Dual oxidase 2

DUOX2
Identifiers
Aliases	DUOX2, LNOX2, NOXEF2, P138-TOX, TDH6, THOX2, dual oxidase 2
External IDs	MGI: 3036280 HomoloGene: 9689 GeneCards: DUOX2
Gene location (Human) Chr. Chromosome 15 (human) Band 15q21.1 Start 45,092,650 bp End 45,114,344 bp
Gene location (Mouse) Chr. Chromosome 2 (mouse) Band 2|2 E5 Start 122,279,247 bp End 122,298,165 bp
RNA expression pattern More reference expression data
Gene ontology Molecular function • calcium ion binding • peroxidase activity • metal ion binding • heme binding • oxidoreductase activity • NAD(P)H oxidase activity Cellular component • integral component of membrane • membrane • plasma membrane • cell junction • apical plasma membrane • extracellular exosome Biological process • cuticle development • bone mineralization • multicellular organism growth • cytokine-mediated signaling pathway • cellular oxidant detoxification • response to virus • response to oxidative stress • thyroid hormone metabolic process • thyroid hormone generation • thyroid gland development • hydrogen peroxide catabolic process • fertilization • inner ear development • response to cAMP • adenohypophysis morphogenesis • oxidation-reduction process • hormone metabolic process • hormone biosynthetic process • hydrogen peroxide biosynthetic process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	50506	214593
Ensembl	ENSG00000140279	ENSMUSG00000068452
UniProt	Q9NRD8	A2AQ99
RefSeq (mRNA)	NM_014080	NM_177610
RefSeq (protein)	NP_054799	NP_808278
Location (UCSC)	Chr 15: 45.09 – 45.11 Mb	Chr 15: 122.28 – 122.3 Mb
PubMed search

50506

214593

ENSG00000140279

ENSMUSG00000068452

Q9NRD8

A2AQ99

NM_014080

NM_177610

NP_054799

NP_808278

Dual oxidase 2, also known as DUOX2 or ThOX2 (for thyroid oxidase) is an enzyme which in humans is encoded by the DUOX2 gene. Dual oxidase is an enzyme that was first identified in the mammalian thyroid gland. In humans, two isoforms are found; hDUOX1 and hDUOX2 (this enzyme). The protein location is not exclusive to thyroid tissue; hDUOX1 is prominent in airway epithelial cells and hDUOX2 in the salivary glands and gastrointestinal tract.

Investigations into reactive oxygen species (ROS) in biological systems have, until recently, focused on characterization of phagocytic cell processes. It is now well accepted that production of such species is not restricted to phagocytic cells and can occur in eukaryotic non-phagocytic cell types via NADPH oxidase (NOX) or dual oxidase (DUOX). This new family of proteins, termed the NOX/DUOX family or NOX family of NADPH oxidases, consists of homologs to the catalytic moiety of phagocytic NADPH-oxidase, gp91^phox. Members of the NOX/DUOX family have been found throughout eukaryotic species, including invertebrates, insects, nematodes, fungi, amoeba, alga, and plants (not found in prokaryotes). These enzymes clearly demonstrate regulated production of ROS as their sole function. Genetic analyses have implicated NOX/DUOX derived ROS in biological roles and pathological conditions including hypertension (NOX1), innate immunity (NOX2/DUOX), otoconia formation in the inner ear (NOX3) and thyroid hormone biosynthesis (DUOX1/2). It has been suggested that DUOX2 is the isoform to generate H₂O₂ utilized by thyroid peroxidase (TPO) for the biosynthesis of thyroid hormones, supported by the discovery of congenital hypothyroidism resultant from an inactivating mutation in the DUOX2 gene.

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Wikipedia