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P09933

- PERT_PIG

UniProt

P09933 - PERT_PIG

Protein

Thyroid peroxidase

Gene

TPO

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    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

    Binds 1 calcium ion per heterodimer.PROSITE-ProRule annotation
    Binds 1 heme B (iron-protoporphyrin IX) group covalently per heterodimer.PROSITE-ProRule annotation

    Pathwayi

    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

    1. calcium ion binding Source: InterPro
    2. heme binding Source: InterPro
    3. iodide peroxidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. hormone biosynthetic process Source: UniProtKB-KW
    2. hydrogen peroxide catabolic process Source: UniProtKB-KW
    3. thyroid hormone generation Source: UniProtKB-UniPathway

    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.
    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: Unplaced

    Subcellular locationi

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

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW

    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.ENSSSCP00000009228.

    Structurei

    3D structure databases

    ProteinModelPortaliP09933.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei845 – 86925HelicalSequence AnalysisAdd
    BLAST

    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.

    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.
    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

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    MGARAVLGVT LAVACAGAFF ASILRRKDLL GGDTEASGVA GLVEASRLLV    50
    DEAIHTTMRR NLRKRGIFSP SQLLSFSKLP EPTSRTASRA AEIMETAVQE 100
    VKRRVCRRRD TDQLPTDVLS EELLSTIANL SGCLPHMLPP SCPHTCLANK 150
    YRLITGACNN RDHPRWGASN TALARWLPPA YEDGVTEPRG WNPHFLYNGL 200
    PLPPVREVTR QVIHVSNEAV TEDGQYSDLL MAWGQYIDHD IAFTPQSTSK 250
    AAFAGGADCQ LTCENRSPCF PIQLPTNASG AAGATCLPFY RSSAACGSGR 300
    QGALVGNLSW AAPRQQMNGL TSFLDASTVY GSSPAQEQRL RNWTSAEGLL 350
    RVNTRHRDAG RAFLPFAPPP APPACAPEPG TPAARAPCFL AGDSRASEVP 400
    GLTALHTLWL REHNRLAAAF KALNAHWSAD TVYQEARKVV GALHQIVTLR 450
    DYVPKILGAE AFGQHVGPYQ GYDPAVDPTV SNVFSTAAFR FGHATIHPLV 500
    RRLDARFQEH PGSHLPLRAA FFQPWRLLRE GGVDPVLRGL LARPAKLQVQ 550
    DQLMNEELTE RLFVLSNSGT LDLASINLQR GRDHGLPGYN EWREFCGLSR 600
    LETWADLSAA TANGRVADRI LGLYQHPDNI DVWLGGLAES FLPGARTGPL 650
    FACIIGKQMR ALRDGDRFWW ENPGVFTEAQ RRELSRHSMS RVICDNSGLS 700
    HVPLDAFRVG QWPQEFEPCA SIQGMDLGAW REAPPSGDAC GFPDPVEDGG 750
    FLLCEERGQR VLVFSCRHGF RLRGPAQITC TPRGWDSPPP LCKDINECED 800
    ETDPPCHASA RCKNTKGGVL CECSDPLVLG EDGRTCVDAG RLPRASVVSI 850
    ALGAVLVCGL AGLAWTVVCR WTHADARPLL PVGEGEGDGK SPSLPLPGCG 900
    NRRDVGAAPA LEVEQDLSCG SRGLCE 926
    Length:926
    Mass (Da):100,443
    Last modified:July 1, 1989 - v1
    Checksum:i8549FF6F0F742C5E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04645 mRNA. Translation: CAA28306.1.
    PIRiA27416. OPPGIT.
    UniGeneiSsc.99.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04645 mRNA. Translation: CAA28306.1 .
    PIRi A27416. OPPGIT.
    UniGenei Ssc.99.

    3D structure databases

    ProteinModelPortali P09933.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9823.ENSSSCP00000009228.

    Protein family/group databases

    PeroxiBasei 3329. SscTPO.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi NOG262194.
    HOGENOMi HOG000016084.
    HOVERGENi HBG000071.

    Enzyme and pathway databases

    UniPathwayi UPA00194 .
    BioCyci MetaCyc:MONOMER-14809.

    Family and domain databases

    Gene3Di 1.10.640.10. 1 hit.
    InterProi IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR010255. Haem_peroxidase.
    IPR019791. Haem_peroxidase_animal.
    IPR000436. Sushi_SCR_CCP.
    IPR029589. TPO.
    [Graphical view ]
    PANTHERi PTHR11475:SF60. PTHR11475:SF60. 1 hit.
    Pfami PF03098. An_peroxidase. 1 hit.
    PF07645. EGF_CA. 1 hit.
    PF00084. Sushi. 1 hit.
    [Graphical view ]
    PRINTSi PR00457. ANPEROXIDASE.
    SMARTi SM00032. CCP. 1 hit.
    SM00181. EGF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48113. SSF48113. 1 hit.
    SSF57535. SSF57535. 1 hit.
    PROSITEi PS50026. EGF_3. 1 hit.
    PS00435. PEROXIDASE_1. 1 hit.
    PS50292. PEROXIDASE_3. 1 hit.
    PS50923. SUSHI. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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: October 1, 2014
    This is version 135 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