Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Thyroid peroxidase (TPO) (EC 1.11.1.8)

 PERT_HUMAN              Reviewed;         933 AA.
P07202; P09934; P09935; Q8IUL0; Q8NF94; Q8NF95; Q8NF96; Q8NF97;
Q8TCI9;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
13-NOV-2007, sequence version 4.
28-FEB-2018, entry version 223.
RecName: Full=Thyroid peroxidase {ECO:0000305};
Short=TPO;
EC=1.11.1.8 {ECO:0000250|UniProtKB:P09933};
Flags: Precursor;
Name=TPO {ECO:0000312|HGNC:HGNC:12015};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS PRO-725
AND ALA-847.
PubMed=3475693; DOI=10.1073/pnas.84.16.5555;
Kimura S., Kotani T., McBride O.W., Umeki K., Hirai K., Nakayama T.,
Ohtaki S.;
"Human thyroid peroxidase: complete cDNA and protein sequence,
chromosome mapping, and identification of two alternately spliced
mRNAs.";
Proc. Natl. Acad. Sci. U.S.A. 84:5555-5559(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS PRO-725 AND
ALA-847.
TISSUE=Thyroid;
PubMed=3453124; DOI=10.1093/nar/15.16.6735;
Libert F., Ruel J., Ludgate M., Swillens S., Alexander N., Vassart G.,
Dinsart C.;
"Complete nucleotide sequence of the human thyroperoxidase-microsomal
antigen cDNA.";
Nucleic Acids Res. 15:6735-6735(1987).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=2548579; DOI=10.1021/bi00436a054;
Kimura S., Hong Y.S., Kotani T., Ohtaki S., Kikkawa F.;
"Structure of the human thyroid peroxidase gene: comparison and
relationship to the human myeloperoxidase gene.";
Biochemistry 28:4481-4489(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Thyroid;
PubMed=2308857; DOI=10.1093/nar/18.3.670;
Barnett P.S., Banga J.P., Watkins J., Huang G.C., Gluckman D.R.B.,
Page M.J., McGregor A.M.;
"Nucleotide sequence of the alternatively spliced human thyroid
peroxidase cDNA, TPO-2.";
Nucleic Acids Res. 18:670-670(1990).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-257.
TISSUE=Thyroid;
Rapoport B.;
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND VARIANTS SER-257; PRO-725
AND ALA-847.
TISSUE=Thyroid;
Hennen G.P., Igout A., Melen L.B.;
"Homo sapiens thyroid peroxidase (TPO) variant mRNA, alternatively
spliced sequence.";
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
[7]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 5; 6; 2-3 AND 2-4),
AND VARIANTS PRO-725 AND ALA-847.
TISSUE=Thyroid;
PubMed=12454013; DOI=10.1074/jbc.M209513200;
Ferrand M., Le Fourn V., Franc J.-L.;
"Increasing diversity of human thyroperoxidase generated by
alternative splicing. Characterization by molecular cloning of new
transcripts with single- and multispliced mRNAs.";
J. Biol. Chem. 278:3793-3800(2003).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 217-496.
PubMed=3654979; DOI=10.1172/JCI113181;
Seto P., Hirayu H., Magnusson R.P., Gestautas J., Portmann L.,
Degroot L.J., Rapoport B.;
"Isolation of a complementary DNA clone for thyroid microsomal
antigen. Homology with the gene for thyroid peroxidase.";
J. Clin. Invest. 80:1205-1208(1987).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 670-933 (ISOFORM 3), AND ALTERNATIVE
SPLICING IN GRAVES' DISEASE.
TISSUE=Thyroid;
PubMed=2383265; DOI=10.1016/0006-291X(90)92152-P;
Zanelli E., Henry M., Charvet B., Malthiery Y.;
"Evidence for an alternate splicing in the thyroperoxidase messenger
from patients with Graves' disease.";
Biochem. Biophys. Res. Commun. 170:735-741(1990).
[10]
INTERACTION WITH DUOX1; DUOX2 AND CYBA.
PubMed=15561711; DOI=10.1074/jbc.M407709200;
Wang D., De Deken X., Milenkovic M., Song Y., Pirson I., Dumont J.E.,
Miot F.;
"Identification of a novel partner of duox: EFP1, a thioredoxin-
related protein.";
J. Biol. Chem. 280:3096-3103(2005).
[11]
VARIANTS TDH2A ASP-453; SER-590 AND LYS-799, AND VARIANTS SER-257;
SER-373; THR-398 AND PRO-725.
PubMed=7550241; DOI=10.1002/humu.1380060104;
Bikker H., Vulsma T., Baas F., de Vijlder J.J.M.;
"Identification of five novel inactivating mutations in the human
thyroid peroxidase gene by denaturing gradient gel electrophoresis.";
Hum. Mutat. 6:9-16(1995).
[12]
VARIANT TDH2A PHE-447.
PubMed=9024270; DOI=10.1210/jcem.82.2.3729;
Bikker H., Baas F., De Vijlder J.J.M.;
"Molecular analysis of mutated thyroid peroxidase detected in patients
with total iodide organification defects.";
J. Clin. Endocrinol. Metab. 82:649-653(1997).
[13]
VARIANT TDH2A GLU-660.
PubMed=10468986; DOI=10.1046/j.1365-2265.1999.00746.x;
Santos C.L.S., Bikker H., Rego K.G.M., Nascimento A.C., Tambascia M.,
De Vijlder J.J.M., Medeiros-Neto G.;
"A novel mutation in the TPO gene in goitrous hypothyroid patients
with iodide organification defect.";
Clin. Endocrinol. (Oxf.) 51:165-172(1999).
[14]
VARIANTS TDH2A GLN-648 AND LYS-799.
PubMed=10084596; DOI=10.1210/jcem.84.3.5541;
Pannain S., Weiss R.E., Jackson C.E., Dian D., Beck J.C.,
Sheffield V.C., Cox N., Refetoff S.;
"Two different mutations in the thyroid peroxidase gene of a large
inbred Amish kindred: power and limits of homozygosity mapping.";
J. Clin. Endocrinol. Metab. 84:1061-1071(1999).
[15]
VARIANT TDH2A ASN-240, AND CHARACTERIZATION OF VARIANT TDH2A ASN-240.
PubMed=9924196; DOI=10.1677/joe.0.1600267;
Kotani T., Umeki K., Yamamoto I., Maesaka H., Tachibana K., Ohtaki S.;
"A novel mutation in the human thyroid peroxidase gene resulting in a
total iodide organification defect.";
J. Endocrinol. 160:267-273(1999).
[16]
VARIANTS TDH2A THR-326; PHE-447; ASP-453; CYS-527; TRP-693 AND
LYS-799.
PubMed=11061528; DOI=10.1210/jcem.85.10.6878;
Bakker B., Bikker H., Vulsma T., de Randamie J.S.E., Wiedijk B.M.,
De Vijlder J.J.M.;
"Two decades of screening for congenital hypothyroidism in The
Netherlands: TPO gene mutations in total iodide organification defects
(an update).";
J. Clin. Endocrinol. Metab. 85:3708-3712(2000).
[17]
VARIANTS TDH2A PRO-458 AND HIS-491.
PubMed=11415848; DOI=10.1530/eje.0.1450019;
Ambrugger P., Stoeva I., Biebermann H., Torresani T., Leitner C.,
Grueters A.;
"Novel mutations of the thyroid peroxidase gene in patients with
permanent congenital hypothyroidism.";
Eur. J. Endocrinol. 145:19-24(2001).
[18]
VARIANTS TDH2A TRP-665 AND ARG-771, AND CHARACTERIZATION OF VARIANTS
TDH2A TRP-665 AND ARG-771.
PubMed=11916616; DOI=10.1530/eje.0.1460491;
Umeki K., Kotani T., Kawano J., Suganuma T., Yamamoto I., Aratake Y.,
Furujo M., Ichiba Y.;
"Two novel missense mutations in the thyroid peroxidase gene, R665W
and G771R, result in a localization defect and cause congenital
hypothyroidism.";
Eur. J. Endocrinol. 146:491-498(2002).
[19]
VARIANT TDH2A PRO-53.
PubMed=12213873; DOI=10.1210/jc.2002-020153;
Niu D.-M., Hwang B., Chu Y.-K., Liao C.-J., Wang P.-L., Lin C.-Y.;
"High prevalence of a novel mutation (2268 insT) of the thyroid
peroxidase gene in Taiwanese patients with total iodide organification
defect, and evidence for a founder effect.";
J. Clin. Endocrinol. Metab. 87:4208-4212(2002).
[20]
VARIANTS TDH2A SER-493 AND TYR-796.
PubMed=11874711; DOI=10.1677/joe.0.1720627;
Wu J.-Y., Shu S.-G., Yang C.-F., Lee C.-C., Tsai F.-J.;
"Mutation analysis of thyroid peroxidase gene in Chinese patients with
total iodide organification defect: identification of five novel
mutations.";
J. Endocrinol. 172:627-635(2002).
[21]
VARIANT TDH2A ILE-839.
PubMed=12490071; DOI=10.1089/105072502320908277;
Calaciura F., Miscio G., Coco A., Leonardi D., Cisternino C.,
Regalbuto C., Bozzali M., Maiorana R., Ranieri A., Carta A.,
Buscema M., Trischitta V., Sava L., Tassi V.;
"Genetics of specific phenotypes of congenital hypothyroidism: a
population-based approach.";
Thyroid 12:945-951(2002).
[22]
VARIANTS TDH2A CYS-533 AND ASP-574-575-LEU DEL, AND CHARACTERIZATION
OF VARIANTS TDH2A CYS-533 AND ASP-574-575-LEU DEL.
PubMed=12864797; DOI=10.1046/j.1365-2265.2003.01823.x;
Kotani T., Umeki K., Kawano J., Suganuma T., Hishinuma A., Ieiri T.,
Harada S.;
"Partial iodide organification defect caused by a novel mutation of
the thyroid peroxidase gene in three siblings.";
Clin. Endocrinol. (Oxf.) 59:198-206(2003).
[23]
VARIANTS TDH2A THR-307; MET-433; LEU-499 AND ARG-808.
PubMed=12938097; DOI=10.1002/humu.9175;
Rivolta C.M., Esperante S.A., Gruneiro-Papendieck L., Chiesa A.,
Moya C.M., Domene S., Varela V., Targovnik H.M.;
"Five novel inactivating mutations in the thyroid peroxidase gene
responsible for congenital goiter and iodide organification defect.";
Hum. Mutat. 22:259-259(2003).
[24]
VARIANT TDH2A TRP-693.
PubMed=12843174; DOI=10.1210/jc.2002-021377;
Fugazzola L., Cerutti N., Mannavola D., Vannucchi G., Fallini C.,
Persani L., Beck-Peccoz P.;
"Monoallelic expression of mutant thyroid peroxidase allele causing
total iodide organification defect.";
J. Clin. Endocrinol. Metab. 88:3264-3271(2003).
[25]
VARIANT TDH2A LYS-378.
PubMed=16284446; DOI=10.1507/endocrj.52.643;
Tajima T., Tsubaki J., Fujieda K.;
"Two novel mutations in the thyroid peroxidase gene with goitrous
hypothyroidism.";
Endocr. J. 52:643-645(2005).
[26]
VARIANT TDH2A ASP-453.
PubMed=16684826; DOI=10.1210/jc.2006-0142;
Pfarr N., Borck G., Turk A., Napiontek U., Keilmann A.,
Mueller-Forell W., Kopp P., Pohlenz J.;
"Goitrous congenital hypothyroidism and hearing impairment associated
with mutations in the TPO and SLC26A4/PDS genes.";
J. Clin. Endocrinol. Metab. 91:2678-2681(2006).
[27]
VARIANTS TDH2A HIS-412 AND 596-GLU--LEU-933 DEL.
PubMed=27305979; DOI=10.1038/jhg.2016.62;
Mittal K., Rafiq M.A., Rafiullah R., Harripaul R., Ali H., Ayaz M.,
Aslam M., Naeem F., Amin-Ud-Din M., Waqas A., So J., Rappold G.A.,
Vincent J.B., Ayub M.;
"Mutations in the genes for thyroglobulin and thyroid peroxidase cause
thyroid dyshormonogenesis and autosomal-recessive intellectual
disability.";
J. Hum. Genet. 61:867-872(2016).
-!- 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:0000269|PubMed:15561711}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- SUBCELLULAR LOCATION: Isoform 3: Cell surface.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=TPO1;
IsoId=P07202-1; Sequence=Displayed;
Name=2; Synonyms=TPO2;
IsoId=P07202-2; Sequence=VSP_004665;
Note=Lacks exon 10. Found in normal thyroid tissues as well as
Graves'tissues. Rapidly degraded after synthesis, does not reach
the cell surface. Inactive.;
Name=3; Synonyms=TPO3, Graves' disease, TPOzaninelli;
IsoId=P07202-3; Sequence=VSP_004666;
Note=Lacks exon 16. Found in normal thyroid tissues as well as
Graves'tissues. Active.;
Name=4; Synonyms=TPO4;
IsoId=P07202-4; Sequence=VSP_007269;
Note=Lacks exon 14. Active.;
Name=5; Synonyms=TPO5;
IsoId=P07202-5; Sequence=VSP_007268;
Note=Lacks exon 8. Does not fold correctly. Does not reach the
cell surface.;
Name=6; Synonyms=TPO6;
IsoId=P07202-6; Sequence=VSP_004665, VSP_007270;
Note=Lacks exons 10, 12, 13, 14 and 16.;
Name=2-3;
IsoId=P07202-7; Sequence=VSP_004665, VSP_004666;
Note=Lacks exons 10 and 16.;
Name=2-4;
IsoId=P07202-8; Sequence=VSP_004665, VSP_007269;
Note=Lacks exons 10 and 14.;
-!- PTM: Glycosylated.
-!- 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.
-!- PTM: Cleaved in its N-terminal part.
-!- DISEASE: Note=An alternative splicing in the thyroperoxidase mRNA
can cause Graves' disease.
-!- DISEASE: Thyroid dyshormonogenesis 2A (TDH2A) [MIM:274500]: A
disorder due to defective conversion of accumulated iodide to
organically bound iodine. The iodide organification defect can be
partial or complete. {ECO:0000269|PubMed:10084596,
ECO:0000269|PubMed:10468986, ECO:0000269|PubMed:11061528,
ECO:0000269|PubMed:11415848, ECO:0000269|PubMed:11874711,
ECO:0000269|PubMed:11916616, ECO:0000269|PubMed:12213873,
ECO:0000269|PubMed:12490071, ECO:0000269|PubMed:12843174,
ECO:0000269|PubMed:12864797, ECO:0000269|PubMed:12938097,
ECO:0000269|PubMed:16284446, ECO:0000269|PubMed:16684826,
ECO:0000269|PubMed:27305979, ECO:0000269|PubMed:7550241,
ECO:0000269|PubMed:9024270, ECO:0000269|PubMed:9924196}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the peroxidase family. XPO subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00298}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Thyroid peroxidase entry;
URL="https://en.wikipedia.org/wiki/Thyroid_peroxidase";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; J02969; AAA61215.1; -; mRNA.
EMBL; J02970; AAA61216.1; -; mRNA.
EMBL; Y00406; CAA68467.1; -; mRNA.
EMBL; M25715; AAA97517.1; -; Genomic_DNA.
EMBL; M25702; AAA97517.1; JOINED; Genomic_DNA.
EMBL; M25703; AAA97517.1; JOINED; Genomic_DNA.
EMBL; M25704; AAA97517.1; JOINED; Genomic_DNA.
EMBL; M25705; AAA97517.1; JOINED; Genomic_DNA.
EMBL; M25706; AAA97517.1; JOINED; Genomic_DNA.
EMBL; M25707; AAA97517.1; JOINED; Genomic_DNA.
EMBL; M25708; AAA97517.1; JOINED; Genomic_DNA.
EMBL; M25709; AAA97517.1; JOINED; Genomic_DNA.
EMBL; M25710; AAA97517.1; JOINED; Genomic_DNA.
EMBL; M25711; AAA97517.1; JOINED; Genomic_DNA.
EMBL; M25712; AAA97517.1; JOINED; Genomic_DNA.
EMBL; M25713; AAA97517.1; JOINED; Genomic_DNA.
EMBL; M25714; AAA97517.1; JOINED; Genomic_DNA.
EMBL; X17358; CAA35235.1; -; mRNA.
EMBL; M17755; AAA61217.2; -; mRNA.
EMBL; AF439430; AAL74416.1; -; mRNA.
EMBL; AF533528; AAN04471.1; -; mRNA.
EMBL; AY136822; AAN11302.1; -; mRNA.
EMBL; AF533529; AAN04472.1; -; mRNA.
EMBL; AF533530; AAN04473.1; -; mRNA.
EMBL; AF533531; AAN04474.1; -; mRNA.
EMBL; M55702; AAA61219.1; -; mRNA.
EMBL; M55702; AAA61218.1; -; mRNA.
CCDS; CCDS1643.1; -. [P07202-1]
CCDS; CCDS1644.1; -. [P07202-2]
CCDS; CCDS1646.1; -. [P07202-5]
PIR; A32413; OPHUIT.
RefSeq; NP_000538.3; NM_000547.5. [P07202-1]
RefSeq; NP_001193673.1; NM_001206744.1. [P07202-1]
RefSeq; NP_001193674.1; NM_001206745.1. [P07202-2]
RefSeq; NP_783650.1; NM_175719.3. [P07202-2]
RefSeq; NP_783652.1; NM_175721.3. [P07202-4]
RefSeq; NP_783653.1; NM_175722.3. [P07202-5]
RefSeq; XP_011508683.1; XM_011510381.2. [P07202-8]
UniGene; Hs.467554; -.
ProteinModelPortal; P07202; -.
SMR; P07202; -.
STRING; 9606.ENSP00000318820; -.
BindingDB; P07202; -.
ChEMBL; CHEMBL1839; -.
DrugBank; DB00389; Carbimazole.
DrugBank; DB00509; Dextrothyroxine.
DrugBank; DB00763; Methimazole.
DrugBank; DB00550; Propylthiouracil.
Allergome; 9554; Hom s TPO.
PeroxiBase; 3318; HsTPO01.
iPTMnet; P07202; -.
PhosphoSitePlus; P07202; -.
BioMuta; TPO; -.
DMDM; 160281455; -.
PaxDb; P07202; -.
PeptideAtlas; P07202; -.
PRIDE; P07202; -.
Ensembl; ENST00000329066; ENSP00000329869; ENSG00000115705. [P07202-1]
Ensembl; ENST00000345913; ENSP00000318820; ENSG00000115705. [P07202-1]
Ensembl; ENST00000346956; ENSP00000263886; ENSG00000115705. [P07202-4]
Ensembl; ENST00000382198; ENSP00000371633; ENSG00000115705. [P07202-5]
Ensembl; ENST00000382201; ENSP00000371636; ENSG00000115705. [P07202-2]
GeneID; 7173; -.
KEGG; hsa:7173; -.
UCSC; uc002qwr.4; human. [P07202-1]
CTD; 7173; -.
DisGeNET; 7173; -.
EuPathDB; HostDB:ENSG00000115705.20; -.
GeneCards; TPO; -.
H-InvDB; HIX0029848; -.
HGNC; HGNC:12015; TPO.
HPA; CAB009587; -.
HPA; HPA007987; -.
MalaCards; TPO; -.
MIM; 274500; phenotype.
MIM; 606765; gene.
neXtProt; NX_P07202; -.
OpenTargets; ENSG00000115705; -.
Orphanet; 95716; Familial thyroid dyshormonogenesis.
PharmGKB; PA36694; -.
eggNOG; KOG2408; Eukaryota.
eggNOG; ENOG410XPZ3; LUCA.
GeneTree; ENSGT00550000074325; -.
HOVERGEN; HBG000071; -.
InParanoid; P07202; -.
KO; K00431; -.
OMA; TCVDSGR; -.
OrthoDB; EOG091G0236; -.
PhylomeDB; P07202; -.
TreeFam; TF314316; -.
BRENDA; 3.6.1.52; 2681.
Reactome; R-HSA-209968; Thyroxine biosynthesis.
UniPathway; UPA00194; -.
ChiTaRS; TPO; human.
GenomeRNAi; 7173; -.
PRO; PR:P07202; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000115705; -.
ExpressionAtlas; P07202; baseline and differential.
Genevisible; P07202; HS.
GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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; IDA:DFLAT.
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; TAS:Reactome.
CDD; cd00033; CCP; 1.
Gene3D; 1.10.640.10; -; 1.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
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.
Pfam; PF00084; Sushi; 1.
PRINTS; PR00457; ANPEROXIDASE.
SMART; SM00032; CCP; 1.
SMART; SM00181; EGF; 1.
SMART; SM00179; EGF_CA; 1.
SUPFAM; SSF48113; SSF48113; 1.
SUPFAM; SSF57535; SSF57535; 1.
PROSITE; PS00010; ASX_HYDROXYL; 1.
PROSITE; PS01186; EGF_2; 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.
1: Evidence at protein level;
Alternative splicing; Calcium; Complete proteome;
Congenital hypothyroidism; Disease mutation; Disulfide bond;
EGF-like domain; Glycoprotein; Heme; Hydrogen peroxide; Iron;
Membrane; Metal-binding; Oxidoreductase; Peroxidase; Polymorphism;
Reference proteome; Signal; Sushi; Thyroid hormones biosynthesis;
Transmembrane; Transmembrane helix.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 933 Thyroid peroxidase.
/FTId=PRO_0000023662.
TOPO_DOM 19 846 Extracellular. {ECO:0000255}.
TRANSMEM 847 871 Helical. {ECO:0000255}.
TOPO_DOM 872 933 Cytoplasmic. {ECO:0000255}.
DOMAIN 740 795 Sushi. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 796 839 EGF-like; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
ACT_SITE 239 239 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00298}.
METAL 240 240 Calcium. {ECO:0000255|PROSITE-
ProRule:PRU00298}.
METAL 321 321 Calcium. {ECO:0000255|PROSITE-
ProRule:PRU00298}.
METAL 323 323 Calcium; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00298}.
METAL 325 325 Calcium. {ECO:0000255|PROSITE-
ProRule:PRU00298}.
METAL 327 327 Calcium. {ECO:0000255|PROSITE-
ProRule:PRU00298}.
METAL 494 494 Iron (heme axial ligand).
{ECO:0000255|PROSITE-ProRule:PRU00298}.
BINDING 238 238 Heme (covalent; via 2 links).
{ECO:0000250}.
BINDING 399 399 Heme (covalent; via 2 links).
{ECO:0000250}.
SITE 396 396 Transition state stabilizer.
{ECO:0000255|PROSITE-ProRule:PRU00298}.
CARBOHYD 129 129 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 307 307 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 342 342 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 569 569 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 142 158 {ECO:0000250}.
DISULFID 259 269 {ECO:0000250}.
DISULFID 263 286 {ECO:0000250}.
DISULFID 598 655 {ECO:0000250}.
DISULFID 696 721 {ECO:0000250}.
DISULFID 800 814 {ECO:0000250}.
DISULFID 808 823 {ECO:0000250}.
DISULFID 825 838 {ECO:0000250}.
VAR_SEQ 274 446 Missing (in isoform 5).
{ECO:0000303|Ref.6}.
/FTId=VSP_007268.
VAR_SEQ 534 590 Missing (in isoform 2, isoform 2-3,
isoform 2-4 and isoform 6).
{ECO:0000303|PubMed:2308857,
ECO:0000303|PubMed:3475693}.
/FTId=VSP_004665.
VAR_SEQ 669 933 Missing (in isoform 6). {ECO:0000305}.
/FTId=VSP_007270.
VAR_SEQ 796 839 Missing (in isoform 4 and isoform 2-4).
{ECO:0000305}.
/FTId=VSP_007269.
VAR_SEQ 874 933 TRTGTKSTLPISETGGGTPELRCGKHQAVGTSPQRAAAQDS
EQESAGMEGRDTHRLPRAL -> RVLGWKAGILTGCREPSE
GKVAGHCRTASCSQNHRTTLFQTQANRKSAGRLFSQHG
(in isoform 3 and isoform 2-3).
{ECO:0000303|PubMed:2383265}.
/FTId=VSP_004666.
VARIANT 53 53 A -> P (in TDH2A).
{ECO:0000269|PubMed:12213873}.
/FTId=VAR_021622.
VARIANT 240 240 D -> N (in TDH2A; loss of activity).
{ECO:0000269|PubMed:9924196}.
/FTId=VAR_021623.
VARIANT 257 257 A -> S (in dbSNP:rs4927611).
{ECO:0000269|PubMed:7550241,
ECO:0000269|Ref.5, ECO:0000269|Ref.6}.
/FTId=VAR_006057.
VARIANT 307 307 N -> T (in TDH2A).
{ECO:0000269|PubMed:12938097}.
/FTId=VAR_021624.
VARIANT 326 326 A -> T (in TDH2A; dbSNP:rs371367459).
{ECO:0000269|PubMed:11061528}.
/FTId=VAR_021625.
VARIANT 373 373 A -> S (in dbSNP:rs2280132).
{ECO:0000269|PubMed:7550241}.
/FTId=VAR_006058.
VARIANT 378 378 E -> K (in TDH2A).
{ECO:0000269|PubMed:16284446}.
/FTId=VAR_025784.
VARIANT 398 398 S -> T (in dbSNP:rs2175977).
{ECO:0000269|PubMed:7550241}.
/FTId=VAR_006059.
VARIANT 412 412 R -> H (in TDH2A; unknown pathological
significance).
{ECO:0000269|PubMed:27305979}.
/FTId=VAR_078336.
VARIANT 433 433 V -> M (in TDH2A; dbSNP:rs1035791118).
{ECO:0000269|PubMed:12938097}.
/FTId=VAR_021626.
VARIANT 447 447 I -> F (in TDH2A; dbSNP:rs104893669).
{ECO:0000269|PubMed:11061528,
ECO:0000269|PubMed:9024270}.
/FTId=VAR_015375.
VARIANT 453 453 Y -> D (in TDH2A; dbSNP:rs121908083).
{ECO:0000269|PubMed:11061528,
ECO:0000269|PubMed:16684826,
ECO:0000269|PubMed:7550241}.
/FTId=VAR_006060.
VARIANT 458 458 L -> P (in TDH2A).
{ECO:0000269|PubMed:11415848}.
/FTId=VAR_021627.
VARIANT 491 491 R -> H (in TDH2A; dbSNP:rs201165648).
{ECO:0000269|PubMed:11415848}.
/FTId=VAR_021628.
VARIANT 493 493 G -> S (in TDH2A; dbSNP:rs778515113).
{ECO:0000269|PubMed:11874711}.
/FTId=VAR_021629.
VARIANT 499 499 P -> L (in TDH2A).
{ECO:0000269|PubMed:12938097}.
/FTId=VAR_021630.
VARIANT 527 527 W -> C (in TDH2A; dbSNP:rs779434941).
{ECO:0000269|PubMed:11061528}.
/FTId=VAR_021631.
VARIANT 533 533 G -> C (in TDH2A; partial defect;
expression slightly lower in efficiency
and more degenerative than wild-type
enzyme). {ECO:0000269|PubMed:12864797}.
/FTId=VAR_027229.
VARIANT 574 575 Missing (in TDH2A; partial defect;
expressed on the plasma membrane surface
at less than half the rate of wild-type
enzyme).
/FTId=VAR_027230.
VARIANT 590 590 G -> S (in TDH2A; dbSNP:rs121908084).
{ECO:0000269|PubMed:7550241}.
/FTId=VAR_027231.
VARIANT 596 933 Missing (in TDH2A; unknown pathological
significance).
{ECO:0000269|PubMed:27305979}.
/FTId=VAR_078337.
VARIANT 618 618 V -> M (in dbSNP:rs10189135).
/FTId=VAR_027232.
VARIANT 648 648 R -> Q (in TDH2A; dbSNP:rs121908086).
{ECO:0000269|PubMed:10084596}.
/FTId=VAR_013138.
VARIANT 660 660 Q -> E (in TDH2A; dbSNP:rs121908088).
{ECO:0000269|PubMed:10468986}.
/FTId=VAR_021632.
VARIANT 665 665 R -> W (in TDH2A; fails to localize to
the plasma membrane; dbSNP:rs776742629).
{ECO:0000269|PubMed:11916616}.
/FTId=VAR_021633.
VARIANT 693 693 R -> W (in TDH2A; dbSNP:rs121908087).
{ECO:0000269|PubMed:11061528,
ECO:0000269|PubMed:12843174}.
/FTId=VAR_021634.
VARIANT 706 706 M -> V (in dbSNP:rs13431173).
/FTId=VAR_027233.
VARIANT 725 725 T -> P (in dbSNP:rs732609).
{ECO:0000269|PubMed:12454013,
ECO:0000269|PubMed:3453124,
ECO:0000269|PubMed:3475693,
ECO:0000269|PubMed:7550241,
ECO:0000269|Ref.6}.
/FTId=VAR_006061.
VARIANT 771 771 G -> R (in TDH2A; fails to localize to
the plasma membrane; dbSNP:rs138931129).
{ECO:0000269|PubMed:11916616}.
/FTId=VAR_021635.
VARIANT 793 793 L -> P (in dbSNP:rs28991293).
/FTId=VAR_027234.
VARIANT 796 796 D -> Y (in TDH2A).
{ECO:0000269|PubMed:11874711}.
/FTId=VAR_021636.
VARIANT 799 799 E -> K (in TDH2A; dbSNP:rs121908085).
{ECO:0000269|PubMed:10084596,
ECO:0000269|PubMed:11061528,
ECO:0000269|PubMed:7550241}.
/FTId=VAR_006062.
VARIANT 808 808 C -> R (in TDH2A; dbSNP:rs935058009).
{ECO:0000269|PubMed:12938097}.
/FTId=VAR_021637.
VARIANT 839 839 V -> I (in TDH2A; dbSNP:rs146351101).
{ECO:0000269|PubMed:12490071}.
/FTId=VAR_027235.
VARIANT 846 846 R -> W (in dbSNP:rs28913014).
/FTId=VAR_027236.
VARIANT 847 847 V -> A (in dbSNP:rs1126799).
{ECO:0000269|PubMed:12454013,
ECO:0000269|PubMed:3453124,
ECO:0000269|PubMed:3475693,
ECO:0000269|Ref.6}.
/FTId=VAR_027237.
CONFLICT 70 70 P -> G (in Ref. 5; AAA61217).
{ECO:0000305}.
CONFLICT 354 354 A -> G (in Ref. 5 and 8). {ECO:0000305}.
CONFLICT 371 371 A -> R (in Ref. 1; AAA61215/AAA61216).
{ECO:0000305}.
CONFLICT 381 381 I -> N (in Ref. 5 and 8). {ECO:0000305}.
CONFLICT 574 574 D -> N (in Ref. 2; CAA68467).
{ECO:0000305}.
CONFLICT 732 732 W -> C (in Ref. 7; AAN11302).
{ECO:0000305}.
CONFLICT 748 748 V -> M (in Ref. 2 and 7). {ECO:0000305}.
CONFLICT 816 816 N -> S (in Ref. 6; AAL74416).
{ECO:0000305}.
CONFLICT 872 872 R -> K (in Ref. 2 and 7). {ECO:0000305}.
SEQUENCE 933 AA; 102963 MW; F67C5F1A4AEE0B29 CRC64;
MRALAVLSVT LVMACTEAFF PFISRGKELL WGKPEESRVS SVLEESKRLV DTAMYATMQR
NLKKRGILSP AQLLSFSKLP EPTSGVIARA AEIMETSIQA MKRKVNLKTQ QSQHPTDALS
EDLLSIIANM SGCLPYMLPP KCPNTCLANK YRPITGACNN RDHPRWGASN TALARWLPPV
YEDGFSQPRG WNPGFLYNGF PLPPVREVTR HVIQVSNEVV TDDDRYSDLL MAWGQYIDHD
IAFTPQSTSK AAFGGGADCQ MTCENQNPCF PIQLPEEARP AAGTACLPFY RSSAACGTGD
QGALFGNLST ANPRQQMNGL TSFLDASTVY GSSPALERQL RNWTSAEGLL RVHARLRDSG
RAYLPFVPPR APAACAPEPG IPGETRGPCF LAGDGRASEV PSLTALHTLW LREHNRLAAA
LKALNAHWSA DAVYQEARKV VGALHQIITL RDYIPRILGP EAFQQYVGPY EGYDSTANPT
VSNVFSTAAF RFGHATIHPL VRRLDASFQE HPDLPGLWLH QAFFSPWTLL RGGGLDPLIR
GLLARPAKLQ VQDQLMNEEL TERLFVLSNS STLDLASINL QRGRDHGLPG YNEWREFCGL
PRLETPADLS TAIASRSVAD KILDLYKHPD NIDVWLGGLA ENFLPRARTG PLFACLIGKQ
MKALRDGDWF WWENSHVFTD AQRRELEKHS LSRVICDNTG LTRVPMDAFQ VGKFPEDFES
CDSITGMNLE AWRETFPQDD KCGFPESVEN GDFVHCEESG RRVLVYSCRH GYELQGREQL
TCTQEGWDFQ PPLCKDVNEC ADGAHPPCHA SARCRNTKGG FQCLCADPYE LGDDGRTCVD
SGRLPRVTWI SMSLAALLIG GFAGLTSTVI CRWTRTGTKS TLPISETGGG TPELRCGKHQ
AVGTSPQRAA AQDSEQESAG MEGRDTHRLP RAL


Related products :

Catalog number Product name Quantity
orb90286 Human Thyroid Peroxidase protein Thyroid Peroxidase Human Recombinant produced in SF9 is glycosylated, polypeptide chain containing 834 amino acids and having a molecular mass of 92,872 Dalton (exclud 5
LF-PA10016 anti-Thyroid Peroxidase(TPO), Rabbit polyclonal to Thyroid Peroxidase(TPO), Isotype , Host Rabbit 100 ug
SCH-8912-5009 MOUSE ANTI HUMAN THYROID PEROXIDASE, Product Type Monoclonal Antibody, Specificity THYROID PEROXIDASE, Target Species Human, Host Mouse, Format Purified, Isotypes IgG1, Applications E, WB, Clon 0.2 mg
8912-5009 MOUSE ANTI HUMAN THYROID PEROXIDASE, Product Type Monoclonal Antibody, Specificity THYROID PEROXIDASE, Target Species Human, Host Mouse, Format Purified, Isotypes IgG1, Applications E, WB, Clon 0.2 mg
20-272-190795 Thyroid Peroxidase - Mouse monoclonal [MoAb47] to Thyroid Peroxidase; EC 1.11.1.8; TPO Monoclonal 0.25 ml
8912-5109 RABBIT ANTI HUMAN THYROID PEROXIDASE, Product Type Polyclonal Antibody, Specificity THYROID PEROXIDASE, Target Species Human, Host Rabbit, Format Purified, Isotypes Polyclonal IgG, Applications 1000 TESTS/0.25ml
SCH-8912-5109 RABBIT ANTI HUMAN THYROID PEROXIDASE, Product Type Polyclonal Antibody, Specificity THYROID PEROXIDASE, Target Species Human, Host Rabbit, Format Purified, Isotypes Polyclonal IgG, Applications 1000 TESTS/0.25ml
20-272-190158 Thyroid Peroxidase - Mouse monoclonal [6H7] to Thyroid Peroxidase; EC 1.11.1.8; TPO Monoclonal 0.1 mg
Mob 418-05 Thyroid Peroxidase; 0.5ml
8-TPO Thyroid Peroxidase 100ug
8-TPO Thyroid Peroxidase 500ug
BM734 Thyroid peroxidase (TPO) 0.2 mg
Y103941 Thyroid Peroxidase (TPO) 1 mg
DM418 Thyroid peroxidase (TPO) 1 ml
DM418-05 Thyroid peroxidase (TPO) 0,5 ml
TPO TPO Gene thyroid peroxidase
25004 Thyroid peroxidase (TPO) 0.1 mg
8T58 Thyroid peroxidase (TPO) 1 mg
4TP15 Thyroid peroxidase (TPO) 1 mg
25003 Thyroid peroxidase (TPO) 0.1 mg
P275-3 Thyroid peroxidase (TPO) 0.1 mg
P187-3 Thyroid peroxidase (TPO) 0.1 mg
BM734 Thyroid peroxidase (TPO) 0.2 mg
DL-TPO-Ra Rat Thyroid Peroxidase (TPO) ELISA Kit 96T
GWB-8ECAE2 Thyroid Peroxidase


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur