Dual oxidase 1

DUOX1
Identifiers
Aliases	DUOX1, LNOX1, NOXEF1, THOX1, dual oxidase 1
External IDs	MGI: 2139422 HomoloGene: 68136 GeneCards: DUOX1
Gene location (Human) Chr. Chromosome 15 (human) Band 15q21.1 Start 45,129,933 bp End 45,165,576 bp
Gene location (Mouse) Chr. Chromosome 2 (mouse) Band 2|2 E5 Start 122,315,672 bp End 122,347,972 bp
RNA expression pattern More reference expression data
Gene ontology Molecular function • calcium ion binding • peroxidase activity • metal ion binding • heme binding • NADP binding • oxidoreductase activity • NAD(P)H oxidase activity Cellular component • integral component of membrane • membrane • plasma membrane • apical plasma membrane Biological process • cuticle development • cytokine-mediated signaling pathway • cellular oxidant detoxification • response to oxidative stress • reactive oxygen species metabolic process • superoxide anion generation • thyroid hormone generation • hydrogen peroxide catabolic process • hydrogen peroxide biosynthetic process • response to cAMP • oxidation-reduction process • hormone biosynthetic process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	53905	99439
Ensembl	ENSG00000137857	ENSMUSG00000033268
UniProt	Q9NRD9	A2AQ92
RefSeq (mRNA)	NM_017434 NM_175940	NM_001099297
RefSeq (protein)	NP_059130 NP_787954	NP_001092767
Location (UCSC)	Chr 15: 45.13 – 45.17 Mb	Chr 15: 122.32 – 122.35 Mb
PubMed search

53905

99439

ENSG00000137857

ENSMUSG00000033268

Q9NRD9

A2AQ92

NM_017434
NM_175940

NM_001099297

NP_059130
NP_787954

NP_001092767

Dual oxidase 1, also known as DUOX1 or ThOX1 (for thyroid oxidase), is an enzyme which in humans is encoded by the DUOX1 gene. DUOX1 was first identified in the mammalian thyroid gland. In humans, two isoforms are found; hDUOX1 and hDUOX2. Human DUOX protein localization 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). The family currently has seven members including NOX1, NOX2 (formerly known as gp91^phox), NOX3, NOX4, NOX5, DUOX1 (this enzyme) and DUOX2.

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