| IED ID | IndEnz0018000371 |
| Enzyme Type ID | peroxidase000371 |
| Protein Name |
Dual oxidase 1 EC 1.11.1.- EC 1.6.3.1 Large NOX 1 Long NOX 1 NADPH thyroid oxidase 1 Thyroid oxidase 1 |
| Gene Name | DUOX1 DUOX LNOX1 THOX1 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MGFCLALAWTLLVGAWTPLGAQNPISWEVQRFDGWYNNLMEHRWGSKGSRLQRLVPASYADGVYQPLGEPHLPNPRDLSNTISRGPAGLASLRNRTVLGVFFGYHVLSDLVSVETPGCPAEFLNIRIPPGDPMFDPDQRGDVVLPFQRSRWDPETGRSPSNPRDPANQVTGWLDGSAIYGSSHSWSDALRSFSRGQLASGPDPAFPRDSQNPLLMWAAPDPATGQNGPRGLYAFGAERGNREPFLQALGLLWFRYHNLWAQRLARQHPDWEDEELFQHARKRVIATYQNIAVYEWLPSFLQKTLPEYTGYRPFLDPSISSEFVAASEQFLSTMVPPGVYMRNASCHFQGVINRNSSVSRALRVCNSYWSREHPSLQSAEDVDALLLGMASQIAEREDHVLVEDVRDFWPGPLKFSRTDHLASCLQRGRDLGLPSYTKARAALGLSPITRWQDINPALSRSNDTVLEATAALYNQDLSWLELLPGGLLESHRDPGPLFSTIVLEQFVRLRDGDRYWFENTRNGLFSKKEIEEIRNTTLQDVLVAVINIDPSALQPNVFVWHKGDPCPQPRQLSTEGLPACAPSVVRDYFEGSGFGFGVTIGTLCCFPLVSLLSAWIVARLRMRNFKRLQGQDRQSIVSEKLVGGMEALEWQGHKEPCRPVLVYLQPGQIRVVDGRLTVLRTIQLQPPQKVNFVLSSNRGRRTLLLKIPKEYDLVLLFNLEEERQALVENLRGALKESGLSIQEWELREQELMRAAVTREQRRHLLETFFRHLFSQVLDINQADAGTLPLDSSQKVREALTCELSRAEFAESLGLKPQDMFVESMFSLADKDGNGYLSFREFLDILVVFMKGSPEEKSRLMFRMYDFDGNGLISKDEFIRMLRSFIEISNNCLSKAQLAEVVESMFRESGFQDKEELTWEDFHFMLRDHNSELRFTQLCVKGVEVPEVIKDLCRRASYISQDMICPSPRVSARCSRSDIETELTPQRLQCPMDTDPPQEIRRRFGKKVTSFQPLLFTEAHREKFQRSCLHQTVQQFKRFIENYRRHIGCVAVFYAIAGGLFLERAYYYAFAAHHTGITDTTRVGIILSRGTAASISFMFSYILLTMCRNLITFLRETFLNRYVPFDAAVDFHRLIASTAIVLTVLHSVGHVVNVYLFSISPLSVLSCLFPGLFHDDGSELPQKYYWWFFQTVPGLTGVVLLLILAIMYVFASHHFRRRSFRGFWLTHHLYILLYVLLIIHGSFALIQLPRFHIFFLVPAIIYGGDKLVSLSRKKVEISVVKAELLPSGVTHLRFQRPQGFEYKSGQWVRIACLALGTTEYHPFTLTSAPHEDTLSLHIRAAGPWTTRLREIYSAPTGDRCARYPKLYLDGPFGEGHQEWHKFEVSVLVGGGIGVTPFASILKDLVFKSSVSCQVFCKKIYFIWVTRTQRQFEWLADIIREVEENDHQDLVSVHIYITQLAEKFDLRTTMLYICERHFQKVLNRSLFTGLRSITHFGRPPFEPFFNSLQEVHPQVRKIGVFSCGPPGMTKNVEKACQLINRQDRTHFSHHYENF |
| Enzyme Length | 1551 |
| Uniprot Accession Number | Q9NRD9 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: The NADPH oxidase activity is calcium-dependent. Peroxidase activity is inhibited by aminobenzohydrazide. {ECO:0000269|PubMed:11514595, ECO:0000269|PubMed:15972824}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=H(+) + NADH + O2 = H2O2 + NAD(+); Xref=Rhea:RHEA:11264, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.3.1; Evidence={ECO:0000269|PubMed:11514595, ECO:0000269|PubMed:15972824}; CATALYTIC ACTIVITY: Reaction=H(+) + NADPH + O2 = H2O2 + NADP(+); Xref=Rhea:RHEA:11260, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.3.1; Evidence={ECO:0000269|PubMed:11514595, ECO:0000269|PubMed:15972824}; |
| DNA Binding | |
| EC Number | 1.11.1.-; 1.6.3.1 |
| Enzyme Function | FUNCTION: Generates hydrogen peroxide which is required for the activity of thyroid peroxidase/TPO and lactoperoxidase/LPO. Plays a role in thyroid hormones synthesis and lactoperoxidase-mediated antimicrobial defense at the surface of mucosa. May have its own peroxidase activity through its N-terminal peroxidase-like domain. {ECO:0000269|PubMed:11514595, ECO:0000269|PubMed:12824283}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Hormone biosynthesis; thyroid hormone biosynthesis. |
| nucleotide Binding | |
| Features | Alternative sequence (2); Beta strand (38); Chain (1); Compositional bias (1); Domain (5); Erroneous initiation (1); Erroneous termination (1); Glycosylation (5); Helix (59); Metal binding (9); Natural variant (3); Region (3); Sequence conflict (2); Signal peptide (1); Topological domain (8); Transmembrane (7); Turn (13) |
| Keywords | 3D-structure;Alternative splicing;Calcium;Cell membrane;FAD;Flavoprotein;Glycoprotein;Hydrogen peroxide;Membrane;Metal-binding;NADP;Oxidoreductase;Peroxidase;Reference proteome;Repeat;Signal;Thyroid hormones biosynthesis;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | INDUCTION: By forskolin (at protein level). By thyrotropin and the Th2-specific cytokines IL-4 and IL-13. {ECO:0000269|PubMed:10806195, ECO:0000269|PubMed:16111680}. |
| Subcellular Location | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:10806195, ECO:0000269|PubMed:15210697}; Multi-pass membrane protein {ECO:0000269|PubMed:10806195, ECO:0000269|PubMed:15210697}. Note=Localizes to the apical membrane of epithelial cells. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000269|PubMed:11822874}. |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | Electron microscopy (2) |
| Cross Reference PDB | 7D3E; 7D3F; |
| Mapped Pubmed ID | 12482831; 15062544; 15640347; 15677770; 16478776; 16608528; 17135261; 17337509; 18177232; 18281478; 18606821; 19144650; 19339556; 19460756; 19730683; 19952225; 20056178; 20085766; 20346360; 20682913; 21389273; 21411736; 21915726; 23225414; 23281318; 23349873; 23362256; 23691121; 24128054; 24161126; 24164541; 24332816; 24624333; 25164816; 25586178; 25848056; 26597162; 27079415; 27108801; 27110716; 27262981; 28633507; 28982074; 29405261; 30375286; 31706280; 32764116; 33301419; 33309621; 33420071; 33563887; 34784249; |
| Motif | |
| Gene Encoded By | |
| Mass | 177,235 |
| Kinetics | |
| Metal Binding | METAL 828; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 830; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 832; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 834; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 839; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 864; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 866; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 868; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 875; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448 |
| Rhea ID | RHEA:11264; RHEA:11260 |
| Cross Reference Brenda | 1.6.3.1; |