| IED ID | IndEnz0018000524 |
| Enzyme Type ID | peroxidase000524 |
| Protein Name |
Dual oxidase 2 EC 1.11.1.- EC 1.6.3.1 Large NOX 2 Long NOX 2 NADH/NADPH thyroid oxidase p138-tox NADPH oxidase/peroxidase DUOX2 NADPH thyroid oxidase 2 Thyroid oxidase 2 p138 thyroid oxidase |
| Gene Name | DUOX2 LNOX2 THOX2 |
| 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 | MLRARPEALMLLGALLTGSLGPSGNQDALSLPWEVQRYDGWFNNLRHHERGAVGCRLQRRVPANYADGVYQALEEPQLPNPRRLSNAATRGIAGLPSLHNRTVLGVFFGYHVLSDVVSVETPGCPAEFLNIRIPPGDPVFDPDQRGDVVLPFQRSRWDPETGRSPSNPRDLANQVTGWLDGSAIYGSSHSWSDALRSFSGGQLASGPDPAFPRDSQNPLLMWAAPDPATGQNGPRGLYAFGAERGNREPFLQALGLLWFRYHNLWAQRLARQHPDWEDEELFQHARKRVIATYQNIAVYEWLPSFLQKTLPEYTGYRPFLDPSISPEFVVASEQFFSTMVPPGVYMRNASCHFRKVLNKGFQSSQALRVCNNYWIRENPNLNSTQEVNELLLGMASQISELEDNIVVEDLRDYWPGPGKFSRTDYVASSIQRGRDMGLPSYSQALLAFGLDIPRNWSDLNPNVDPQVLEATAALYNQDLSQLELLLGGLLESHGDPGPLFSAIVLDQFVRLRDGDRYWFENTRNGLFSKKEIEDIRNTTLRDVLVAVINIDPSALQPNVFVWHKGAPCPQPKQLTTDGLPQCAPLTVLDFFEGSSPGFAITIIALCCLPLVSLLLSGVVAYFRGREHKKLQKKLKESVKKEAAKDGVPAMEWPGPKERSSPIIIQLLSDRCLQVLNRHLTVLRVVQLQPLQQVNLILSNNRGCRTLLLKIPKEYDLVLLFSSEEERGAFVQQLWDFCVRWALGLHVAEMSEKELFRKAVTKQQRERILEIFFRHLFAQVLDINQADAGTLPLDSSQKVREALTCELSRAEFAESLGLKPQDMFVESMFSLADKDGNGYLSFREFLDILVVFMKGSPEDKSRLMFTMYDLDENGFLSKDEFFTMMRSFIEISNNCLSKAQLAEVVESMFRESGFQDKEELTWEDFHFMLRDHDSELRFTQLCVKGGGGGGNGIRDIFKQNISCRVSFITRTPGERSHPQGLGPPAPEAPELGGPGLKKRFGKKAAVPTPRLYTEALQEKMQRGFLAQKLQQYKRFVENYRRHIVCVAIFSAICVGVFADRAYYYGFASPPSDIAQTTLVGIILSRGTAASVSFMFSYILLTMCRNLITFLRETFLNRYVPFDAAVDFHRWIAMAAVVLAILHSAGHAVNVYIFSVSPLSLLACIFPNVFVNDGSKLPQKFYWWFFQTVPGMTGVLLLLVLAIMYVFASHHFRRRSFRGFWLTHHLYILLYALLIIHGSYALIQLPTFHIYFLVPAIIYGGDKLVSLSRKKVEISVVKAELLPSGVTYLQFQRPQGFEYKSGQWVRIACLALGTTEYHPFTLTSAPHEDTLSLHIRAVGPWTTRLREIYSSPKGNGCAGYPKLYLDGPFGEGHQEWHKFEVSVLVGGGIGVTPFASILKDLVFKSSLGSQMLCKKIYFIWVTRTQRQFEWLADIIQEVEENDHQDLVSVHIYVTQLAEKFDLRTTMLYICERHFQKVLNRSLFTGLRSITHFGRPPFEPFFNSLQEVHPQVRKIGVFSCGPPGMTKNVEKACQLVNRQDRAHFMHHYENF |
| Enzyme Length | 1548 |
| Uniprot Accession Number | Q9NRD8 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Peroxidase activity is inhibited by aminobenzohydrazide (By similarity). The NADPH oxidase activity is calcium-dependent. {ECO:0000250, 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: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: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:12824283}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Hormone biosynthesis; thyroid hormone biosynthesis. |
| nucleotide Binding | |
| Features | Chain (1); Disulfide bond (3); Domain (5); Glycosylation (5); Metal binding (9); Natural variant (8); Region (3); Sequence conflict (3); Signal peptide (1); Topological domain (7); Transmembrane (7) |
| Keywords | Calcium;Cell junction;Cell membrane;Congenital hypothyroidism;Disease variant;Disulfide bond;FAD;Flavoprotein;Glycoprotein;Hydrogen peroxide;Membrane;Metal-binding;NADP;Oxidoreductase;Peroxidase;Reference proteome;Repeat;Signal;Thyroid hormones biosynthesis;Transmembrane;Transmembrane helix |
| Interact With | Q1HG44 |
| Induction | INDUCTION: By forskolin, thyrotropin and the Th1-specific cytokine IFNG/IFN-gamma. {ECO:0000269|PubMed:10806195}. |
| Subcellular Location | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:15591162, ECO:0000269|PubMed:26301257}; Multi-pass membrane protein {ECO:0000269|PubMed:15591162}. Cell junction {ECO:0000269|PubMed:26301257}. Note=Localizes to the apical membrane of epithelial cells. Localizes on internal membrane structures under resting conditions, translocates to the plasma membrane and cell-cell junctions upon challenge with enteric pathogens, such as Escherichia coli. {ECO:0000269|PubMed:26301257}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000269|PubMed:11822874}. |
| Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 15150274; 15677770; 16111680; 16478776; 16608528; 16651268; 17374849; 17684392; 18177232; 18281478; 18765513; 19144650; 19339556; 19759286; 19789206; 19913121; 19952225; 20056178; 20346360; 20381453; 20511343; 20531308; 20628086; 21148036; 21321110; 21565790; 21704604; 21714724; 21915726; 22336364; 22523549; 22592922; 22814254; 23010498; 23225414; 23281318; 23296709; 23362256; 23404210; 23457309; 23545780; 24127536; 24128054; 24161126; 24423310; 24492313; 24735383; 25003194; 25248169; 25263060; 25586178; 25616291; 26046128; 26056003; 26174504; 26207686; 26261005; 26349762; 26506010; 26565538; 26709262; 26742565; 26823467; 27048452; 27110716; 27166716; 27282560; 27349010; 27373512; 27498126; 27557340; 27637085; 28541007; 28633507; 28666341; 28683258; 29092890; 29320567; 29715584; 30375286; 31030636; 31044655; 31501191; 31513783; 31706280; 32207419; 32425884; 32531052; 33488516; 33628596; 33631011; 33651715; 33748270; 34564849; 34784249; 34966441; |
| Motif | |
| Gene Encoded By | |
| Mass | 175,364 |
| Kinetics | |
| Metal Binding | METAL 832; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 834; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 836; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 838; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 843; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 868; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 870; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 872; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 879; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448 |
| Rhea ID | RHEA:11264; RHEA:11260 |
| Cross Reference Brenda | 1.6.3.1; |