Literature summary for 1.6.3.1 extracted from

Grasberger, H.; De Deken, X.; Miot, F.; Pohlenz, J.; Refetoff, S.
Missense mutations of dual oxidase 2 (DUOX2) implicated in congenital hypothyroidism have impaired trafficking in cells reconstituted with DUOX2 maturation factor (2007), Mol. Endocrinol., 21, 1408-1421.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in HeLa cell	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
D506N	naturally occuring missense mutation. Mutant display a partial deficiency phenotype with reduced surface expression of protein with normal intrinsic activity in generating H2O2. N-glycan moieties of the mutant protein are not subject to normal modification in the Golgi apparatus	Homo sapiens
Q36H	naturally occuring missense mutation. Mutation completely prevents routing of the protein to the cell surface. Protein is predominantly present as core N-glycosylated, thiol-reduced folding intermediate and retained within the endoplasmic reticulum	Homo sapiens
R376W	naturally occuring missense mutation. Mutation completely prevents routing of the protein to the cell surface. Protein is predominantly present as core N-glycosylated, thiol-reduced folding intermediate and retained within the endoplasmic reticulum	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
plasma membrane	-	Homo sapiens	5886	-

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	isoform dual oxidase 2	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	-	Homo sapiens
additional information	oxidative folding of wild-type protein in the endoplasmic reticulum is the rate-limiting step in the maturation, which is not faciltated by the speific maturation factor DUOXA2. DUOXA2 may allow for rapid exit of folded protein from the endoplasmatic reticulum or enahnced degradation of mutant protein	Homo sapiens

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Release 2023.1 (January 2023)