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P09933 (PERT_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thyroid peroxidase

Short name=TPO
EC=1.11.1.8
Gene names
Name:TPO
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length926 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Iodination and coupling of the hormonogenic tyrosines in thyroglobulin to yield the thyroid hormones T3 and T4.

Catalytic activity

2 iodide + H2O2 + 2 H+ = 2 iodine + 2 H2O.

[Thyroglobulin]-L-tyrosine + iodide + H2O2 = [thyroglobulin]-3-iodo-L-tyrosine + 2 H2O.

[Thyroglobulin]-3-iodo-L-tyrosine + iodide + H2O2 = [thyroglobulin]-3,5-diiodo-L-tyrosine + 2 H2O.

2 [thyroglobulin]-3,5-diiodo-L-tyrosine + H2O2 = [thyroglobulin]-L-thyroxine + [thyroglobulin]-aminoacrylate + 2 H2O.

[Thyroglobulin]-3-iodo-L-tyrosine + [thyroglobulin]-3,5-diiodo-L-tyrosine + H2O2 = [thyroglobulin]-3,5,3'-triiodo-L-thyronine + [thyroglobulin]-aminoacrylate + 2 H2O.

Cofactor

Binds 1 calcium ion per heterodimer By similarity.

Binds 1 heme B (iron-protoporphyrin IX) group covalently per heterodimer By similarity.

Pathway

Hormone biosynthesis; thyroid hormone biosynthesis.

Subunit structure

Interacts with DUOX1, DUOX2 and CYBA By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein By similarity.

Post-translational modification

Heme is covalently bound through a H2O(2)-dependent autocatalytic process. Heme insertion is important for the delivery of protein at the cell surface By similarity.

Cleaved in its N-terminal part By similarity.

N-glycosylated; contains mannose and N-acetylglucosamine. Ref.3

Sequence similarities

Belongs to the peroxidase family. XPO subfamily.

Contains 1 EGF-like domain.

Contains 1 Sushi (CCP/SCR) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1414 Potential
Chain15 – 926912Thyroid peroxidase
PRO_0000023664

Regions

Topological domain19 – 844826Extracellular Potential
Transmembrane845 – 86925Helical; Potential
Topological domain870 – 92657Cytoplasmic Potential
Domain738 – 79356Sushi
Domain794 – 83744EGF-like; calcium-binding Potential

Sites

Active site2391Proton acceptor By similarity
Metal binding2401Calcium By similarity
Metal binding3211Calcium By similarity
Metal binding3231Calcium; via carbonyl oxygen By similarity
Metal binding3251Calcium By similarity
Metal binding3271Calcium By similarity
Metal binding4931Iron (heme axial ligand) By similarity
Binding site2381Heme (covalent; via 2 links) By similarity
Binding site3981Heme (covalent; via 2 links) By similarity
Site3951Transition state stabilizer By similarity

Amino acid modifications

Glycosylation1291N-linked (GlcNAc...) Ref.3
Glycosylation2771N-linked (GlcNAc...) Ref.3
Glycosylation3071N-linked (GlcNAc...) Ref.3
Glycosylation3421N-linked (GlcNAc...) Ref.3
Disulfide bond142 ↔ 158 By similarity
Disulfide bond259 ↔ 269 By similarity
Disulfide bond263 ↔ 286 By similarity
Disulfide bond596 ↔ 653 By similarity
Disulfide bond694 ↔ 719 By similarity
Disulfide bond740 ↔ 780 By similarity
Disulfide bond766 ↔ 792 By similarity
Disulfide bond798 ↔ 812 By similarity
Disulfide bond806 ↔ 821 By similarity
Disulfide bond823 ↔ 836 By similarity

Sequences

Sequence LengthMass (Da)Tools
P09933 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 8549FF6F0F742C5E

FASTA926100,443
        10         20         30         40         50         60 
MGARAVLGVT LAVACAGAFF ASILRRKDLL GGDTEASGVA GLVEASRLLV DEAIHTTMRR 

        70         80         90        100        110        120 
NLRKRGIFSP SQLLSFSKLP EPTSRTASRA AEIMETAVQE VKRRVCRRRD TDQLPTDVLS 

       130        140        150        160        170        180 
EELLSTIANL SGCLPHMLPP SCPHTCLANK YRLITGACNN RDHPRWGASN TALARWLPPA 

       190        200        210        220        230        240 
YEDGVTEPRG WNPHFLYNGL PLPPVREVTR QVIHVSNEAV TEDGQYSDLL MAWGQYIDHD 

       250        260        270        280        290        300 
IAFTPQSTSK AAFAGGADCQ LTCENRSPCF PIQLPTNASG AAGATCLPFY RSSAACGSGR 

       310        320        330        340        350        360 
QGALVGNLSW AAPRQQMNGL TSFLDASTVY GSSPAQEQRL RNWTSAEGLL RVNTRHRDAG 

       370        380        390        400        410        420 
RAFLPFAPPP APPACAPEPG TPAARAPCFL AGDSRASEVP GLTALHTLWL REHNRLAAAF 

       430        440        450        460        470        480 
KALNAHWSAD TVYQEARKVV GALHQIVTLR DYVPKILGAE AFGQHVGPYQ GYDPAVDPTV 

       490        500        510        520        530        540 
SNVFSTAAFR FGHATIHPLV RRLDARFQEH PGSHLPLRAA FFQPWRLLRE GGVDPVLRGL 

       550        560        570        580        590        600 
LARPAKLQVQ DQLMNEELTE RLFVLSNSGT LDLASINLQR GRDHGLPGYN EWREFCGLSR 

       610        620        630        640        650        660 
LETWADLSAA TANGRVADRI LGLYQHPDNI DVWLGGLAES FLPGARTGPL FACIIGKQMR 

       670        680        690        700        710        720 
ALRDGDRFWW ENPGVFTEAQ RRELSRHSMS RVICDNSGLS HVPLDAFRVG QWPQEFEPCA 

       730        740        750        760        770        780 
SIQGMDLGAW REAPPSGDAC GFPDPVEDGG FLLCEERGQR VLVFSCRHGF RLRGPAQITC 

       790        800        810        820        830        840 
TPRGWDSPPP LCKDINECED ETDPPCHASA RCKNTKGGVL CECSDPLVLG EDGRTCVDAG 

       850        860        870        880        890        900 
RLPRASVVSI ALGAVLVCGL AGLAWTVVCR WTHADARPLL PVGEGEGDGK SPSLPLPGCG 

       910        920 
NRRDVGAAPA LEVEQDLSCG SRGLCE 

« Hide

References

[1]"Molecular cloning of the structural gene for porcine thyroid peroxidase."
Magnusson R.P., Gestautas J., Taurog A., Rapoport B.
J. Biol. Chem. 262:13885-13888(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Isolation and characterization of a cDNA clone for porcine thyroid peroxidase."
Magnusson R.P., Gestautas J., Seto P., Taurog A., Rapoport B.
FEBS Lett. 208:391-396(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 595-926.
[3]"Thyroid peroxidase glycosylation: the location and nature of the N-linked oligosaccharide units in porcine thyroid peroxidase."
Rawitch A.B., Pollock G., Yang S.-X., Taurog A.
Arch. Biochem. Biophys. 297:321-327(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 110-115; 267-274; 301-308 AND 340-351, GLYCOSYLATION AT ASN-129; ASN-277; ASN-307 AND ASN-342.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04645 mRNA. Translation: CAA28306.1.
PIROPPGIT. A27416.
UniGeneSsc.99.

3D structure databases

ProteinModelPortalP09933.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9823.ENSSSCP00000009228.

Protein family/group databases

PeroxiBase3329. SscTPO.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG262194.
HOGENOMHOG000016084.
HOVERGENHBG000071.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14809.
UniPathwayUPA00194.

Family and domain databases

Gene3D1.10.640.10. 1 hit.
InterProIPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR010255. Haem_peroxidase.
IPR002007. Haem_peroxidase_animal.
IPR019791. Haem_peroxidase_animal_subgr.
IPR000436. Sushi_SCR_CCP.
[Graphical view]
PfamPF03098. An_peroxidase. 1 hit.
PF07645. EGF_CA. 1 hit.
PF00084. Sushi. 1 hit.
[Graphical view]
PRINTSPR00457. ANPEROXIDASE.
SMARTSM00032. CCP. 1 hit.
SM00181. EGF. 1 hit.
[Graphical view]
SUPFAMSSF48113. SSF48113. 1 hit.
SSF57535. SSF57535. 1 hit.
PROSITEPS50026. EGF_3. 1 hit.
PS00435. PEROXIDASE_1. 1 hit.
PS50292. PEROXIDASE_3. 1 hit.
PS50923. SUSHI. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePERT_PIG
AccessionPrimary (citable) accession number: P09933
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: February 19, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways