerrschmidt N, Stielow C, Muller G, ''et al.'' |title=NO-mediated regulation of NAD(P)H oxidase by laminar shear stress in human endothelial cells. |journal=J. Physiol. (Lond.) |volume=576 |issue= Pt 2 |pages= 557-67 |year= 2006 |pmid= 16873416 |doi= 10.1113/jphysiol.2006.111070 }}
*{{cite journal   |vauthors=Duerrschmidt N, Stielow C, Muller G, etal |title=NO-mediated regulation of NAD(P)H oxidase by laminar shear stress in human endothelial cells |journal=J. Physiol. |volume=576 |issue= Pt 2 |pages= 557–67 |year= 2006 |pmid= 16873416 |doi= 10.1113/jphysiol.2006.111070  | pmc=1890367 }}
*{{cite journal | author=Chenevier-Gobeaux C, Lemarechal H, Bonnefont-Rousselot D, ''et al.'' |title=Superoxide production and NADPH oxidase expression in human rheumatoid synovial cells: regulation by interleukin-1beta and tumour necrosis factor-alpha. |journal=Inflamm. Res. |volume=55 |issue= 11 |pages= 483-90 |year= 2007 |pmid= 17122966 |doi= 10.1007/s00011-006-6036-8 }}
*{{cite journal   |vauthors=Chenevier-Gobeaux C, Lemarechal H, Bonnefont-Rousselot D, etal |title=Superoxide production and NADPH oxidase expression in human rheumatoid synovial cells: regulation by interleukin-1beta and tumour necrosis factor-alpha |journal=Inflamm. Res. |volume=55 |issue= 11 |pages= 483–90 |year= 2007 |pmid= 17122966 |doi= 10.1007/s00011-006-6036-8 }}
*{{cite journal | author=Jagnandan D, Church JE, Banfi B, ''et al.'' |title=Novel mechanism of activation of NADPH oxidase 5. calcium sensitization via phosphorylation. |journal=J. Biol. Chem. |volume=282 |issue= 9 |pages= 6494-507 |year= 2007 |pmid= 17164239 |doi= 10.1074/jbc.M608966200 }}
*{{cite journal   |vauthors=Jagnandan D, Church JE, Banfi B, etal |title=Novel mechanism of activation of NADPH oxidase 5. calcium sensitization via phosphorylation |journal=J. Biol. Chem. |volume=282 |issue= 9 |pages= 6494–507 |year= 2007 |pmid= 17164239 |doi= 10.1074/jbc.M608966200 }}
*{{cite journal | author=BelAiba RS, Djordjevic T, Petry A, ''et al.'' |title=NOX5 variants are functionally active in endothelial cells. |journal=Free Radic. Biol. Med. |volume=42 |issue= 4 |pages= 446-59 |year= 2007 |pmid= 17275676 |doi= 10.1016/j.freeradbiomed.2006.10.054 }}
*{{cite journal   |vauthors=BelAiba RS, Djordjevic T, Petry A, etal |title=NOX5 variants are functionally active in endothelial cells |journal=Free Radic. Biol. Med. |volume=42 |issue= 4 |pages= 446–59 |year= 2007 |pmid= 17275676 |doi= 10.1016/j.freeradbiomed.2006.10.054 }}
*{{cite journal  | author=Tirone F, Cox JA |title=NADPH oxidase 5 (NOX5) interacts with and is regulated by calmodulin. |journal=FEBS Lett. |volume=581 |issue= 6 |pages= 1202-8 |year= 2007 |pmid= 17346712 |doi= 10.1016/j.febslet.2007.02.047 }}
*{{cite journal  | vauthors=Tirone F, Cox JA |title=NADPH oxidase 5 (NOX5) interacts with and is regulated by calmodulin |journal=FEBS Lett. |volume=581 |issue= 6 |pages= 1202–8 |year= 2007 |pmid= 17346712 |doi= 10.1016/j.febslet.2007.02.047 }}
*{{cite journal  | author=Qin F, Simeone M, Patel R |title=Inhibition of NADPH oxidase reduces myocardial oxidative stress and apoptosis and improves cardiac function in heart failure after myocardial infarction. |journal=Free Radic. Biol. Med. |volume=43 |issue= 2 |pages= 271-81 |year= 2007 |pmid= 17603936 |doi= 10.1016/j.freeradbiomed.2007.04.021 }}
*{{cite journal  | vauthors=Qin F, Simeone M, Patel R |title=Inhibition of NADPH oxidase reduces myocardial oxidative stress and apoptosis and improves cardiac function in heart failure after myocardial infarction |journal=Free Radic. Biol. Med. |volume=43 |issue= 2 |pages= 271–81 |year= 2007 |pmid= 17603936 |doi= 10.1016/j.freeradbiomed.2007.04.021 }}
}}
}}
{{refend}}
{{refend}}


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[[Category:EF-hand-containing proteins]]
 
 
{{gene-15-stub}}

Latest revision as of 13:11, 5 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

NADPH oxidase, EF-hand calcium binding domain 5, also known as NOX5, is a protein which in humans is encoded by the NOX5 gene.[1][2]

Function

NOX5 is a novel NADPH oxidase that generates superoxide.[1]

Nox5 interacts with c-abl, superoxide production leads to phosphorylation of c-abl, while inhibition of c-abl kinase activity inhibits Nox5 superoxide production.[3]

References

  1. ↑ 1.0 1.1 "Entrez Gene: NOX5 NADPH oxidase, EF-hand calcium binding domain 5".
  2. ↑ Bánfi B, Molnár G, Maturana A, Steger K, Hegedûs B, Demaurex N, Krause KH (October 2001). "A Ca(2+)-activated NADPH oxidase in testis, spleen, and lymph nodes". J. Biol. Chem. 276 (40): 37594–601. doi:10.1074/jbc.M103034200. PMID 11483596.
  3. ↑ El Jamali A, Valente AJ, Lechleiter JD, Gamez MJ, Pearson DW, Nauseef WM, Clark RA (March 2008). "NOVEL REDOX-DEPENDENT REGULATION OF NOX5 BY THE TYROSINE KINASE C-ABL". Free Radic. Biol. Med. 44 (5): 868–81. doi:10.1016/j.freeradbiomed.2007.11.020. PMC 2278123. PMID 18160052.

Further reading


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