P35419 · PERT_MOUSE
- ProteinThyroid peroxidase
- GeneTpo
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids914 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Iodination and coupling of the hormonogenic tyrosines in thyroglobulin to yield the thyroid hormones T3 and T4.
Catalytic activity
- 2 H+ + H2O2 + 2 iodide = diiodine + 2 H2O
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 Ca2+ ion per heterodimer.
Note: Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per heterodimer.
Pathway
Hormone biosynthesis; thyroid hormone biosynthesis.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 232 | heme b (UniProtKB | ChEBI); covalent | ||||
Sequence: D | ||||||
Active site | 233 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 234 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 313 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 315 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 317 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 319 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Site | 384 | Transition state stabilizer | ||||
Sequence: R | ||||||
Binding site | 387 | heme b (UniProtKB | ChEBI); covalent | ||||
Sequence: E | ||||||
Binding site | 482 | Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cell surface | |
Cellular Component | extracellular space | |
Cellular Component | membrane | |
Cellular Component | mitochondrion | |
Molecular Function | calcium ion binding | |
Molecular Function | heme binding | |
Molecular Function | iodide peroxidase activity | |
Molecular Function | peroxidase activity | |
Biological Process | embryonic hemopoiesis | |
Biological Process | hormone biosynthetic process | |
Biological Process | hydrogen peroxide catabolic process | |
Biological Process | response to oxidative stress | |
Biological Process | thyroid hormone generation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameThyroid peroxidase
- EC number
- Short namesTPO
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP35419
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 32-834 | Extracellular | ||||
Sequence: GKTMKSHVISAVETSQLMVDHAVYNTMKRNLKKREVLSPAQLLSFFKLPESTSGAISRAAEIMETSIQVMKREQSQFSTDALSADILGTIANLSGCLPFMLPPRCPDTCLANKYRPITGACNNRDHPRWGASNTALARWLPPVYEDGFSQPKGWNPNFLYHGFPLPPVREVTRHLIQVSNEAVTEDDQYSDFLPVWGQYIDHDIALTPQSTSTAAFWGGVDCQLTCENQNPCFPIQLPSNSSGTTACLPFYRSSAACGTGDQGALFGNLSAANPRQQMNGLTSFLDASTVYGSSPGVEKQLRNWSSSAGLLRVNTLHLDAGRAYLPFATAACAPEPGTPRTNRTPCFLAGDGRASEVPALAAVHTLWLREHNRLASAFKAINKHWSANTAYQEARKVVGALHQIITMRDYIPKILGPDAFRQYVGPYEGYNPTVNPTVSNIFSTAAFRFGHATVHPLVRRLNTDFQEHTELPRLQLRDVFFRPWRLIQEGGLDPIVRGLLARAAKLQVQGQLMNEELTERLFVLSNVGTLDLASLNLQRGRDHGLPDYNEWREFCGLSRLETPAELNKAIANRSMVNKIMDLYKHADNIDVWLGGLAEKFLPGARTGPLFACIIGKQMKALRDGDRFWWENTNVFTDAQRQELEKHSLPRVICDNTGLTRVPVDAFRIGKFPQDFESCEDIPSMDLELWRETFPQDDKCVFPEEVDNGNFVHCEESGKLVLVYSCFHGYKLQGQEQVTCTQKGWDSEPPVCKDVNECADLTHPPCHPSAQCKNTKGSFQCVCTDPYVLGEDEKTCIDSGRLPR | ||||||
Transmembrane | 835-859 | Helical | ||||
Sequence: ASWVSIALGALLIGGLASLTWIVIC | ||||||
Topological domain | 860-914 | Cytoplasmic | ||||
Sequence: RWTHADKKATLPITERVTTQSGCRKSQGRGISPHKAAAQDTGQEPASGSRVLLCE |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-31 | |||||
Sequence: MRTLGAMAIMLVVMGTVIFLSFILRSRDILC | ||||||
Chain | PRO_0000023663 | 32-914 | Thyroid peroxidase | |||
Sequence: GKTMKSHVISAVETSQLMVDHAVYNTMKRNLKKREVLSPAQLLSFFKLPESTSGAISRAAEIMETSIQVMKREQSQFSTDALSADILGTIANLSGCLPFMLPPRCPDTCLANKYRPITGACNNRDHPRWGASNTALARWLPPVYEDGFSQPKGWNPNFLYHGFPLPPVREVTRHLIQVSNEAVTEDDQYSDFLPVWGQYIDHDIALTPQSTSTAAFWGGVDCQLTCENQNPCFPIQLPSNSSGTTACLPFYRSSAACGTGDQGALFGNLSAANPRQQMNGLTSFLDASTVYGSSPGVEKQLRNWSSSAGLLRVNTLHLDAGRAYLPFATAACAPEPGTPRTNRTPCFLAGDGRASEVPALAAVHTLWLREHNRLASAFKAINKHWSANTAYQEARKVVGALHQIITMRDYIPKILGPDAFRQYVGPYEGYNPTVNPTVSNIFSTAAFRFGHATVHPLVRRLNTDFQEHTELPRLQLRDVFFRPWRLIQEGGLDPIVRGLLARAAKLQVQGQLMNEELTERLFVLSNVGTLDLASLNLQRGRDHGLPDYNEWREFCGLSRLETPAELNKAIANRSMVNKIMDLYKHADNIDVWLGGLAEKFLPGARTGPLFACIIGKQMKALRDGDRFWWENTNVFTDAQRQELEKHSLPRVICDNTGLTRVPVDAFRIGKFPQDFESCEDIPSMDLELWRETFPQDDKCVFPEEVDNGNFVHCEESGKLVLVYSCFHGYKLQGQEQVTCTQKGWDSEPPVCKDVNECADLTHPPCHPSAQCKNTKGSFQCVCTDPYVLGEDEKTCIDSGRLPRASWVSIALGALLIGGLASLTWIVICRWTHADKKATLPITERVTTQSGCRKSQGRGISPHKAAAQDTGQEPASGSRVLLCE | ||||||
Glycosylation | 123 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 136↔152 | |||||
Sequence: CPDTCLANKYRPITGAC | ||||||
Disulfide bond | 253↔263 | |||||
Sequence: CQLTCENQNPC | ||||||
Disulfide bond | 257↔278 | |||||
Sequence: CENQNPCFPIQLPSNSSGTTAC | ||||||
Glycosylation | 271 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 299 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 334 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 586↔643 | |||||
Sequence: CGLSRLETPAELNKAIANRSMVNKIMDLYKHADNIDVWLGGLAEKFLPGARTGPLFAC | ||||||
Glycosylation | 603 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 684↔709 | |||||
Sequence: CDNTGLTRVPVDAFRIGKFPQDFESC | ||||||
Disulfide bond | 730↔770 | |||||
Sequence: CVFPEEVDNGNFVHCEESGKLVLVYSCFHGYKLQGQEQVTC | ||||||
Disulfide bond | 756↔782 | |||||
Sequence: CFHGYKLQGQEQVTCTQKGWDSEPPVC | ||||||
Disulfide bond | 788↔802 | |||||
Sequence: CADLTHPPCHPSAQC | ||||||
Disulfide bond | 796↔811 | |||||
Sequence: CHPSAQCKNTKGSFQC | ||||||
Disulfide bond | 813↔826 | |||||
Sequence: CTDPYVLGEDEKTC |
Post-translational modification
Heme is covalently bound through a H2O2-dependent autocatalytic process. Heme insertion is important for the delivery of protein at the cell surface (By similarity).
Cleaved in its N-terminal part.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 728-783 | Sushi | ||||
Sequence: DKCVFPEEVDNGNFVHCEESGKLVLVYSCFHGYKLQGQEQVTCTQKGWDSEPPVCK | ||||||
Domain | 784-827 | EGF-like; calcium-binding | ||||
Sequence: DVNECADLTHPPCHPSAQCKNTKGSFQCVCTDPYVLGEDEKTCI | ||||||
Region | 881-909 | Disordered | ||||
Sequence: GCRKSQGRGISPHKAAAQDTGQEPASGSR |
Sequence similarities
Belongs to the peroxidase family. XPO subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length914
- Mass (Da)101,342
- Last updated1994-06-01 v1
- Checksum595E9A0B71F3DD01
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
G3UXW8 | G3UXW8_MOUSE | Tpo | 164 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 614 | in Ref. 2; BAC33171 | ||||
Sequence: Y → H |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X60703 EMBL· GenBank· DDBJ | CAA43114.1 EMBL· GenBank· DDBJ | mRNA | ||
AK047843 EMBL· GenBank· DDBJ | BAC33171.1 EMBL· GenBank· DDBJ | mRNA |