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Protein

Thyroid peroxidase

Gene

TPO

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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.

Cofactori

Protein has several cofactor binding sites:
  • Ca2+PROSITE-ProRule annotationNote: Binds 1 Ca2+ ion per heterodimer.PROSITE-ProRule annotation
  • heme bPROSITE-ProRule annotationNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per heterodimer.PROSITE-ProRule annotation

Pathway:ithyroid hormone biosynthesis

This protein is involved in the pathway thyroid hormone biosynthesis, which is part of Hormone biosynthesis.
View all proteins of this organism that are known to be involved in the pathway thyroid hormone biosynthesis and in Hormone biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei238 – 2381Heme (covalent; via 2 links)By similarity
Active sitei239 – 2391Proton acceptorPROSITE-ProRule annotation
Metal bindingi240 – 2401CalciumPROSITE-ProRule annotation
Metal bindingi321 – 3211CalciumPROSITE-ProRule annotation
Metal bindingi323 – 3231Calcium; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi325 – 3251CalciumPROSITE-ProRule annotation
Metal bindingi327 – 3271CalciumPROSITE-ProRule annotation
Sitei395 – 3951Transition state stabilizerPROSITE-ProRule annotation
Binding sitei398 – 3981Heme (covalent; via 2 links)By similarity
Metal bindingi493 – 4931Iron (heme axial ligand)PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide, Thyroid hormones biosynthesis

Keywords - Ligandi

Calcium, Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14809.
BRENDAi1.11.1.8. 6170.
UniPathwayiUPA00194.

Protein family/group databases

PeroxiBasei3329. SscTPO.

Names & Taxonomyi

Protein namesi
Recommended name:
Thyroid peroxidase (EC:1.11.1.8)
Short name:
TPO
Gene namesi
Name:TPO
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 844826ExtracellularSequence AnalysisAdd
BLAST
Transmembranei845 – 86925HelicalSequence AnalysisAdd
BLAST
Topological domaini870 – 92657CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1414Sequence AnalysisAdd
BLAST
Chaini15 – 926912Thyroid peroxidasePRO_0000023664Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi129 – 1291N-linked (GlcNAc...)1 Publication
Disulfide bondi142 ↔ 158By similarity
Disulfide bondi259 ↔ 269By similarity
Disulfide bondi263 ↔ 286By similarity
Glycosylationi277 – 2771N-linked (GlcNAc...)1 Publication
Glycosylationi307 – 3071N-linked (GlcNAc...)1 Publication
Glycosylationi342 – 3421N-linked (GlcNAc...)1 Publication
Disulfide bondi596 ↔ 653By similarity
Disulfide bondi694 ↔ 719By similarity
Disulfide bondi740 ↔ 780By similarity
Disulfide bondi766 ↔ 792By similarity
Disulfide bondi798 ↔ 812By similarity
Disulfide bondi806 ↔ 821By similarity
Disulfide bondi823 ↔ 836By similarity

Post-translational modificationi

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).By similarity
Cleaved in its N-terminal part.By similarity
N-glycosylated; contains mannose and N-acetylglucosamine.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Interacts with DUOX1, DUOX2 and CYBA.By similarity

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000027731.

Structurei

3D structure databases

ProteinModelPortaliP09933.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini738 – 79356SushiPROSITE-ProRule annotationAdd
BLAST
Domaini794 – 83744EGF-like; calcium-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peroxidase family. XPO subfamily.PROSITE-ProRule annotation
Contains 1 EGF-like domain.PROSITE-ProRule annotation
Contains 1 Sushi (CCP/SCR) domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Signal, Sushi, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG262194.
HOGENOMiHOG000016084.
HOVERGENiHBG000071.
InParanoidiP09933.

Family and domain databases

Gene3Di1.10.640.10. 1 hit.
InterProiIPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR010255. Haem_peroxidase.
IPR019791. Haem_peroxidase_animal.
IPR000436. Sushi_SCR_CCP_dom.
IPR029589. TPO.
[Graphical view]
PANTHERiPTHR11475:SF60. PTHR11475:SF60. 1 hit.
PfamiPF03098. An_peroxidase. 1 hit.
PF07645. EGF_CA. 1 hit.
PF00084. Sushi. 1 hit.
[Graphical view]
PRINTSiPR00457. ANPEROXIDASE.
SMARTiSM00032. CCP. 1 hit.
SM00181. EGF. 1 hit.
[Graphical view]
SUPFAMiSSF48113. SSF48113. 1 hit.
SSF57535. SSF57535. 1 hit.
PROSITEiPS50026. EGF_3. 1 hit.
PS00435. PEROXIDASE_1. 1 hit.
PS50292. PEROXIDASE_3. 1 hit.
PS50923. SUSHI. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P09933-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGARAVLGVT LAVACAGAFF ASILRRKDLL GGDTEASGVA GLVEASRLLV
60 70 80 90 100
DEAIHTTMRR NLRKRGIFSP SQLLSFSKLP EPTSRTASRA AEIMETAVQE
110 120 130 140 150
VKRRVCRRRD TDQLPTDVLS EELLSTIANL SGCLPHMLPP SCPHTCLANK
160 170 180 190 200
YRLITGACNN RDHPRWGASN TALARWLPPA YEDGVTEPRG WNPHFLYNGL
210 220 230 240 250
PLPPVREVTR QVIHVSNEAV TEDGQYSDLL MAWGQYIDHD IAFTPQSTSK
260 270 280 290 300
AAFAGGADCQ LTCENRSPCF PIQLPTNASG AAGATCLPFY RSSAACGSGR
310 320 330 340 350
QGALVGNLSW AAPRQQMNGL TSFLDASTVY GSSPAQEQRL RNWTSAEGLL
360 370 380 390 400
RVNTRHRDAG RAFLPFAPPP APPACAPEPG TPAARAPCFL AGDSRASEVP
410 420 430 440 450
GLTALHTLWL REHNRLAAAF KALNAHWSAD TVYQEARKVV GALHQIVTLR
460 470 480 490 500
DYVPKILGAE AFGQHVGPYQ GYDPAVDPTV SNVFSTAAFR FGHATIHPLV
510 520 530 540 550
RRLDARFQEH PGSHLPLRAA FFQPWRLLRE GGVDPVLRGL LARPAKLQVQ
560 570 580 590 600
DQLMNEELTE RLFVLSNSGT LDLASINLQR GRDHGLPGYN EWREFCGLSR
610 620 630 640 650
LETWADLSAA TANGRVADRI LGLYQHPDNI DVWLGGLAES FLPGARTGPL
660 670 680 690 700
FACIIGKQMR ALRDGDRFWW ENPGVFTEAQ RRELSRHSMS RVICDNSGLS
710 720 730 740 750
HVPLDAFRVG QWPQEFEPCA SIQGMDLGAW REAPPSGDAC GFPDPVEDGG
760 770 780 790 800
FLLCEERGQR VLVFSCRHGF RLRGPAQITC TPRGWDSPPP LCKDINECED
810 820 830 840 850
ETDPPCHASA RCKNTKGGVL CECSDPLVLG EDGRTCVDAG RLPRASVVSI
860 870 880 890 900
ALGAVLVCGL AGLAWTVVCR WTHADARPLL PVGEGEGDGK SPSLPLPGCG
910 920
NRRDVGAAPA LEVEQDLSCG SRGLCE
Length:926
Mass (Da):100,443
Last modified:July 1, 1989 - v1
Checksum:i8549FF6F0F742C5E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04645 mRNA. Translation: CAA28306.1.
PIRiA27416. OPPGIT.
UniGeneiSsc.99.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04645 mRNA. Translation: CAA28306.1.
PIRiA27416. OPPGIT.
UniGeneiSsc.99.

3D structure databases

ProteinModelPortaliP09933.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000027731.

Protein family/group databases

PeroxiBasei3329. SscTPO.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiNOG262194.
HOGENOMiHOG000016084.
HOVERGENiHBG000071.
InParanoidiP09933.

Enzyme and pathway databases

UniPathwayiUPA00194.
BioCyciMetaCyc:MONOMER-14809.
BRENDAi1.11.1.8. 6170.

Family and domain databases

Gene3Di1.10.640.10. 1 hit.
InterProiIPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR010255. Haem_peroxidase.
IPR019791. Haem_peroxidase_animal.
IPR000436. Sushi_SCR_CCP_dom.
IPR029589. TPO.
[Graphical view]
PANTHERiPTHR11475:SF60. PTHR11475:SF60. 1 hit.
PfamiPF03098. An_peroxidase. 1 hit.
PF07645. EGF_CA. 1 hit.
PF00084. Sushi. 1 hit.
[Graphical view]
PRINTSiPR00457. ANPEROXIDASE.
SMARTiSM00032. CCP. 1 hit.
SM00181. EGF. 1 hit.
[Graphical view]
SUPFAMiSSF48113. SSF48113. 1 hit.
SSF57535. SSF57535. 1 hit.
PROSITEiPS50026. EGF_3. 1 hit.
PS00435. PEROXIDASE_1. 1 hit.
PS50292. PEROXIDASE_3. 1 hit.
PS50923. SUSHI. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiPERT_PIG
AccessioniPrimary (citable) accession number: P09933
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: June 24, 2015
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.