DUOX1
entrez
53905
canonical
uniprot
Q9NRD9
canonical
ensembl
ENSG00000137857
resolver
ensp
ENSP00000317997
resolver
ensp
ENSP00000373689
resolver
ensp
ENSP00000454065
resolver
ensp
ENSP00000555406
resolver
genesymbol
DUOX1
resolver
genesymbol_syn
DUOX
resolver
genesymbol_syn
LNOX1
resolver
genesymbol_syn
THOX1
resolver
hgnc
HGNC:3062
resolver
uniprot
A6NH28
resolver
uniprot
Q14C94
resolver
uniprot
Q6ZMB3
resolver
uniprot
Q6ZR09
resolver
uniprot
Q9NZC1
resolver
uniprot_entry
DUOX1_HUMAN
resolver
uniprot_sec
A6NH28
resolver
uniprot_sec
Q14C94
resolver
uniprot_sec
Q6ZMB3
resolver
uniprot_sec
Q6ZR09
resolver
uniprot_sec
Q9NZC1
resolver
activity_regulation
ACTIVITY REGULATION: The NADPH oxidase activity is calcium-dependent (PubMed:11514595). It is activated by release of cellular ATP which is promoted by bacterial infection (PubMed:19386603). Peroxidase activity is inhibited by aminobenzohydrazide (PubMed:15972824). {ECO:0000269|PubMed:11514595, ECO:0000269|PubMed:15972824, ECO:0000269|PubMed:19386603}.
uniprot
proteins
amino_acid_sequence
MGFCLALAWTLLVGAWTPLGAQNPISWEVQRFDGWYNNLMEHRWGSKGSRLQRLVPASYADGVYQPLGEPHLPNPRDLSNTISRGPAGLASLRNRTVLGVFFGYHVLSDLVSVETPGCPAEFLNIRIPPGDPMFDPDQRGDVVLPFQRSRWDPETGRSPSNPRDPANQVTGWLDGSAIYGSSHSWSDALRSFSRGQLASGPDPAFPRDSQNPLLMWAAPDPATGQNGPRGLYAFGAERGNREPFLQALGLLWFRYHNLWAQRLARQHPDWEDEELFQHARKRVIATYQNIAVYEWLPSFLQKTLPEYTGYRPFLDPSISSEFVAASEQFLSTMVPPGVYMRNASCHFQGVINRNSSVSRALRVCNSYWSREHPSLQSAEDVDALLLGMASQIAEREDHVLVEDVRDFWPGPLKFSRTDHLASCLQRGRDLGLPSYTKARAALGLSPITRWQDINPALSRSNDTVLEATAALYNQDLSWLELLPGGLLESHRDPGPLFSTIVLEQFVRLRDGDRYWFENTRNGLFSKKEIEEIRNTTLQDVLVAVINIDPSALQPNVFVWHKGDPCPQPRQLSTEGLPACAPSVVRDYFEGSGFGFGVTIGTLCCFPLVSLLSAWIVARLRMRNFKRLQGQDRQSIVSEKLVGGMEALEWQGHKEPCRPVLVYLQPGQIRVVDGRLTVLRTIQLQPPQKVNFVLSSNRGRRTLLLKIPKEYDLVLLFNLEEERQALVENLRGALKESGLSIQEWELREQELMRAAVTREQRRHLLETFFRHLFSQVLDINQADAGTLPLDSSQKVREALTCELSRAEFAESLGLKPQDMFVESMFSLADKDGNGYLSFREFLDILVVFMKGSPEEKSRLMFRMYDFDGNGLISKDEFIRMLRSFIEISNNCLSKAQLAEVVESMFRESGFQDKEELTWEDFHFMLRDHNSELRFTQLCVKGVEVPEVIKDLCRRASYISQDMICPSPRVSARCSRSDIETELTPQRLQCPMDTDPPQEIRRRFGKKVTSFQPLLFTEAHREKFQRSCLHQTVQQFKRFIENYRRHIGCVAVFYAIAGGLFLERAYYYAFAAHHTGITDTTRVGIILSRGTAASISFMFSYILLTMCRNLITFLRETFLNRYVPFDAAVDFHRLIASTAIVLTVLHSVGHVVNVYLFSISPLSVLSCLFPGLFHDDGSELPQKYYWWFFQTVPGLTGVVLLLILAIMYVFASHHFRRRSFRGFWLTHHLYILLYVLLIIHGSFALIQLPRFHIFFLVPAIIYGGDKLVSLSRKKVEISVVKAELLPSGVTHLRFQRPQGFEYKSGQWVRIACLALGTTEYHPFTLTSAPHEDTLSLHIRAAGPWTTRLREIYSAPTGDRCARYPKLYLDGPFGEGHQEWHKFEVSVLVGGGIGVTPFASILKDLVFKSSVSCQVFCKKIYFIWVTRTQRQFEWLADIIREVEENDHQDLVSVHIYITQLAEKFDLRTTMLYICERHFQKVLNRSLFTGLRSITHFGRPPFEPFFNSLQEVHPQVRKIGVFSCGPPGMTKNVEKACQLINRQDRTHFSHHYENF
uniprot
proteins
ec_number
1.-.-.-
uniprot
proteins
ec_number
1.11.1.-
uniprot
proteins
ec_number
1.6.3.1
uniprot
proteins
function
FUNCTION: Generates hydrogen peroxide (H2O2) which is required for the activity of thyroid peroxidase/TPO and lactoperoxidase/LPO (PubMed:10806195, PubMed:15972824). Plays a role in thyroid hormone synthesis (PubMed:10806195). Also required for lactoperoxidase-mediated antimicrobial defense at the surface of mucosa (PubMed:12824283). Antimicrobial agent hypothiocyanite (OSCN-), which is produced by LPO from DUOX1-derived H2O2, promotes influenza virus inactivation by reducing viral binding to and entry into host cells (PubMed:34168077). Promotes antiviral immunity by increasing airway cytokine levels, promoting innate immune cell recruitment and reducing airway epithelial cell apoptosis (By similarity). In response to bacterial stimuli, activated by ATP and promotes EGFR/ERK signaling, ADAM17 activation, and EGFR ligand shedding, leading to enhanced CXCL8/IL8 expression and secretion in airway epithelia (PubMed:19386603). Synthesizes NAADP from its reduced NAADPH form which promotes Ca(2+) signaling during T cell activation (PubMed:34784249). In addition to its oxidase activity, has also been shown to have peroxidase activity through its N-terminal peroxidase-like domain (PubMed:11514595). However, another study showed that the isolated peroxidase-like domain does not bind heme and has no intrinsic peroxidase activity (PubMed:19460756). {ECO:0000250|UniProtKB:A2AQ92, ECO:0000269|PubMed:10806195, ECO:0000269|PubMed:11514595, ECO:0000269|PubMed:12824283, ECO:0000269|PubMed:15972824, ECO:0000269|PubMed:19386603, ECO:0000269|PubMed:19460756, ECO:0000269|PubMed:34168077, ECO:0000269|PubMed:34784249}.
uniprot
proteins
mass_dalton
177235
uniprot
proteins
mutagenesis
MUTAGEN 50; /note="R->E: Severely reduces tetramer formation."; /evidence="ECO:0000269|PubMed:33420071"; MUTAGEN 109; /note="D->A: Fails to assemble with DUOXA1; when associated with A-174."; /evidence="ECO:0000269|PubMed:33420071"; MUTAGEN 174; /note="D->A: Fails to assemble with DUOXA1; when associated with A-109."; /evidence="ECO:0000269|PubMed:33420071"; MUTAGEN 332; /note="T->A: Fails to assemble with DUOXA1; when associated with A-397."; /evidence="ECO:0000269|PubMed:33420071"; MUTAGEN 397; /note="D->A: Fails to assemble with DUOXA1; when associated with A-332."; /evidence="ECO:0000269|PubMed:33420071"; MUTAGEN 507; /note="R->E: Severely reduces tetramer formation."; /evidence="ECO:0000269|PubMed:33420071
uniprot
proteins
pathway_participation
PATHWAY: Hormone biosynthesis; thyroid hormone biosynthesis.
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000269|PubMed:11822874}.
uniprot
proteins
protein_family
Peroxidase family
uniprot
proteins
pubmed
10806195
uniprot
proteins
pubmed
11514595
uniprot
proteins
pubmed
11822874
uniprot
proteins
pubmed
12824283
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15210697
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15561711
uniprot
proteins
pubmed
15972824
uniprot
proteins
pubmed
16111680
uniprot
proteins
pubmed
16572171
uniprot
proteins
pubmed
19386603
uniprot
proteins
pubmed
19460756
uniprot
proteins
pubmed
33420071
uniprot
proteins
pubmed
34168077
uniprot
proteins
pubmed
34784249
uniprot
proteins
pubmed
34845039
uniprot
proteins
pubmed
39126279
uniprot
proteins
sequence_length
1551
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:10806195, ECO:0000269|PubMed:15210697, ECO:0000269|PubMed:34784249, ECO:0000269|PubMed:39126279}; Multi-pass membrane protein {ECO:0000269|PubMed:33420071}. Note=Localizes to the apical membrane of epithelial cells. {ECO:0000269|PubMed:15210697}.
uniprot
proteins
transmembrane_region
TRANSMEM 592..616; /note="Helical"; /evidence="ECO:0000269|PubMed:33420071, ECO:0007744|PDB:7D3F"; TRANSMEM 1044..1066; /note="Helical"; /evidence="ECO:0000269|PubMed:33420071, ECO:0007744|PDB:7D3F"; TRANSMEM 1081..1105; /note="Helical"; /evidence="ECO:0000269|PubMed:33420071, ECO:0007744|PDB:7D3F"; TRANSMEM 1128..1152; /note="Helical"; /evidence="ECO:0000269|PubMed:33420071, ECO:0007744|PDB:7D3F"; TRANSMEM 1185..1210; /note="Helical"; /evidence="ECO:0000269|PubMed:33420071, ECO:0007744|PDB:7D3F"; TRANSMEM 1223..1241; /note="Helical"; /evidence="ECO:0000269|PubMed:33420071, ECO:0007744|PDB:7D3F"; TRANSMEM 1249..1262; /note="Helical"; /evidence="ECO:0000269|PubMed:33420071, ECO:0007744|PDB:7D3F
uniprot
proteins