DUOX1
Dual oxidase 1
Also known as: DUOX1_HUMAN, LNOX1, NOXEF1, THOX1
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q9NRD9
- Gene
- DUOX1
- Ensembl
- ENSG00000137857
- Chromosome
- 15
- Canonical length
- 1551 aa
- Protein class
- Enzymes, Metabolic proteins, Predicted intracellular proteins, Predicted membrane proteins, Transporters
OverviewNCBI Gene
The protein encoded by this gene is a glycoprotein and a member of the NADPH oxidase family. The synthesis of thyroid hormone is catalyzed by a protein complex located at the apical membrane of thyroid follicular cells. This complex contains an iodide transporter, thyroperoxidase, and a peroxide generating system that includes proteins encoded by this gene and the similar DUOX2 gene. This protein is known as dual oxidase because it has both a peroxidase homology domain and a gp91phox domain. This protein generates hydrogen peroxide and thereby plays a role in the activity of thyroid peroxidase, lactoperoxidase, and in lactoperoxidase-mediated antimicrobial defense at mucosal surfaces. Two alternatively spliced transcript variants encoding the same protein have been described for this gene. [provided by RefSeq, Jul 2012]
Canonical amino-acid sequenceUniProt
1551 residues, UniProt reviewed canonical sequence.
>Q9NRD9|DUOX1
1 MGFCLALAWT LLVGAWTPLG AQNPISWEVQ RFDGWYNNLM EHRWGSKGSR LQRLVPASYA
61 DGVYQPLGEP HLPNPRDLSN TISRGPAGLA SLRNRTVLGV FFGYHVLSDL VSVETPGCPA
121 EFLNIRIPPG DPMFDPDQRG DVVLPFQRSR WDPETGRSPS NPRDPANQVT GWLDGSAIYG
181 SSHSWSDALR SFSRGQLASG PDPAFPRDSQ NPLLMWAAPD PATGQNGPRG LYAFGAERGN
241 REPFLQALGL LWFRYHNLWA QRLARQHPDW EDEELFQHAR KRVIATYQNI AVYEWLPSFL
301 QKTLPEYTGY RPFLDPSISS EFVAASEQFL STMVPPGVYM RNASCHFQGV INRNSSVSRA
361 LRVCNSYWSR EHPSLQSAED VDALLLGMAS QIAEREDHVL VEDVRDFWPG PLKFSRTDHL
421 ASCLQRGRDL GLPSYTKARA ALGLSPITRW QDINPALSRS NDTVLEATAA LYNQDLSWLE
481 LLPGGLLESH RDPGPLFSTI VLEQFVRLRD GDRYWFENTR NGLFSKKEIE EIRNTTLQDV
541 LVAVINIDPS ALQPNVFVWH KGDPCPQPRQ LSTEGLPACA PSVVRDYFEG SGFGFGVTIG
601 TLCCFPLVSL LSAWIVARLR MRNFKRLQGQ DRQSIVSEKL VGGMEALEWQ GHKEPCRPVL
661 VYLQPGQIRV VDGRLTVLRT IQLQPPQKVN FVLSSNRGRR TLLLKIPKEY DLVLLFNLEE
721 ERQALVENLR GALKESGLSI QEWELREQEL MRAAVTREQR RHLLETFFRH LFSQVLDINQ
781 ADAGTLPLDS SQKVREALTC ELSRAEFAES LGLKPQDMFV ESMFSLADKD GNGYLSFREF
841 LDILVVFMKG SPEEKSRLMF RMYDFDGNGL ISKDEFIRML RSFIEISNNC LSKAQLAEVV
901 ESMFRESGFQ DKEELTWEDF HFMLRDHNSE LRFTQLCVKG VEVPEVIKDL CRRASYISQD
961 MICPSPRVSA RCSRSDIETE LTPQRLQCPM DTDPPQEIRR RFGKKVTSFQ PLLFTEAHRE
1021 KFQRSCLHQT VQQFKRFIEN YRRHIGCVAV FYAIAGGLFL ERAYYYAFAA HHTGITDTTR
1081 VGIILSRGTA ASISFMFSYI LLTMCRNLIT FLRETFLNRY VPFDAAVDFH RLIASTAIVL
1141 TVLHSVGHVV NVYLFSISPL SVLSCLFPGL FHDDGSELPQ KYYWWFFQTV PGLTGVVLLL
1201 ILAIMYVFAS HHFRRRSFRG FWLTHHLYIL LYVLLIIHGS FALIQLPRFH IFFLVPAIIY
1261 GGDKLVSLSR KKVEISVVKA ELLPSGVTHL RFQRPQGFEY KSGQWVRIAC LALGTTEYHP
1321 FTLTSAPHED TLSLHIRAAG PWTTRLREIY SAPTGDRCAR YPKLYLDGPF GEGHQEWHKF
1381 EVSVLVGGGI GVTPFASILK DLVFKSSVSC QVFCKKIYFI WVTRTQRQFE WLADIIREVE
1441 ENDHQDLVSV HIYITQLAEK FDLRTTMLYI CERHFQKVLN RSLFTGLRSI THFGRPPFEP
1501 FFNSLQEVHP QVRKIGVFSC GPPGMTKNVE KACQLINRQD RTHFSHHYEN FLocalizationUniProt · AlphaFold · HPA
Whether an antibody against DUOX1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Cell surface
- Secreted
- No
- Transmembrane segments
- 7
- Mean surface accessibility (rSASA)
- 0.26
- Highest tissue expression
- 99 nTPM
Expression across tissuesHPA
Tissue
- skin: 99 nTPM
- epididymis: 78 nTPM
- esophagus: 70 nTPM
- cervix: 66 nTPM
- thyroid gland: 59 nTPM
- lung: 46 nTPM
Single-cell type
- esophageal apical cells: 454 nCPM
- alveolar cells type 2: 440 nCPM
- alveolar cells type 1: 386 nCPM
- transitional alveolar cells: 283 nCPM
- esophageal suprabasal cells: 236 nCPM
- respiratory secretory cells: 163 nCPM
Immune cell
- plasmacytoid DC: 0.6 nTPM
- myeloid DC: 0.4 nTPM
- eosinophil: 0.1 nTPM
- intermediate monocyte: 0.1 nTPM
- T-reg: 0.1 nTPM
- basophil: 0 nTPM
Brain region
- cerebellum: 77 nTPM
- cerebral cortex: 15 nTPM
- white matter: 14 nTPM
- hippocampal formation: 13 nTPM
- amygdala: 13 nTPM
- basal ganglia: 13 nTPM
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 0.94
- gnomAD pLI
- 0
- gnomAD missense Z
- 0.89
- DepMap mean gene effect
- -0.03
- DepMap dependency class
- none
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- cuticle development
- cytokine-mediated signaling pathway
- defense response
- hormone biosynthetic process
- hydrogen peroxide biosynthetic process
- hydrogen peroxide catabolic process
- positive regulation of cell motility
- positive regulation of wound healing
- response to cAMP
- response to oxidative stress
- superoxide anion generation
- thyroid hormone generation
Molecular functions
- calcium ion binding
- FAD binding
- heme binding
- NAD(P)H oxidase H2O2-forming activity
- NADP binding
- NADPH binding
- peroxidase activity
- protein heterodimerization activity
- superoxide-generating NAD(P)H oxidase activity
Cellular components
Protein domainsUniProt · Pfam · InterPro
- EF-hand domain
- Haem peroxidase superfamily
- EF-hand domain pair
- FAD-binding 8
- Ferric reductase, NAD binding domain
- Ferric reductase transmembrane component-like domain
- FAD-binding domain, ferredoxin reductase-type
- Riboflavin synthase-like beta-barrel
- EF-Hand 1, calcium-binding site
- Haem peroxidase, animal-type
- Dual oxidase, peroxidase domain
- Haem peroxidase domain superfamily, animal type
- Ferredoxin-NADP reductase (FNR), nucleotide-binding domain
- Respiratory burst oxidase/Ferric reductase
- EF hand domain
- Ferric reductase like transmembrane component
- Animal haem peroxidase
- FAD-binding domain
- Ferric reductase NAD binding domain
- EF-hand domain pair
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of DUOX1 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads DUOX1 as an antibody target. Whether an autoantibody or antibody against DUOX1 could matter depends on whether native DUOX1 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
DUOX1 is annotated at the cell surface, where native DUOX1 is exposed to circulating antibodies and is a prime autoantibody target that could block, deplete, or overstimulate it.
Annotation status
The present source text does not explicitly label DUOX1 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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