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P35419

- PERT_MOUSE

UniProt

P35419 - PERT_MOUSE

Protein

Thyroid peroxidase

Gene

Tpo

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      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: UniProtKB-EC

    GO - Biological processi

    1. embryonic hemopoiesis Source: Ensembl
    2. hormone biosynthetic process Source: UniProtKB-KW
    3. hydrogen peroxide catabolic process Source: UniProtKB-KW
    4. 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

    ReactomeiREACT_219697. Thyroxine biosynthesis.
    UniPathwayiUPA00194.

    Protein family/group databases

    PeroxiBasei3345. MmTPO.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thyroid peroxidase (EC:1.11.1.8)
    Short name:
    TPO
    Gene namesi
    Name:Tpo
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 12

    Organism-specific databases

    MGIiMGI:98813. Tpo.

    Subcellular locationi

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

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3131Sequence AnalysisAdd
    BLAST
    Chaini32 – 914883Thyroid peroxidasePRO_0000023663Add
    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

    PRIDEiP35419.

    PTM databases

    PhosphoSiteiP35419.

    Expressioni

    Gene expression databases

    BgeeiP35419.
    CleanExiMM_TPO.
    GenevestigatoriP35419.

    Interactioni

    Subunit structurei

    Interacts with DUOX1, DUOX2 and CYBA.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP35419.
    SMRiP35419. Positions 143-722, 751-827.
    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.
    GeneTreeiENSGT00550000074325.
    HOGENOMiHOG000016084.
    HOVERGENiHBG000071.
    InParanoidiP35419.
    KOiK00431.
    OMAiIMETSIQ.
    OrthoDBiEOG7D2FD6.
    PhylomeDBiP35419.
    TreeFamiTF314316.

    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.

    P35419-1 [UniParc]FASTAAdd to Basket

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    MRTLGAMAIM LVVMGTVIFL SFILRSRDIL CGKTMKSHVI SAVETSQLMV    50
    DHAVYNTMKR NLKKREVLSP AQLLSFFKLP ESTSGAISRA AEIMETSIQV 100
    MKREQSQFST DALSADILGT IANLSGCLPF MLPPRCPDTC LANKYRPITG 150
    ACNNRDHPRW GASNTALARW LPPVYEDGFS QPKGWNPNFL YHGFPLPPVR 200
    EVTRHLIQVS NEAVTEDDQY SDFLPVWGQY IDHDIALTPQ STSTAAFWGG 250
    VDCQLTCENQ NPCFPIQLPS NSSGTTACLP FYRSSAACGT GDQGALFGNL 300
    SAANPRQQMN GLTSFLDAST VYGSSPGVEK QLRNWSSSAG LLRVNTLHLD 350
    AGRAYLPFAT AACAPEPGTP RTNRTPCFLA GDGRASEVPA LAAVHTLWLR 400
    EHNRLASAFK AINKHWSANT AYQEARKVVG ALHQIITMRD YIPKILGPDA 450
    FRQYVGPYEG YNPTVNPTVS NIFSTAAFRF GHATVHPLVR RLNTDFQEHT 500
    ELPRLQLRDV FFRPWRLIQE GGLDPIVRGL LARAAKLQVQ GQLMNEELTE 550
    RLFVLSNVGT LDLASLNLQR GRDHGLPDYN EWREFCGLSR LETPAELNKA 600
    IANRSMVNKI MDLYKHADNI DVWLGGLAEK FLPGARTGPL FACIIGKQMK 650
    ALRDGDRFWW ENTNVFTDAQ RQELEKHSLP RVICDNTGLT RVPVDAFRIG 700
    KFPQDFESCE DIPSMDLELW RETFPQDDKC VFPEEVDNGN FVHCEESGKL 750
    VLVYSCFHGY KLQGQEQVTC TQKGWDSEPP VCKDVNECAD LTHPPCHPSA 800
    QCKNTKGSFQ CVCTDPYVLG EDEKTCIDSG RLPRASWVSI ALGALLIGGL 850
    ASLTWIVICR WTHADKKATL PITERVTTQS GCRKSQGRGI SPHKAAAQDT 900
    GQEPASGSRV LLCE 914
    Length:914
    Mass (Da):101,342
    Last modified:June 1, 1994 - v1
    Checksum:i595E9A0B71F3DD01
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti614 – 6141Y → H in BAC33171. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60703 mRNA. Translation: CAA43114.1.
    AK047843 mRNA. Translation: BAC33171.1.
    CCDSiCCDS25857.1.
    PIRiJN0550.
    RefSeqiNP_033443.1. NM_009417.2.
    UniGeneiMm.4991.

    Genome annotation databases

    EnsembliENSMUST00000021005; ENSMUSP00000021005; ENSMUSG00000020673.
    GeneIDi22018.
    KEGGimmu:22018.
    UCSCiuc007ngo.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60703 mRNA. Translation: CAA43114.1 .
    AK047843 mRNA. Translation: BAC33171.1 .
    CCDSi CCDS25857.1.
    PIRi JN0550.
    RefSeqi NP_033443.1. NM_009417.2.
    UniGenei Mm.4991.

    3D structure databases

    ProteinModelPortali P35419.
    SMRi P35419. Positions 143-722, 751-827.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    PeroxiBasei 3345. MmTPO.

    PTM databases

    PhosphoSitei P35419.

    Proteomic databases

    PRIDEi P35419.

    Protocols and materials databases

    DNASUi 22018.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000021005 ; ENSMUSP00000021005 ; ENSMUSG00000020673 .
    GeneIDi 22018.
    KEGGi mmu:22018.
    UCSCi uc007ngo.1. mouse.

    Organism-specific databases

    CTDi 7173.
    MGIi MGI:98813. Tpo.

    Phylogenomic databases

    eggNOGi NOG262194.
    GeneTreei ENSGT00550000074325.
    HOGENOMi HOG000016084.
    HOVERGENi HBG000071.
    InParanoidi P35419.
    KOi K00431.
    OMAi IMETSIQ.
    OrthoDBi EOG7D2FD6.
    PhylomeDBi P35419.
    TreeFami TF314316.

    Enzyme and pathway databases

    UniPathwayi UPA00194 .
    Reactomei REACT_219697. Thyroxine biosynthesis.

    Miscellaneous databases

    NextBioi 301744.
    PROi P35419.
    SOURCEi Search...

    Gene expression databases

    Bgeei P35419.
    CleanExi MM_TPO.
    Genevestigatori P35419.

    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. "Nucleotide sequence of the cDNA encoding mouse thyroid peroxidase."
      Kotani T., Umeki K., Yamamoto I., Takeuchi M., Takechi S., Nakayama T., Ohtaki S.
      Gene 123:289-290(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6.
      Tissue: Thyroid.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Head.

    Entry informationi

    Entry nameiPERT_MOUSE
    AccessioniPrimary (citable) accession number: P35419
    Secondary accession number(s): Q8C8B1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 147 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3