Detail Information for IndEnz0018000779
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