| IED ID | IndEnz0018000779 |
| Enzyme Type ID | peroxidase000779 |
| Protein Name |
Dual oxidase 1 EC 1.11.1.- EC 1.6.3.1 |
| Gene Name | Duox1 |
| Organism | Rattus norvegicus (Rat) |
| 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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MAVYSAVAWILLFGVLASLGAQNPVSWEVQRFDGWYNNLMEHRWGSKGSRLQRLVPASYADGVYQPLREPYLPNPRHLSNRVMRGPAGQPSLRNRTVLGVFFGYHVLSDLVSVETPGCPAEFLNIYIPRGDPVFDPDKRGNVVLPFQRSRWDRSTGQSPSNPRDLTNQVTGWLDGSAIYGSSHSWSDTLRSFSGGQLASGPDPAFPRNSQNSLLMWMAPDPATGQGGPQGLYAFGAQRGNREPFLQALGLLWFRYHNLCAKRLAQEHPHWGDEELFQHARKRVIATYQNIAMYEWLPSFLKQTPPEYPGYHPFLDPSISPEFVVASEQFLSTMVPPGVYMRNASCHFQGIANRNSSVSGALRVCNSYWSRENPKLQRAEDVDALLLGMASQIAEREDHLVVEDVQDFWPGPLKFSRTDYLASCLQRGRDLGLPSYTKAREALGLPPVSHWQDINPALSRSNGTVLEATAALYNQDLSRLELLAGGLLESHGDPGPLFSAIVLDQFVRLRDGDRYWFENNRNGLFSKEEIAEIRNTSLRDILVAVTNVDPSALQPSVFFWLAGDPCPQPSQLSTQGLPACAPLFVRDYFKGSGFGFGLTIGTLCCFPLVSLLSAWIVARLRMRNFKRLQRQDRQSIMCEKLVGGVEALEWQGRKEPCRPVLVHLQPGQIRVVDGRLTVLRTIQLRPPQQVNLILSSNRGRRTLLLKIPKEYDLVLLFNMEEERQALVENIRAALKENGLSFQEWELREQELMRAAVTRQQRGHLLETFFRHLFSQVLDINQADAGTLPLDSSTKVREALTCELSRAEFADSLGLKPQDMFVESMFSLADKDGNGYLSFREFLDILVVFMKGSPEEKSRLMFRMYDFDGNGLISKDEFIRMLRSFIEISNNCLSKDQLAEVVESMFRESGFQDKEELTWEDFHFMLRDHDSDLRFTQLCVKGVEVPEVIKNLCRRASYISQEKICPSPRMSAHCARNNTKTASSPQRLQCPVDTDPPQEIRRRFGKKVTSFQPLLFTEAHREKFQRSRRHQTVQQFKRFIENYRRHIGCVAVFYTITGALFLERAYYYAFAAHHSGITDTTRVGIILSRGTAASISFMFSYILLTMCRNLITFLRETFLNRYIPFDAAVDFHRFIASTAIILTVLHSAGHVVNVYLFSISPLSVLSCLFPDLFHDDGSEFPQKYYWWFFQTVPGLTGVLLLLALAIMYVFASHHFRRRSFRGFWLTHHLYIFLYILLIIHGSFALIQMPRFHIFFLVPAIIYVGDKLVSLSRKKVEISVVKAELLPSGVTHLRFQRPQGFEYKSGQWVRIACLALGTTEYHPFTLTSAPHEDTLSLHIRAAGPWTTRLREIYSPPTGDTCARYPKLYLDGPFGEGHQEWHKFEVSVLVGAGIGVTPFASILKDLVFKSSVSCQVFCKKIYFIWVTRTQRQFEWLADIIREVEENDSRDLVSVHIYITQLAEKFDLRTTMLYICERHFQKVLNRSLFTGLRSVTHFGRPPFEPFFNSLQEVHPQVRKIGVFSCGPPGMTKNVEKACQLINKQDRTHFSHHYENF |
| Enzyme Length | 1551 |
| Uniprot Accession Number | Q8CIY2 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: The NADPH oxidase activity is calcium-dependent. Peroxidase activity is inhibited by aminobenzohydrazide (By similarity). {ECO:0000250}. |
| 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; 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; |
| 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. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Hormone biosynthesis; thyroid hormone biosynthesis. |
| nucleotide Binding | |
| Features | Chain (1); Domain (5); Glycosylation (5); Metal binding (9); Region (2); Signal peptide (1); Topological domain (8); Transmembrane (7) |
| Keywords | 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 | |
| Subcellular Location | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Localizes to the apical membrane of epithelial cells. {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 177,197 |
| 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 |