| IED ID | IndEnz0018001008 |
| Enzyme Type ID | peroxidase001008 |
| Protein Name |
Dual oxidase 2 EC 1.11.1.- EC 1.6.3.1 NADH/NADPH thyroid oxidase p138-tox |
| Gene Name | DUOX2 |
| Organism | Sus scrofa (Pig) |
| 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 Laurasiatheria Artiodactyla Suina Suidae (pigs) Sus Sus scrofa (Pig) |
| Enzyme Sequence | MLCIRPEALVLLGALLTVPLDPVGGQDALSLTWEVQRYDGWFNNLRQHEHGAAGSPLRRLVPANYADGVYQALGEPLLPNPRQLSHTTMRGPAGLRSIRNRTVLGVFFGYHVLSDLVSIEKPGCPAEFLNIHIPPGDPVFDPHKSGDVVLPFQRSRWDPNTGQSPSNPRDLTNEVTGWLDGSAIYGSSHSWSDELRSFSGGQLASGPDPAFPRQAQDPLFMWTPPDPATGQRGPQGLYAFGAEQGNREPFLQALGLLWFRYHNLCAQKLAREHPLWGDEELFQHARKRVIATYQSITMYEWLPSFLQQTPPNYTEYRPFLDPSISPEFLAASEQFFSTMVPPGVYMRNASCHFQMVLNESYGSFPALRVCNSYWIRENPNLNSAEAVNQLLLGMASQISELEDWIVVEDLRDYWPGPGKFSRTDYVASSIQRGRDMGLPSYTQALQALGLNTPKNWSDFNPNVDPQVLEATAALYNQDLSRLELFSGGLLESYGDPGPLFSTIVLDQFVRLRDGDRYWFENTKNGLFSKEEIAEIRSTTLRDVLVAVTNVSSSALQPNVFIWNEDSPCPQPQQLTTEDLPHCVPLTVIQYFEGSGPGFGITIVALCCLPLMSLLISGVVAYFRSRERKKLQKRGKESVKKEADKDGVSAMEWPGPKERSYPVSIQLLPDRHLQVLDRHLSVLRTIQLRPRHRVNLILSNNLGRRTLLLKIPKEYDLVLLFNSEDERGAFVQHLQGFCASCALGLDIDEMGESELFRKAVTKQQRGRILEIFFRHLFAQVLDIDQADAGALPLDSSQKVREALTCELSRAEFAESLGLKPQDMFVESMFSLADKDGNGYLSFREFLDVLVVFMKGSPEDKSRLMFTMYDLDGNGFLSKDEFFTMIRSFIEISNNCLSKAQLTEVVESMFREAGFQDKQELTWEDFHFMLRDHDSELRHTQLCVKGGGGGVGVIFKPDISSRVSFIIRTPEERSSPQGVRLPASEASELGGPVLKKRFGKKAVVPPPRLYTEALQEKKQRGFLAQKLQQYKRFVENYRRHIVCVAIFSAICAGLFVERAYYYAFVSPPSGIAETTFVGIILSRGTAASVSFMFSYILLTMCRNLITFLRETFLNHYVPFDAAVDFHRWIAMAALVLAILHSVGHVVNVYIFSVSPLSLLACVFPSVFVNDGSKLPQKFYWWFFQTIPGMTGVLLLVVLAIMYVFASPYFRRRSFRGFWLTHHFYILLYVLLIIHGSFALIQLPRFHIFFLVPALIYVGDKLVSLSRKKVEISVVKAELLPSGVTHLQFQRPQGFEYKSGQWVRIACLGLGTNEYHPFTLTSAPHEDTLSLHIRAVGPWTTRLREIYSHPMGDGYARYPKLYLDGPFGEGHQEWHKFEVSVLVGGGIGVTPFASILKDLVFKSSLGSQMLCKKIYFIWVTRTQRQFEWLADIIREVEENDHRDLVSVHIYITQLAEKFDLRTTMLYICERHFQKVLNRSLFTGLRSITHFGRPPFEPFFNSLQEVHPQVRKIGVFSCGPPGMTKNVEKTCQLINRQDQTHFVHHYENF |
| Enzyme Length | 1545 |
| Uniprot Accession Number | Q8HZK2 |
| 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; 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. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Hormone biosynthesis; thyroid hormone biosynthesis. |
| nucleotide Binding | |
| Features | Chain (1); Disulfide bond (3); Domain (5); Glycosylation (6); Metal binding (9); Region (2); Sequence conflict (1); Signal peptide (1); Topological domain (8); Transmembrane (7) |
| Keywords | Calcium;Cell junction;Cell membrane;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 | |
| Induction | INDUCTION: By forskolin and down-regulated by iodide (at protein level). By insulin. {ECO:0000269|PubMed:10601291, ECO:0000269|PubMed:12538618, ECO:0000269|PubMed:12639906}. |
| Subcellular Location | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:15591162}; Multi-pass membrane protein {ECO:0000269|PubMed:15591162}. Cell junction {ECO:0000250|UniProtKB:Q9NRD8}. 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. {ECO:0000250|UniProtKB:Q9NRD8}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000269|PubMed:12639906}. |
| Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 175,284 |
| 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; |