Literature summary for 1.6.3.1 extracted from

Ameziane-El-Hassani, R.; Morand, S.; Boucher, J.L.; Frapart, Y.M.; Apostolou, D.; Agnandji, D.; Gnidehou, S.; Ohayon, R.; Noel-Hudson, M.S.; Francon, J.; Lalaoui, K.; Virion, A.; Dupuy, C.
Dual oxidase-2 has an intrinsic Ca2+-dependent H2O2-generating activity (2005), J. Biol. Chem., 280, 30046-30054.

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Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
endoplasmic reticulum	partially glycosylated isoform Duox2	Homo sapiens	5783	-
endoplasmic reticulum	partially glycosylated isoform Duox2	Sus scrofa	5783	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	-	Sus scrofa
Ca2+	generation of H2O2 by transfected isoform Duox2 depends on Ca2+	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	isoforms Duox1, Duox2, stable transfection in HEK293 and Chinese hamster ovary cells. Enzymes demonstrate a functional NADPH/Ca2+-dependent H2O2-generating activity. Human Duox2 is more active than human Duox1, but only half as active as its porcine counterpart	-
Sus scrofa	-	isoforms Duox1, Duox2, stable transfection in HEK293 and Chinese hamster ovary cells. Enzymes demonstrate a functional NADPH/Ca2+-dependent H2O2-generating activity. Human Duox2 is only half as active as its porcine counterpart	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	isoform Duox2, partial glycosylation. Post-translational modifications during the maturation process may be implicated in the mechanism of H2O2 formation by favoring intramolecular superoxide dismutation	Homo sapiens

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Release 2023.1 (January 2023)