| IED ID | IndEnz0018000711 |
| Enzyme Type ID | peroxidase000711 |
| Protein Name |
Thyroid peroxidase TPO EC 1.11.1.8 |
| Gene Name | TPO |
| Organism | Canis lupus familiaris (Dog) (Canis familiaris) |
| 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 Carnivora Caniformia Canidae (dog coyote wolf fox) Canis Canis lupus (Gray wolf) Canis lupus familiaris (Dog) (Canis familiaris) |
| Enzyme Sequence | MVGLVPAGSAWGGRALAVLGVTLLVALARGLLPFFLGGRDLLWGQSGEASVLGVVEESRRVVDGAIQHTVRRDLSKRGLPSPSQLLSFSKLPEPTSRAVSRAAEIMEASVQAVRTRVYGKLGRSWPLTDTLPEAVLDTIANASGCRPHMLPPRCPDTCLARKYRLITGACNNRDHPRWGASNTALARWLPPAYEDGISEPRGWNPHVLYSGFPLPPVREVTRQVIRVPNEAVTEDDQYSDLLTVWGQYIDHDVAFTPQSASGAAFGAGADCQLTCENRSPCFPIQLPPDASGPACLPFSRSSAACGTGIQGAFFGNLSSANPRQQMNGLTSFLDASTVYGSSPALEKQLRNWTSAEGLLRVNTRHWDAGRAHLPFMRPPAPLACVPEPGTRGTAGAPCFLAGDSRASEVPTLAALHTLWLREHNRLASALKALNAHWSADTAYQEARKVVGALHQIITLRDYVPKVLGPEAFQQHVGPYEGYDPTMDPTVSNVFSTAAFRLGHATVHPLVRRLDARFQEHPGLPPLGLQDAFFPWRLLKEGGLDPLLRGLLASPAKLPVQEQLMNEELTERLFVLGSSGSLDLASINLQRGRDHGLPGYNAWREFCGLGRLHTRAELRSAVANATLAGRIMDLYGHPDNIDVWLGGLAEPLLPRARTGPLFACLIGRQMKALRDGDRFWWESSGVFTDEQRRELARHSLSRVICDNTGLPSVPADAFQVSRFPQDFEPCENIPGLNLDVWREALPQGDACGLPDSLDNGDVVLCGEAGRRVLVFSCRHGFKLQGPEQVACSPRGGAVRAPVCRDINECEDASHPPCHGSARCRNTKGGFRCECTDPAVLGEDGTTCVDSGRLPKASLVSIALGIVLVVGLAGLTWTLVCRWAHAGRKASLSIAELGGRGAPPPGRGAGQDGASGSLVPPLGPQGRTRAVDPTSSRSHVAQGSPA |
| Enzyme Length | 944 |
| Uniprot Accession Number | Q8HYB7 |
| Absorption | |
| Active Site | ACT_SITE 251; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298 |
| Activity Regulation | |
| Binding Site | BINDING 250; /note="Heme b; covalent, via 2 links"; /evidence="ECO:0000250"; BINDING 408; /note="Heme b; covalent, via 2 links"; /evidence="ECO:0000250" |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=2 H(+) + H2O2 + 2 iodide = diiodine + 2 H2O; Xref=Rhea:RHEA:23336, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:16382, ChEBI:CHEBI:17606; EC=1.11.1.8; Evidence={ECO:0000250|UniProtKB:P09933}; CATALYTIC ACTIVITY: Reaction=[thyroglobulin]-L-tyrosine + H(+) + H2O2 + iodide = [thyroglobulin]-3-iodo-L-tyrosine + 2 H2O; Xref=Rhea:RHEA:48956, Rhea:RHEA-COMP:12274, Rhea:RHEA-COMP:12275, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:16382, ChEBI:CHEBI:46858, ChEBI:CHEBI:90870; EC=1.11.1.8; Evidence={ECO:0000250|UniProtKB:P09933}; CATALYTIC ACTIVITY: Reaction=[thyroglobulin]-3-iodo-L-tyrosine + H(+) + H2O2 + iodide = [thyroglobulin]-3,5-diiodo-L-tyrosine + 2 H2O; Xref=Rhea:RHEA:48960, Rhea:RHEA-COMP:12275, Rhea:RHEA-COMP:12276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:16382, ChEBI:CHEBI:90870, ChEBI:CHEBI:90871; EC=1.11.1.8; Evidence={ECO:0000250|UniProtKB:P09933}; CATALYTIC ACTIVITY: Reaction=2 [thyroglobulin]-3,5-diiodo-L-tyrosine + H2O2 = [thyroglobulin]-dehydroalanine + [thyroglobulin]-L-thyroxine + 2 H2O; Xref=Rhea:RHEA:48964, Rhea:RHEA-COMP:12276, Rhea:RHEA-COMP:12277, Rhea:RHEA-COMP:12278, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:90871, ChEBI:CHEBI:90872, ChEBI:CHEBI:90873; EC=1.11.1.8; Evidence={ECO:0000250|UniProtKB:P09933}; CATALYTIC ACTIVITY: Reaction=[thyroglobulin]-3,5-diiodo-L-tyrosine + [thyroglobulin]-3-iodo-L-tyrosine + H2O2 = [thyroglobulin]-3,3',5-triiodo-L-thyronine + [thyroglobulin]-dehydroalanine + 2 H2O; Xref=Rhea:RHEA:48968, Rhea:RHEA-COMP:12275, Rhea:RHEA-COMP:12276, Rhea:RHEA-COMP:12278, Rhea:RHEA-COMP:12279, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:90870, ChEBI:CHEBI:90871, ChEBI:CHEBI:90873, ChEBI:CHEBI:90874; EC=1.11.1.8; Evidence={ECO:0000250|UniProtKB:P09933}; |
| DNA Binding | |
| EC Number | 1.11.1.8 |
| Enzyme Function | FUNCTION: Iodination and coupling of the hormonogenic tyrosines in thyroglobulin to yield the thyroid hormones T(3) and T(4). {ECO:0000250|UniProtKB:P09933}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Hormone biosynthesis; thyroid hormone biosynthesis. |
| nucleotide Binding | |
| Features | Active site (1); Binding site (2); Chain (1); Compositional bias (1); Disulfide bond (10); Domain (2); Glycosylation (4); Metal binding (6); Region (1); Sequence conflict (4); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) |
| Keywords | Calcium;Disulfide bond;EGF-like domain;Glycoprotein;Heme;Hydrogen peroxide;Iron;Membrane;Metal-binding;Oxidoreductase;Peroxidase;Reference proteome;Signal;Sushi;Thyroid hormones biosynthesis;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: Heme is covalently bound through a H(2)O(2)-dependent autocatalytic process. Heme insertion is important for the delivery of protein at the cell surface (By similarity). {ECO:0000250}.; PTM: Cleaved in its N-terminal part. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..30; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 101,406 |
| Kinetics | |
| Metal Binding | METAL 252; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 330; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 332; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 334; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 336; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 503; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00298 |
| Rhea ID | RHEA:23336; RHEA:48956; RHEA:48960; RHEA:48964; RHEA:48968 |
| Cross Reference Brenda |