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Q8HYB7

- PERT_CANFA

UniProt

Q8HYB7 - PERT_CANFA

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Protein

Thyroid peroxidase

Gene
TPO
Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

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 By similarity.
Binds 1 heme B (iron-protoporphyrin IX) group covalently per heterodimer By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei250 – 2501Heme (covalent; via 2 links) By similarity
Active sitei251 – 2511Proton acceptor By similarity
Metal bindingi252 – 2521Calcium By similarity
Metal bindingi330 – 3301Calcium By similarity
Metal bindingi332 – 3321Calcium; via carbonyl oxygen By similarity
Metal bindingi334 – 3341Calcium By similarity
Metal bindingi336 – 3361Calcium By similarity
Sitei405 – 4051Transition state stabilizer By similarity
Binding sitei408 – 4081Heme (covalent; via 2 links) By similarity
Metal bindingi503 – 5031Iron (heme axial ligand) By similarity

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
Complete GO annotation...

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

PeroxiBasei3334. CfaTPO.

Names & Taxonomyi

Protein namesi
Recommended name:
Thyroid peroxidase (EC:1.11.1.8)
Short name:
TPO
Gene namesi
Name:TPO
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254: Chromosome 17

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini31 – 858828Extracellular Reviewed predictionAdd
BLAST
Transmembranei859 – 87921Helical; Reviewed predictionAdd
BLAST
Topological domaini880 – 94465Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. mitochondrion Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030 Reviewed predictionAdd
BLAST
Chaini31 – 944914Thyroid peroxidasePRO_0000023661Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi141 – 1411N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi154 ↔ 170 By similarity
Disulfide bondi271 ↔ 281 By similarity
Disulfide bondi275 ↔ 295 By similarity
Glycosylationi316 – 3161N-linked (GlcNAc...) Reviewed prediction
Glycosylationi351 – 3511N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi606 ↔ 663 By similarity
Glycosylationi623 – 6231N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi704 ↔ 729 By similarity
Disulfide bondi750 ↔ 790 By similarity
Disulfide bondi776 ↔ 802 By similarity
Disulfide bondi808 ↔ 822 By similarity
Disulfide bondi816 ↔ 831 By similarity
Disulfide bondi833 ↔ 846 By 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.
Cleaved in its N-terminal part By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Interacts with DUOX1, DUOX2 and CYBA By similarity.

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000004788.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini748 – 80457SushiAdd
BLAST
Domaini804 – 84744EGF-like; calcium-binding Reviewed predictionAdd
BLAST

Sequence similaritiesi

Contains 1 EGF-like domain.

Keywords - Domaini

EGF-like domain, Signal, Sushi, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG262194.
GeneTreeiENSGT00550000074325.
HOGENOMiHOG000016084.
HOVERGENiHBG000071.
InParanoidiQ8HYB7.
KOiK00431.
OMAiIMETSIQ.
OrthoDBiEOG7D2FD6.
TreeFamiTF314316.

Family and domain databases

Gene3Di1.10.640.10. 2 hits.
InterProiIPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
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.
[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.
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.

Q8HYB7-1 [UniParc]FASTAAdd to Basket

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MVGLVPAGSA WGGRALAVLG VTLLVALARG LLPFFLGGRD LLWGQSGEAS    50
VLGVVEESRR VVDGAIQHTV RRDLSKRGLP SPSQLLSFSK LPEPTSRAVS 100
RAAEIMEASV QAVRTRVYGK LGRSWPLTDT LPEAVLDTIA NASGCRPHML 150
PPRCPDTCLA RKYRLITGAC NNRDHPRWGA SNTALARWLP PAYEDGISEP 200
RGWNPHVLYS GFPLPPVREV TRQVIRVPNE AVTEDDQYSD LLTVWGQYID 250
HDVAFTPQSA SGAAFGAGAD CQLTCENRSP CFPIQLPPDA SGPACLPFSR 300
SSAACGTGIQ GAFFGNLSSA NPRQQMNGLT SFLDASTVYG SSPALEKQLR 350
NWTSAEGLLR VNTRHWDAGR AHLPFMRPPA PLACVPEPGT RGTAGAPCFL 400
AGDSRASEVP TLAALHTLWL REHNRLASAL KALNAHWSAD TAYQEARKVV 450
GALHQIITLR DYVPKVLGPE AFQQHVGPYE GYDPTMDPTV SNVFSTAAFR 500
LGHATVHPLV RRLDARFQEH PGLPPLGLQD AFFPWRLLKE GGLDPLLRGL 550
LASPAKLPVQ EQLMNEELTE RLFVLGSSGS LDLASINLQR GRDHGLPGYN 600
AWREFCGLGR LHTRAELRSA VANATLAGRI MDLYGHPDNI DVWLGGLAEP 650
LLPRARTGPL FACLIGRQMK ALRDGDRFWW ESSGVFTDEQ RRELARHSLS 700
RVICDNTGLP SVPADAFQVS RFPQDFEPCE NIPGLNLDVW REALPQGDAC 750
GLPDSLDNGD VVLCGEAGRR VLVFSCRHGF KLQGPEQVAC SPRGGAVRAP 800
VCRDINECED ASHPPCHGSA RCRNTKGGFR CECTDPAVLG EDGTTCVDSG 850
RLPKASLVSI ALGIVLVVGL AGLTWTLVCR WAHAGRKASL SIAELGGRGA 900
PPPGRGAGQD GASGSLVPPL GPQGRTRAVD PTSSRSHVAQ GSPA 944
Length:944
Mass (Da):101,406
Last modified:October 3, 2012 - v2
Checksum:i95031FB3A3FEFBD1
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti232 – 2321V → I in AAM26737. 1 Publication
Sequence conflicti501 – 5011L → F in AAM26737. 1 Publication
Sequence conflicti527 – 5271G → R in AAM26737. 1 Publication
Sequence conflicti533 – 5331F → FS in AAM26737. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY094504 mRNA. Translation: AAM26737.2.
JH373195 Genomic DNA. No translation available.
RefSeqiNP_001003009.2. NM_001003009.2.
UniGeneiCfa.20.

Genome annotation databases

EnsembliENSCAFT00000005172; ENSCAFP00000004788; ENSCAFG00000003217.
GeneIDi403521.
KEGGicfa:403521.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY094504 mRNA. Translation: AAM26737.2 .
JH373195 Genomic DNA. No translation available.
RefSeqi NP_001003009.2. NM_001003009.2.
UniGenei Cfa.20.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9615.ENSCAFP00000004788.

Protein family/group databases

PeroxiBasei 3334. CfaTPO.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSCAFT00000005172 ; ENSCAFP00000004788 ; ENSCAFG00000003217 .
GeneIDi 403521.
KEGGi cfa:403521.

Organism-specific databases

CTDi 7173.

Phylogenomic databases

eggNOGi NOG262194.
GeneTreei ENSGT00550000074325.
HOGENOMi HOG000016084.
HOVERGENi HBG000071.
InParanoidi Q8HYB7.
KOi K00431.
OMAi IMETSIQ.
OrthoDBi EOG7D2FD6.
TreeFami TF314316.

Enzyme and pathway databases

UniPathwayi UPA00194 .

Miscellaneous databases

NextBioi 20817032.

Family and domain databases

Gene3Di 1.10.640.10. 2 hits.
InterProi IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
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.
[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.
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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Thyroid.
  2. "Genome sequence, comparative analysis and haplotype structure of the domestic dog."
    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.
    Nature 438:803-819(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Boxer.
  3. Dodgson S.E., Day R., Fyfe J.C.
    Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO N-TERMINUS.

Entry informationi

Entry nameiPERT_CANFA
AccessioniPrimary (citable) accession number: Q8HYB7
Secondary accession number(s): F1Q066
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: October 3, 2012
Last modified: September 3, 2014
This is version 105 of the entry and version 2 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

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