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P14650

- PERT_RAT

UniProt

P14650 - PERT_RAT

Protein

Thyroid peroxidase

Gene

Tpo

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      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 sitei232 – 2321Heme (covalent; via 2 links)By similarity
    Active sitei233 – 2331Proton acceptorPROSITE-ProRule annotation
    Metal bindingi234 – 2341CalciumPROSITE-ProRule annotation
    Metal bindingi313 – 3131CalciumPROSITE-ProRule annotation
    Metal bindingi315 – 3151Calcium; via carbonyl oxygenPROSITE-ProRule annotation
    Metal bindingi317 – 3171CalciumPROSITE-ProRule annotation
    Metal bindingi319 – 3191CalciumPROSITE-ProRule annotation
    Sitei384 – 3841Transition state stabilizerPROSITE-ProRule annotation
    Binding sitei387 – 3871Heme (covalent; via 2 links)By similarity
    Metal bindingi482 – 4821Iron (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: RGD

    GO - Biological processi

    1. cellular response to nitric oxide Source: RGD
    2. hormone biosynthetic process Source: UniProtKB-KW
    3. hydrogen peroxide catabolic process Source: UniProtKB-KW
    4. response to lipid Source: RGD
    5. thyroid hormone generation Source: RGD

    Keywords - Molecular functioni

    Oxidoreductase, Peroxidase

    Keywords - Biological processi

    Hydrogen peroxide, Thyroid hormones biosynthesis

    Keywords - Ligandi

    Calcium, Heme, Iron, Metal-binding

    Enzyme and pathway databases

    UniPathwayiUPA00194.

    Protein family/group databases

    PeroxiBasei3973. RnoTPO.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thyroid peroxidase (EC:1.11.1.8)
    Short name:
    TPO
    Gene namesi
    Name:Tpo
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi3900. Tpo.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cell surface Source: RGD
    2. integral component of membrane Source: UniProtKB-KW
    3. plasma membrane Source: RGD

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3131Sequence AnalysisAdd
    BLAST
    Chaini32 – 914883Thyroid peroxidasePRO_0000023665Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi123 – 1231N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi136 ↔ 152By similarity
    Disulfide bondi253 ↔ 263By similarity
    Disulfide bondi257 ↔ 278By similarity
    Glycosylationi271 – 2711N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi299 – 2991N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi334 – 3341N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi586 ↔ 643By similarity
    Glycosylationi603 – 6031N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi684 ↔ 709By similarity
    Disulfide bondi730 ↔ 770By similarity
    Disulfide bondi756 ↔ 782By similarity
    Disulfide bondi788 ↔ 802By similarity
    Disulfide bondi796 ↔ 811By similarity
    Disulfide bondi813 ↔ 826By 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

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP14650.
    PRIDEiP14650.

    Expressioni

    Gene expression databases

    GenevestigatoriP14650.

    Interactioni

    Subunit structurei

    Interacts with DUOX1, DUOX2 and CYBA.By similarity

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000006526.

    Structurei

    3D structure databases

    ProteinModelPortaliP14650.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini32 – 834803ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini860 – 91455CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei835 – 85925HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini728 – 78356SushiPROSITE-ProRule annotationAdd
    BLAST
    Domaini784 – 82744EGF-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.
    InParanoidiP14650.
    PhylomeDBiP14650.

    Family and domain databases

    Gene3Di1.10.640.10. 2 hits.
    InterProiIPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    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.
    SM00179. EGF_CA. 1 hit.
    [Graphical view]
    SUPFAMiSSF48113. SSF48113. 1 hit.
    SSF57535. SSF57535. 1 hit.
    PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
    PS01186. EGF_2. 1 hit.
    PS50026. EGF_3. 1 hit.
    PS01187. EGF_CA. 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.

    P14650-1 [UniParc]FASTAAdd to Basket

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    MRTLGAMAVM LVVMGTAIFL PFLLRSRDIL GGKTMTSHVI SVVETSQLLV    50
    DNAVYNTMKR NLKKRGVLSP AQLLSFSKLP ESTSGAISRA AEIMETSIQV 100
    MKREQSQFST DALSADILAT IANLSGCLPF MLPPRCPDTC LANKYRPITG 150
    VCNNRDHPRW GASNTALARW LPPVYEDGFS QPRGWNPNFL YHGFPLPPVR 200
    EVTRHLIQVS NEAVTEDDQY SDFLPVWGQY IDHDIALTPQ STSTAAFWGG 250
    VDCQLTCENQ NPCFPIQLPS NSSRTTACLP FYRSSAACGT GDQGALFGNL 300
    SAANPRQQMN GLTSFLDAST VYGSSPGVEK QLRNWSSSAG LLRVNTLHLD 350
    SGRAYLPFAS AACAPEPGAP HANRTPCFLA GDGRASEVPA LAAVHTLWLR 400
    EHNRLATAFK AINTHWSANT AYQEARKVVG ALHQIITMRD YIPKILGPDA 450
    FRQYVGPYEG YNPTVNPTVS NVFSTAAFRF GHATVHPLVR RLNTDFQDHT 500
    ELPRLQLHDV FFRPWRLIQE GGLDPIVRGL LARPAKLQVQ EQLMNEELTE 550
    RLFVLSNVGT LDLASLNLQR GRDHGLPGYN EWREFCGLSR LDTGAELNKA 600
    IANRSMVNKI MELYKHADNI DVWLGGLAEK FLPGARTGPL FACIIGKQMK 650
    ALRDGDRFWW ENSHVFTDAQ RQELEKHSLP RVICDNTGLT RVPVDAFRIG 700
    KFPQDFESCE EIPSMDLRLW RETFPQDDKC VFPEKVDNGN FVHCEESGKL 750
    VLVYSCFHGY KLQGQEQVTC TQNGWDSEPP VCKDVNECAD LTHPPCHSSA 800
    KCKNTKGSFQ CVCTDPYMLG EDEKTCIDSG RLPRASWVSI ALGALLIGGL 850
    ASLSWTVICR WTHADKKSTL LITERVTMES GFRKSQESGI SPQKAEVQDA 900
    EQEPAYGSRV LLCE 914
    Length:914
    Mass (Da):101,460
    Last modified:April 1, 1990 - v1
    Checksum:iB700B89439E85191
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti194 – 1952FP → LG in AAA42265. (PubMed:2691880)Curated
    Sequence conflicti198 – 1981P → S in AAA42265. (PubMed:2691880)Curated
    Sequence conflicti228 – 2281G → A in AAA42265. (PubMed:2691880)Curated
    Sequence conflicti592 – 5943DTG → ETP in AAA42265. (PubMed:2691880)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X17396 mRNA. Translation: CAA35257.1.
    M31655 mRNA. Translation: AAA42265.1.
    PIRiS07047.
    UniGeneiRn.233736.

    Genome annotation databases

    UCSCiRGD:3900. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X17396 mRNA. Translation: CAA35257.1 .
    M31655 mRNA. Translation: AAA42265.1 .
    PIRi S07047.
    UniGenei Rn.233736.

    3D structure databases

    ProteinModelPortali P14650.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000006526.

    Protein family/group databases

    PeroxiBasei 3973. RnoTPO.

    Proteomic databases

    PaxDbi P14650.
    PRIDEi P14650.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    UCSCi RGD:3900. rat.

    Organism-specific databases

    RGDi 3900. Tpo.

    Phylogenomic databases

    eggNOGi NOG262194.
    HOGENOMi HOG000016084.
    HOVERGENi HBG000071.
    InParanoidi P14650.
    PhylomeDBi P14650.

    Enzyme and pathway databases

    UniPathwayi UPA00194 .

    Miscellaneous databases

    NextBioi 610988.
    PROi P14650.

    Gene expression databases

    Genevestigatori P14650.

    Family and domain databases

    Gene3Di 1.10.640.10. 2 hits.
    InterProi IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    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.
    SM00179. EGF_CA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48113. SSF48113. 1 hit.
    SSF57535. SSF57535. 1 hit.
    PROSITEi PS00010. ASX_HYDROXYL. 1 hit.
    PS01186. EGF_2. 1 hit.
    PS50026. EGF_3. 1 hit.
    PS01187. EGF_CA. 1 hit.
    PS00435. PEROXIDASE_1. 1 hit.
    PS50292. PEROXIDASE_3. 1 hit.
    PS50923. SUSHI. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete nucleotide sequence of the cDNA for thyroid peroxidase in FRTL5 rat thyroid cells."
      Derwahl M., Seto P., Rapoport B.
      Nucleic Acids Res. 17:8380-8380(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Thyroid peroxidase: rat cDNA sequence, chromosomal localization in mouse, and regulation of gene expression by comparison to thyroglobulin in rat FRTL-5 cells."
      Isozaki O., Kohn L.D., Kozak C.A., Kimura S.
      Mol. Endocrinol. 3:1681-1692(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 145-914.

    Entry informationi

    Entry nameiPERT_RAT
    AccessioniPrimary (citable) accession number: P14650
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 144 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, 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