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UniProtKB/Swiss-Prot entry Q8HYB7

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PERT_CANFA
Primary accession number Q8HYB7
Secondary accession numbers None
Integrated into Swiss-Prot on April 23, 2003
Sequence was last modified on March 1, 2003 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 59)
Name and origin of the protein
Protein name Thyroid peroxidase [Precursor]
Synonyms TPO
EC 1.11.1.8
Gene name
Name: TPO
From
Canis familiaris (Dog) [TaxID: 9615] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
Protein existence 2: Evidence at transcript level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Thyroid;
DOI=10.1892/0891-6640(2003)017<0050:CHWGIT>2.3.CO;2; PubMed=12564727 [NCBI, ExPASy, EBI, Israel, Japan]
Fyfe J.C., Kampschmidt K., Dang V., Poteet B.A., He Q., Lowrie C., Graham P.A., Fetro V.M.;
"Congenital hypothyroidism with goiter in toy fox terriers.";
J. Vet. Intern. Med. 17:50-57(2003).
Comments
  • FUNCTION: Iodination and coupling of the hormonogenic tyrosines in thyroglobulin to yield the thyroid hormones T(3) and T(4).
  • CATALYTIC ACTIVITY: 2 iodide + H2O2 + 2 H+ = 2 iodine + 2 H2O.
  • COFACTOR: Binds 1 calcium ion per heterodimer (By similarity).
  • COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group covalently per heterodimer (By similarity).
  • PATHWAY: Hormone biosynthesis; thyroid hormone biosynthesis.
  • SUBUNIT: Interacts with DUOX1, DUOX2 and CYBA (By similarity).
  • SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein (By similarity).
  • PTM: Heme is covalently bound through a H(2)O(2)-dependent autocatalytic process. Heme insertion is important for the delivery of protein at the cell surface (By similarity).
  • PTM: Cleaved in its N-terminal part (By similarity).
  • DISEASE: Defects in TPO are the cause of congenital hypothyroidism with goiter, a simple autosomal recessive trait observed in Toy Fox Terriers (TFTs). Neonatal affected pups exhibited inactivity, abnormal hair coat, stenotic ear canals, and delayed eye opening. Palpable ventrolateral cervical swellings were evident by 1 week of age. Serum thyroid hormone and thyroid-stimulating hormone concentrations were low and high, respectively. Histologic examination of the cervical masses disclosed cuboidal to columnar follicular epithelial cell hyperplasia with widely varying follicular size, shape, and amount of colloid. Oral thyroid hormone replacement therapy restored near-normal growth and development. At 8 weeks of age, radioiodine uptake and perchlorate discharge testing indicated an iodine organification defect. Biochemical analysis of thyroid tissue from affected dogs demonstrated enzymatic iodine oxidation deficiency and lack of sodium dodecyl sulfate-resistant thyroglobulin dimers, suggesting thyroid peroxidase deficiency.
  • SIMILARITY: Belongs to the peroxidase family. XPO subfamily.
  • SIMILARITY: Contains 1 EGF-like domain.
  • SIMILARITY: Contains 1 Sushi (CCP/SCR) domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AY094504; AAM26737.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001003009.1; -.
UniGene Cfa.20
3D structure databases
HSSP P05164; 1D5L. [HSSP ENTRY / PDB]
ModBase Q8HYB7.
Protein family/group databases
PeroxiBase 3334; CfaTPO.
Ontologies
GO
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005509; Molecular function: calcium ion binding (inferred from electronic annotation from InterPro).
GO:0020037; Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0004447; Molecular function: iodide peroxidase activity (inferred from electronic annotation from EC).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0042446; Biological process: hormone biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0042744; Biological process: hydrogen peroxide catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000152; EGF-type_Asp/Asn_hydroxyl_CS.
IPR000742; EGF_3.
IPR001881; EGF_Ca_bd.
IPR013091; EGF_Ca_bd_2.
IPR013032; EGF_like_reg_CS.
IPR002007; Haem_peroxidase_animal.
IPR002016; Haem_peroxidase_pln/fun/bac.
IPR000436; Sushi_SCR_CCP.
Graphical view of domain structure.
Gene3D G3DSA:1.10.640.10; Haem_peroxidase_animal; 1.
Pfam PF03098; An_peroxidase; 1.
PF07645; EGF_CA; 1.
Pfam graphical view of domain structure.
PRINTS PR00457; ANPEROXIDASE.
SMART SM00032; CCP; 1.
SM00179; EGF_CA; 1.
SMART graphical view of domain structure.
PROSITE PS00010; ASX_HYDROXYL; 1.
PS00022; EGF_1; FALSE_NEG.
PS01186; EGF_2; FALSE_NEG.
PS50026; EGF_3; 1.
PS01187; EGF_CA; 1.
PS00435; PEROXIDASE_1; 1.
PS00436; PEROXIDASE_2; FALSE_NEG.
PS50292; PEROXIDASE_3; 1.
PS50923; SUSHI; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
Ensembl ENSCAFG00000003217; Canis familiaris. [Contig view]
GeneID 403521; -.
KEGG cfa:403521; -.
Phylogenomic databases
HOVERGEN Q8HYB7; -.
Other
ProtoNet Q8HYB7.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calcium; EGF-like domain; Glycoprotein; Heme; Hydrogen peroxide; Iron; Membrane; Metal-binding; Oxidoreductase; Peroxidase; Signal; Sushi; Thyroid hormones biosynthesis; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    18  18     Potential. 
CHAIN   19   933  915     Thyroid peroxidase. PRO_0000023661
TOPO_DOM   19   846  828     Extracellular (Potential). 
TRANSMEM   847   867  21     Potential. 
TOPO_DOM   868   933  66     Cytoplasmic (Potential). 
DOMAIN   737   792  56     Sushi. 
DOMAIN   793   836  44     EGF-like; calcium-binding (Potential). 
ACT_SITE   239   239        Proton acceptor (By similarity). 
METAL   240   240        Calcium (By similarity). 
METAL   318   318        Calcium (By similarity). 
METAL   320   320        Calcium; via carbonyl oxygen (By similarity). 
METAL   322   322        Calcium (By similarity). 
METAL   324   324        Calcium (By similarity). 
METAL   491   491        Iron (heme axial ligand) (By similarity). 
BINDING   238   238        Heme (covalent; via 2 links) (By similarity). 
BINDING   396   396        Heme (covalent; via 2 links) (By similarity). 
SITE   393   393  1     Transition state stabilizer (By similarity). 
CARBOHYD   129   129        N-linked (GlcNAc...) (Potential). 
CARBOHYD   304   304        N-linked (GlcNAc...) (Potential). 
CARBOHYD   339   339        N-linked (GlcNAc...) (Potential). 
CARBOHYD   612   612        N-linked (GlcNAc...) (Potential). 
DISULFID   142   158        By similarity. 
DISULFID   259   269        By similarity. 
DISULFID   263   283        By similarity. 
DISULFID   595   652        By similarity. 
DISULFID   693   718        By similarity. 
DISULFID   739   779        By similarity. 
DISULFID   765   791        By similarity. 
DISULFID   797   811        By similarity. 
DISULFID   805   820        By similarity. 
DISULFID   822   835        By similarity. 
Sequence information
Length: 933 AA [This is the length of the unprocessed precursor] Molecular weight: 100461 Da [This is the MW of the unprocessed precursor] CRC64: 30ABDDD87FE70587 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MGALAVLGVT LLVALARGLL PFFLGGRDLL WGQSGEASVL GVVEESRRVV DGAIQHTVRR 

        70         80         90        100        110        120 
DLSKRGLPSP SQLLSFSKLP EPTSRAVSRA AEIMEASVQA VRTRVYGKLG RSWPLTDTLP 

       130        140        150        160        170        180 
EAVLDTIANA SGCRPHMLPP RCPDTCLARK YRLITGACNN RDHPRWGASN TALARWLPPA 

       190        200        210        220        230        240 
YEDGISEPRG WNPHVLYSGF PLPPVREVTR QVIRVPNEAV TEDDQYSDLL TVWGQYIDHD 

       250        260        270        280        290        300 
VAFTPQSASG AAFGAGADCQ LTCENRSPCF PIQLPPDASG PACLPFSRSS AACGTGIQGA 

       310        320        330        340        350        360 
FFGNLSSANP RQQMNGLTSF LDASTVYGSS PALEKQLRNW TSAEGLLRVN TRHWDAGRAH 

       370        380        390        400        410        420 
LPFMRPPAPL ACVPEPGTRG TAGAPCFLAG DSRASEVPTL AALHTLWLRE HNRLASALKA 

       430        440        450        460        470        480 
LNAHWSADTA YQEARKVVGA LHQIITLRDY VPKVLGPEAF QQHVGPYEGY DPTMDPTVSN 

       490        500        510        520        530        540 
VFSTAAFRFG HATVHPLVRR LDARFQEHPG LPPLRLQDAF FSPWRLLKEG GLDPLLRGLL 

       550        560        570        580        590        600 
ASPAKLPVQE QLMNEELTER LFVLGSSGSL DLGSINLQRG RDHGLPGYNA WREFCGLGRL 

       610        620        630        640        650        660 
HTRAELRSAV ANATLAGRIM DLYGHPDNID VWLGGLAEPL LPRARTGPLF ACLIGRQMKA 

       670        680        690        700        710        720 
LRDGDRFWWE SSGVFTDEQR RELARHSLSR VICDNTGLPS VPADAFQVSR FPQDFEPCEN 

       730        740        750        760        770        780 
IPGLNLDVWR EALPQGDACG LPDSLDNGDV VLCGEAGRRV LVFSCRHGFK LQGPEQVACS 

       790        800        810        820        830        840 
PRGGAVRAPV CRDINECEDA SHPPCHGSAR CRNTKGGFRC ECTDPAVLGE DGTTCVDSGR 

       850        860        870        880        890        900 
LPKASLVSIA LGIVLVVGLA GLTWTLVCRW AHAGRKASLS IAELGGRGAP PPGRGAGQDG 

       910        920        930 
ASGSLVPPLG PQGRTRAVDP TSSRSHVAQG SPA
Q8HYB7 in FASTA format

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