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Thyroid peroxidase (TPO) (EC 1.11.1.8)

 PERT_CANLF              Reviewed;         944 AA.
Q8HYB7; F1Q066;
23-APR-2003, integrated into UniProtKB/Swiss-Prot.
03-OCT-2012, sequence version 2.
23-MAY-2018, entry version 133.
RecName: Full=Thyroid peroxidase;
Short=TPO;
EC=1.11.1.8 {ECO:0000250|UniProtKB:P09933};
Flags: Precursor;
Name=TPO;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Thyroid;
PubMed=12564727; DOI=10.1111/j.1939-1676.2003.tb01323.x;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Boxer;
PubMed=16341006; DOI=10.1038/nature04338;
Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C.,
Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A.,
Ponting C.P., Galibert F., Smith D.R., deJong P.J., Kirkness E.F.,
Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A.,
Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M.,
Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L.,
Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J.,
Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L.,
Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A.,
Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L.,
Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N.,
Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A.,
Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N.,
Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N.,
Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K.,
Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G.,
Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E.,
Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C.,
Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L.,
Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C.,
Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T.,
Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J.,
Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J.,
Marabella R., Maru K., Matthews C., McDonough S., Mehta T.,
Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K.,
Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J.,
Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K.,
Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F.,
Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C.,
Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S.,
Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J.,
Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S.,
Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S.,
Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T.,
Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T.,
Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X.,
Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.;
"Genome sequence, comparative analysis and haplotype structure of the
domestic dog.";
Nature 438:803-819(2005).
[3]
SEQUENCE REVISION TO N-TERMINUS.
Dodgson S.E., Day R., Fyfe J.C.;
Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Iodination and coupling of the hormonogenic tyrosines in
thyroglobulin to yield the thyroid hormones T(3) and T(4).
{ECO:0000250|UniProtKB:P09933}.
-!- CATALYTIC ACTIVITY: 2 iodide + H(2)O(2) + 2 H(+) = diiodine + 2
H(2)O. {ECO:0000250|UniProtKB:P09933}.
-!- CATALYTIC ACTIVITY: [Thyroglobulin]-L-tyrosine + iodide + H(2)O(2)
= [thyroglobulin]-3-iodo-L-tyrosine + 2 H(2)O.
{ECO:0000250|UniProtKB:P09933}.
-!- CATALYTIC ACTIVITY: [Thyroglobulin]-3-iodo-L-tyrosine + iodide +
H(2)O(2) = [thyroglobulin]-3,5-diiodo-L-tyrosine + 2 H(2)O.
{ECO:0000250|UniProtKB:P09933}.
-!- CATALYTIC ACTIVITY: 2 [thyroglobulin]-3,5-diiodo-L-tyrosine +
H(2)O(2) = [thyroglobulin]-L-thyroxine + [thyroglobulin]-
aminoacrylate + 2 H(2)O. {ECO:0000250|UniProtKB:P09933}.
-!- CATALYTIC ACTIVITY: [Thyroglobulin]-3-iodo-L-tyrosine +
[thyroglobulin]-3,5-diiodo-L-tyrosine + H(2)O(2) =
[thyroglobulin]-3,5,3'-triiodo-L-thyronine + [thyroglobulin]-
aminoacrylate + 2 H(2)O. {ECO:0000250|UniProtKB:P09933}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00298};
Note=Binds 1 Ca(2+) ion per heterodimer. {ECO:0000255|PROSITE-
ProRule:PRU00298};
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00298};
Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently
per heterodimer. {ECO:0000255|PROSITE-ProRule:PRU00298};
-!- PATHWAY: Hormone biosynthesis; thyroid hormone biosynthesis.
-!- SUBUNIT: Interacts with DUOX1, DUOX2 and CYBA. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
membrane protein {ECO:0000250}.
-!- 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).
{ECO:0000250}.
-!- PTM: Cleaved in its N-terminal part. {ECO:0000250}.
-!- DISEASE: Note=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.
{ECO:0000255|PROSITE-ProRule:PRU00298}.
-----------------------------------------------------------------------
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EMBL; AY094504; AAM26737.2; -; mRNA.
EMBL; JH373195; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; NP_001003009.2; NM_001003009.2.
UniGene; Cfa.20; -.
SMR; Q8HYB7; -.
STRING; 9615.ENSCAFP00000004788; -.
PeroxiBase; 3334; CfaTPO.
PaxDb; Q8HYB7; -.
PRIDE; Q8HYB7; -.
Ensembl; ENSCAFT00000005172; ENSCAFP00000004788; ENSCAFG00000003217.
GeneID; 403521; -.
KEGG; cfa:403521; -.
CTD; 7173; -.
VGNC; VGNC:47746; TPO.
eggNOG; KOG2408; Eukaryota.
eggNOG; ENOG410XPZ3; LUCA.
GeneTree; ENSGT00550000074325; -.
HOGENOM; HOG000016084; -.
HOVERGEN; HBG000071; -.
InParanoid; Q8HYB7; -.
KO; K00431; -.
OMA; TCVDSGR; -.
OrthoDB; EOG091G0236; -.
TreeFam; TF314316; -.
Reactome; R-CFA-209968; Thyroxine biosynthesis.
UniPathway; UPA00194; -.
Proteomes; UP000002254; Chromosome 17.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0004447; F:iodide peroxidase activity; IEA:UniProtKB-EC.
GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
GO; GO:0035162; P:embryonic hemopoiesis; IEA:Ensembl.
GO; GO:0042446; P:hormone biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
GO; GO:0006590; P:thyroid hormone generation; IEA:UniProtKB-UniPathway.
CDD; cd00033; CCP; 1.
Gene3D; 1.10.640.10; -; 1.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR010255; Haem_peroxidase.
InterPro; IPR019791; Haem_peroxidase_animal.
InterPro; IPR037120; Haem_peroxidase_sf.
InterPro; IPR035976; Sushi/SCR/CCP_sf.
InterPro; IPR000436; Sushi_SCR_CCP_dom.
InterPro; IPR029589; TPO.
PANTHER; PTHR11475:SF60; PTHR11475:SF60; 1.
Pfam; PF03098; An_peroxidase; 1.
Pfam; PF07645; EGF_CA; 1.
PRINTS; PR00457; ANPEROXIDASE.
SMART; SM00032; CCP; 1.
SMART; SM00179; EGF_CA; 1.
SUPFAM; SSF48113; SSF48113; 1.
SUPFAM; SSF57535; SSF57535; 1.
PROSITE; PS00010; ASX_HYDROXYL; 1.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS01187; EGF_CA; 1.
PROSITE; PS00435; PEROXIDASE_1; 1.
PROSITE; PS50292; PEROXIDASE_3; 1.
PROSITE; PS50923; SUSHI; 1.
2: Evidence at transcript level;
Calcium; Complete proteome; Disulfide bond; EGF-like domain;
Glycoprotein; Heme; Hydrogen peroxide; Iron; Membrane; Metal-binding;
Oxidoreductase; Peroxidase; Reference proteome; Signal; Sushi;
Thyroid hormones biosynthesis; Transmembrane; Transmembrane helix.
SIGNAL 1 30 {ECO:0000255}.
CHAIN 31 944 Thyroid peroxidase.
/FTId=PRO_0000023661.
TOPO_DOM 31 858 Extracellular. {ECO:0000255}.
TRANSMEM 859 879 Helical. {ECO:0000255}.
TOPO_DOM 880 944 Cytoplasmic. {ECO:0000255}.
DOMAIN 748 804 Sushi. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 804 847 EGF-like; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
ACT_SITE 251 251 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00298}.
METAL 252 252 Calcium. {ECO:0000255|PROSITE-
ProRule:PRU00298}.
METAL 330 330 Calcium. {ECO:0000255|PROSITE-
ProRule:PRU00298}.
METAL 332 332 Calcium; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00298}.
METAL 334 334 Calcium. {ECO:0000255|PROSITE-
ProRule:PRU00298}.
METAL 336 336 Calcium. {ECO:0000255|PROSITE-
ProRule:PRU00298}.
METAL 503 503 Iron (heme axial ligand).
{ECO:0000255|PROSITE-ProRule:PRU00298}.
BINDING 250 250 Heme (covalent; via 2 links).
{ECO:0000250}.
BINDING 408 408 Heme (covalent; via 2 links).
{ECO:0000250}.
SITE 405 405 Transition state stabilizer.
{ECO:0000255|PROSITE-ProRule:PRU00298}.
CARBOHYD 141 141 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 316 316 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 351 351 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 623 623 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 154 170 {ECO:0000250}.
DISULFID 271 281 {ECO:0000250}.
DISULFID 275 295 {ECO:0000250}.
DISULFID 606 663 {ECO:0000250}.
DISULFID 704 729 {ECO:0000250}.
DISULFID 750 790 {ECO:0000250}.
DISULFID 776 802 {ECO:0000250}.
DISULFID 808 822 {ECO:0000250}.
DISULFID 816 831 {ECO:0000250}.
DISULFID 833 846 {ECO:0000250}.
CONFLICT 232 232 V -> I (in Ref. 1; AAM26737).
{ECO:0000305}.
CONFLICT 501 501 L -> F (in Ref. 1; AAM26737).
{ECO:0000305}.
CONFLICT 527 527 G -> R (in Ref. 1; AAM26737).
{ECO:0000305}.
CONFLICT 533 533 F -> FS (in Ref. 1; AAM26737).
{ECO:0000305}.
SEQUENCE 944 AA; 101406 MW; 95031FB3A3FEFBD1 CRC64;
MVGLVPAGSA WGGRALAVLG VTLLVALARG LLPFFLGGRD LLWGQSGEAS VLGVVEESRR
VVDGAIQHTV RRDLSKRGLP SPSQLLSFSK LPEPTSRAVS RAAEIMEASV QAVRTRVYGK
LGRSWPLTDT LPEAVLDTIA NASGCRPHML PPRCPDTCLA RKYRLITGAC NNRDHPRWGA
SNTALARWLP PAYEDGISEP RGWNPHVLYS GFPLPPVREV TRQVIRVPNE AVTEDDQYSD
LLTVWGQYID HDVAFTPQSA SGAAFGAGAD CQLTCENRSP CFPIQLPPDA SGPACLPFSR
SSAACGTGIQ GAFFGNLSSA NPRQQMNGLT SFLDASTVYG SSPALEKQLR NWTSAEGLLR
VNTRHWDAGR AHLPFMRPPA PLACVPEPGT RGTAGAPCFL AGDSRASEVP TLAALHTLWL
REHNRLASAL KALNAHWSAD TAYQEARKVV GALHQIITLR DYVPKVLGPE AFQQHVGPYE
GYDPTMDPTV SNVFSTAAFR LGHATVHPLV RRLDARFQEH PGLPPLGLQD AFFPWRLLKE
GGLDPLLRGL LASPAKLPVQ EQLMNEELTE RLFVLGSSGS LDLASINLQR GRDHGLPGYN
AWREFCGLGR LHTRAELRSA VANATLAGRI MDLYGHPDNI DVWLGGLAEP LLPRARTGPL
FACLIGRQMK ALRDGDRFWW ESSGVFTDEQ RRELARHSLS RVICDNTGLP SVPADAFQVS
RFPQDFEPCE NIPGLNLDVW REALPQGDAC GLPDSLDNGD VVLCGEAGRR VLVFSCRHGF
KLQGPEQVAC SPRGGAVRAP VCRDINECED ASHPPCHGSA RCRNTKGGFR CECTDPAVLG
EDGTTCVDSG RLPKASLVSI ALGIVLVVGL AGLTWTLVCR WAHAGRKASL SIAELGGRGA
PPPGRGAGQD GASGSLVPPL GPQGRTRAVD PTSSRSHVAQ GSPA


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