PERT_HUMAN
ID PERT_HUMAN Reviewed; 933 AA.
AC P07202; P09934; P09935; Q8IUL0; Q8NF94; Q8NF95; Q8NF96; Q8NF97; Q8TCI9;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 4.
DT 03-AUG-2022, entry version 250.
DE RecName: Full=Thyroid peroxidase {ECO:0000305};
DE Short=TPO;
DE EC=1.11.1.8 {ECO:0000250|UniProtKB:P09933};
DE Flags: Precursor;
GN Name=TPO {ECO:0000312|HGNC:HGNC:12015};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS PRO-725 AND
RP ALA-847.
RX PubMed=3475693; DOI=10.1073/pnas.84.16.5555;
RA Kimura S., Kotani T., McBride O.W., Umeki K., Hirai K., Nakayama T.,
RA Ohtaki S.;
RT "Human thyroid peroxidase: complete cDNA and protein sequence, chromosome
RT mapping, and identification of two alternately spliced mRNAs.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:5555-5559(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS PRO-725 AND ALA-847.
RC TISSUE=Thyroid;
RX PubMed=3453124; DOI=10.1093/nar/15.16.6735;
RA Libert F., Ruel J., Ludgate M., Swillens S., Alexander N., Vassart G.,
RA Dinsart C.;
RT "Complete nucleotide sequence of the human thyroperoxidase-microsomal
RT antigen cDNA.";
RL Nucleic Acids Res. 15:6735-6735(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=2548579; DOI=10.1021/bi00436a054;
RA Kimura S., Hong Y.S., Kotani T., Ohtaki S., Kikkawa F.;
RT "Structure of the human thyroid peroxidase gene: comparison and
RT relationship to the human myeloperoxidase gene.";
RL Biochemistry 28:4481-4489(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Thyroid;
RX PubMed=2308857; DOI=10.1093/nar/18.3.670;
RA Barnett P.S., Banga J.P., Watkins J., Huang G.C., Gluckman D.R.B.,
RA Page M.J., McGregor A.M.;
RT "Nucleotide sequence of the alternatively spliced human thyroid peroxidase
RT cDNA, TPO-2.";
RL Nucleic Acids Res. 18:670-670(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-257.
RC TISSUE=Thyroid;
RA Rapoport B.;
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND VARIANTS SER-257; PRO-725 AND
RP ALA-847.
RC TISSUE=Thyroid;
RA Hennen G.P., Igout A., Melen L.B.;
RT "Homo sapiens thyroid peroxidase (TPO) variant mRNA, alternatively spliced
RT sequence.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 5; 6; 2-3 AND 2-4), AND
RP VARIANTS PRO-725 AND ALA-847.
RC TISSUE=Thyroid;
RX PubMed=12454013; DOI=10.1074/jbc.m209513200;
RA Ferrand M., Le Fourn V., Franc J.-L.;
RT "Increasing diversity of human thyroperoxidase generated by alternative
RT splicing. Characterization by molecular cloning of new transcripts with
RT single- and multispliced mRNAs.";
RL J. Biol. Chem. 278:3793-3800(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 217-496.
RX PubMed=3654979; DOI=10.1172/jci113181;
RA Seto P., Hirayu H., Magnusson R.P., Gestautas J., Portmann L.,
RA Degroot L.J., Rapoport B.;
RT "Isolation of a complementary DNA clone for thyroid microsomal antigen.
RT Homology with the gene for thyroid peroxidase.";
RL J. Clin. Invest. 80:1205-1208(1987).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 670-933 (ISOFORM 3), AND ALTERNATIVE SPLICING
RP IN GRAVES' DISEASE.
RC TISSUE=Thyroid;
RX PubMed=2383265; DOI=10.1016/0006-291x(90)92152-p;
RA Zanelli E., Henry M., Charvet B., Malthiery Y.;
RT "Evidence for an alternate splicing in the thyroperoxidase messenger from
RT patients with Graves' disease.";
RL Biochem. Biophys. Res. Commun. 170:735-741(1990).
RN [10]
RP INTERACTION WITH DUOX1; DUOX2 AND CYBA.
RX PubMed=15561711; DOI=10.1074/jbc.m407709200;
RA Wang D., De Deken X., Milenkovic M., Song Y., Pirson I., Dumont J.E.,
RA Miot F.;
RT "Identification of a novel partner of duox: EFP1, a thioredoxin-related
RT protein.";
RL J. Biol. Chem. 280:3096-3103(2005).
RN [11]
RP VARIANTS TDH2A ASP-453; SER-590 AND LYS-799, AND VARIANTS SER-257; SER-373;
RP THR-398 AND PRO-725.
RX PubMed=7550241; DOI=10.1002/humu.1380060104;
RA Bikker H., Vulsma T., Baas F., de Vijlder J.J.M.;
RT "Identification of five novel inactivating mutations in the human thyroid
RT peroxidase gene by denaturing gradient gel electrophoresis.";
RL Hum. Mutat. 6:9-16(1995).
RN [12]
RP VARIANT TDH2A PHE-447.
RX PubMed=9024270; DOI=10.1210/jcem.82.2.3729;
RA Bikker H., Baas F., De Vijlder J.J.M.;
RT "Molecular analysis of mutated thyroid peroxidase detected in patients with
RT total iodide organification defects.";
RL J. Clin. Endocrinol. Metab. 82:649-653(1997).
RN [13]
RP VARIANT TDH2A GLU-660.
RX PubMed=10468986; DOI=10.1046/j.1365-2265.1999.00746.x;
RA Santos C.L.S., Bikker H., Rego K.G.M., Nascimento A.C., Tambascia M.,
RA De Vijlder J.J.M., Medeiros-Neto G.;
RT "A novel mutation in the TPO gene in goitrous hypothyroid patients with
RT iodide organification defect.";
RL Clin. Endocrinol. (Oxf.) 51:165-172(1999).
RN [14]
RP VARIANTS TDH2A GLN-648 AND LYS-799.
RX PubMed=10084596; DOI=10.1210/jcem.84.3.5541;
RA Pannain S., Weiss R.E., Jackson C.E., Dian D., Beck J.C., Sheffield V.C.,
RA Cox N., Refetoff S.;
RT "Two different mutations in the thyroid peroxidase gene of a large inbred
RT Amish kindred: power and limits of homozygosity mapping.";
RL J. Clin. Endocrinol. Metab. 84:1061-1071(1999).
RN [15]
RP VARIANT TDH2A ASN-240, AND CHARACTERIZATION OF VARIANT TDH2A ASN-240.
RX PubMed=9924196; DOI=10.1677/joe.0.1600267;
RA Kotani T., Umeki K., Yamamoto I., Maesaka H., Tachibana K., Ohtaki S.;
RT "A novel mutation in the human thyroid peroxidase gene resulting in a total
RT iodide organification defect.";
RL J. Endocrinol. 160:267-273(1999).
RN [16]
RP VARIANTS TDH2A THR-326; PHE-447; ASP-453; CYS-527; TRP-693 AND LYS-799.
RX PubMed=11061528; DOI=10.1210/jcem.85.10.6878;
RA Bakker B., Bikker H., Vulsma T., de Randamie J.S.E., Wiedijk B.M.,
RA De Vijlder J.J.M.;
RT "Two decades of screening for congenital hypothyroidism in The Netherlands:
RT TPO gene mutations in total iodide organification defects (an update).";
RL J. Clin. Endocrinol. Metab. 85:3708-3712(2000).
RN [17]
RP VARIANTS TDH2A PRO-458 AND HIS-491.
RX PubMed=11415848; DOI=10.1530/eje.0.1450019;
RA Ambrugger P., Stoeva I., Biebermann H., Torresani T., Leitner C.,
RA Grueters A.;
RT "Novel mutations of the thyroid peroxidase gene in patients with permanent
RT congenital hypothyroidism.";
RL Eur. J. Endocrinol. 145:19-24(2001).
RN [18]
RP VARIANTS TDH2A TRP-665 AND ARG-771, AND CHARACTERIZATION OF VARIANTS TDH2A
RP TRP-665 AND ARG-771.
RX PubMed=11916616; DOI=10.1530/eje.0.1460491;
RA Umeki K., Kotani T., Kawano J., Suganuma T., Yamamoto I., Aratake Y.,
RA Furujo M., Ichiba Y.;
RT "Two novel missense mutations in the thyroid peroxidase gene, R665W and
RT G771R, result in a localization defect and cause congenital
RT hypothyroidism.";
RL Eur. J. Endocrinol. 146:491-498(2002).
RN [19]
RP VARIANT TDH2A PRO-53.
RX PubMed=12213873; DOI=10.1210/jc.2002-020153;
RA Niu D.-M., Hwang B., Chu Y.-K., Liao C.-J., Wang P.-L., Lin C.-Y.;
RT "High prevalence of a novel mutation (2268 insT) of the thyroid peroxidase
RT gene in Taiwanese patients with total iodide organification defect, and
RT evidence for a founder effect.";
RL J. Clin. Endocrinol. Metab. 87:4208-4212(2002).
RN [20]
RP VARIANTS TDH2A SER-493 AND TYR-796.
RX PubMed=11874711; DOI=10.1677/joe.0.1720627;
RA Wu J.-Y., Shu S.-G., Yang C.-F., Lee C.-C., Tsai F.-J.;
RT "Mutation analysis of thyroid peroxidase gene in Chinese patients with
RT total iodide organification defect: identification of five novel
RT mutations.";
RL J. Endocrinol. 172:627-635(2002).
RN [21]
RP VARIANT TDH2A ILE-839.
RX PubMed=12490071; DOI=10.1089/105072502320908277;
RA Calaciura F., Miscio G., Coco A., Leonardi D., Cisternino C., Regalbuto C.,
RA Bozzali M., Maiorana R., Ranieri A., Carta A., Buscema M., Trischitta V.,
RA Sava L., Tassi V.;
RT "Genetics of specific phenotypes of congenital hypothyroidism: a
RT population-based approach.";
RL Thyroid 12:945-951(2002).
RN [22]
RP VARIANTS TDH2A CYS-533 AND ASP-574-575-LEU DEL, AND CHARACTERIZATION OF
RP VARIANTS TDH2A CYS-533 AND ASP-574-575-LEU DEL.
RX PubMed=12864797; DOI=10.1046/j.1365-2265.2003.01823.x;
RA Kotani T., Umeki K., Kawano J., Suganuma T., Hishinuma A., Ieiri T.,
RA Harada S.;
RT "Partial iodide organification defect caused by a novel mutation of the
RT thyroid peroxidase gene in three siblings.";
RL Clin. Endocrinol. (Oxf.) 59:198-206(2003).
RN [23]
RP VARIANTS TDH2A THR-307; MET-433; LEU-499 AND ARG-808.
RX PubMed=12938097; DOI=10.1002/humu.9175;
RA Rivolta C.M., Esperante S.A., Gruneiro-Papendieck L., Chiesa A., Moya C.M.,
RA Domene S., Varela V., Targovnik H.M.;
RT "Five novel inactivating mutations in the thyroid peroxidase gene
RT responsible for congenital goiter and iodide organification defect.";
RL Hum. Mutat. 22:259-259(2003).
RN [24]
RP VARIANT TDH2A TRP-693.
RX PubMed=12843174; DOI=10.1210/jc.2002-021377;
RA Fugazzola L., Cerutti N., Mannavola D., Vannucchi G., Fallini C.,
RA Persani L., Beck-Peccoz P.;
RT "Monoallelic expression of mutant thyroid peroxidase allele causing total
RT iodide organification defect.";
RL J. Clin. Endocrinol. Metab. 88:3264-3271(2003).
RN [25]
RP VARIANT TDH2A LYS-378.
RX PubMed=16284446; DOI=10.1507/endocrj.52.643;
RA Tajima T., Tsubaki J., Fujieda K.;
RT "Two novel mutations in the thyroid peroxidase gene with goitrous
RT hypothyroidism.";
RL Endocr. J. 52:643-645(2005).
RN [26]
RP VARIANT TDH2A ASP-453.
RX PubMed=16684826; DOI=10.1210/jc.2006-0142;
RA Pfarr N., Borck G., Turk A., Napiontek U., Keilmann A., Mueller-Forell W.,
RA Kopp P., Pohlenz J.;
RT "Goitrous congenital hypothyroidism and hearing impairment associated with
RT mutations in the TPO and SLC26A4/PDS genes.";
RL J. Clin. Endocrinol. Metab. 91:2678-2681(2006).
RN [27]
RP VARIANTS TDH2A HIS-412 AND 596-GLU--LEU-933 DEL.
RX PubMed=27305979; DOI=10.1038/jhg.2016.62;
RA Mittal K., Rafiq M.A., Rafiullah R., Harripaul R., Ali H., Ayaz M.,
RA Aslam M., Naeem F., Amin-Ud-Din M., Waqas A., So J., Rappold G.A.,
RA Vincent J.B., Ayub M.;
RT "Mutations in the genes for thyroglobulin and thyroid peroxidase cause
RT thyroid dyshormonogenesis and autosomal-recessive intellectual
RT disability.";
RL J. Hum. Genet. 61:867-872(2016).
CC -!- FUNCTION: Iodination and coupling of the hormonogenic tyrosines in
CC thyroglobulin to yield the thyroid hormones T(3) and T(4).
CC {ECO:0000250|UniProtKB:P09933}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + H2O2 + 2 iodide = diiodine + 2 H2O;
CC Xref=Rhea:RHEA:23336, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:16382, ChEBI:CHEBI:17606; EC=1.11.1.8;
CC Evidence={ECO:0000250|UniProtKB:P09933};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thyroglobulin]-L-tyrosine + H(+) + H2O2 + iodide =
CC [thyroglobulin]-3-iodo-L-tyrosine + 2 H2O; Xref=Rhea:RHEA:48956,
CC Rhea:RHEA-COMP:12274, Rhea:RHEA-COMP:12275, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:16382,
CC ChEBI:CHEBI:46858, ChEBI:CHEBI:90870; EC=1.11.1.8;
CC Evidence={ECO:0000250|UniProtKB:P09933};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thyroglobulin]-3-iodo-L-tyrosine + H(+) + H2O2 + iodide =
CC [thyroglobulin]-3,5-diiodo-L-tyrosine + 2 H2O; Xref=Rhea:RHEA:48960,
CC Rhea:RHEA-COMP:12275, Rhea:RHEA-COMP:12276, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:16382,
CC ChEBI:CHEBI:90870, ChEBI:CHEBI:90871; EC=1.11.1.8;
CC Evidence={ECO:0000250|UniProtKB:P09933};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 [thyroglobulin]-3,5-diiodo-L-tyrosine + H2O2 =
CC [thyroglobulin]-dehydroalanine + [thyroglobulin]-L-thyroxine + 2 H2O;
CC Xref=Rhea:RHEA:48964, Rhea:RHEA-COMP:12276, Rhea:RHEA-COMP:12277,
CC Rhea:RHEA-COMP:12278, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:90871, ChEBI:CHEBI:90872, ChEBI:CHEBI:90873; EC=1.11.1.8;
CC Evidence={ECO:0000250|UniProtKB:P09933};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thyroglobulin]-3,5-diiodo-L-tyrosine + [thyroglobulin]-3-
CC iodo-L-tyrosine + H2O2 = [thyroglobulin]-3,3',5-triiodo-L-thyronine +
CC [thyroglobulin]-dehydroalanine + 2 H2O; Xref=Rhea:RHEA:48968,
CC Rhea:RHEA-COMP:12275, Rhea:RHEA-COMP:12276, Rhea:RHEA-COMP:12278,
CC Rhea:RHEA-COMP:12279, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:90870, ChEBI:CHEBI:90871, ChEBI:CHEBI:90873,
CC ChEBI:CHEBI:90874; EC=1.11.1.8;
CC Evidence={ECO:0000250|UniProtKB:P09933};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00298};
CC Note=Binds 1 Ca(2+) ion per heterodimer. {ECO:0000255|PROSITE-
CC ProRule:PRU00298};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00298};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per
CC heterodimer. {ECO:0000255|PROSITE-ProRule:PRU00298};
CC -!- PATHWAY: Hormone biosynthesis; thyroid hormone biosynthesis.
CC -!- SUBUNIT: Interacts with DUOX1, DUOX2 and CYBA.
CC {ECO:0000269|PubMed:15561711}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cell surface.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=TPO1;
CC IsoId=P07202-1; Sequence=Displayed;
CC Name=2; Synonyms=TPO2;
CC IsoId=P07202-2; Sequence=VSP_004665;
CC Name=3; Synonyms=TPO3, Graves' disease, TPOzaninelli;
CC IsoId=P07202-3; Sequence=VSP_004666;
CC Name=4; Synonyms=TPO4;
CC IsoId=P07202-4; Sequence=VSP_007269;
CC Name=5; Synonyms=TPO5;
CC IsoId=P07202-5; Sequence=VSP_007268;
CC Name=6; Synonyms=TPO6;
CC IsoId=P07202-6; Sequence=VSP_004665, VSP_007270;
CC Name=2-3;
CC IsoId=P07202-7; Sequence=VSP_004665, VSP_004666;
CC Name=2-4;
CC IsoId=P07202-8; Sequence=VSP_004665, VSP_007269;
CC -!- PTM: Glycosylated.
CC -!- PTM: Heme is covalently bound through a H(2)O(2)-dependent
CC autocatalytic process. Heme insertion is important for the delivery of
CC protein at the cell surface.
CC -!- PTM: Cleaved in its N-terminal part.
CC -!- DISEASE: Note=An alternative splicing in the thyroperoxidase mRNA can
CC cause Graves' disease.
CC -!- DISEASE: Thyroid dyshormonogenesis 2A (TDH2A) [MIM:274500]: A disorder
CC due to defective conversion of accumulated iodide to organically bound
CC iodine. The iodide organification defect can be partial or complete.
CC {ECO:0000269|PubMed:10084596, ECO:0000269|PubMed:10468986,
CC ECO:0000269|PubMed:11061528, ECO:0000269|PubMed:11415848,
CC ECO:0000269|PubMed:11874711, ECO:0000269|PubMed:11916616,
CC ECO:0000269|PubMed:12213873, ECO:0000269|PubMed:12490071,
CC ECO:0000269|PubMed:12843174, ECO:0000269|PubMed:12864797,
CC ECO:0000269|PubMed:12938097, ECO:0000269|PubMed:16284446,
CC ECO:0000269|PubMed:16684826, ECO:0000269|PubMed:27305979,
CC ECO:0000269|PubMed:7550241, ECO:0000269|PubMed:9024270,
CC ECO:0000269|PubMed:9924196}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 2]: Lacks exon 10. Found in normal thyroid
CC tissues as well as Graves'tissues. Rapidly degraded after synthesis,
CC does not reach the cell surface. Inactive. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Lacks exon 16. Found in normal thyroid
CC tissues as well as Graves'tissues. Active. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Lacks exon 14. Active. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: Lacks exon 8. Does not fold correctly. Does
CC not reach the cell surface. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 6]: Lacks exons 10, 12, 13, 14 and 16.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 2-3]: Lacks exons 10 and 16. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 2-4]: Lacks exons 10 and 14. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peroxidase family. XPO subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00298}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Thyroid peroxidase entry;
CC URL="https://en.wikipedia.org/wiki/Thyroid_peroxidase";
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DR EMBL; J02969; AAA61215.1; -; mRNA.
DR EMBL; J02970; AAA61216.1; -; mRNA.
DR EMBL; Y00406; CAA68467.1; -; mRNA.
DR EMBL; M25715; AAA97517.1; -; Genomic_DNA.
DR EMBL; M25702; AAA97517.1; JOINED; Genomic_DNA.
DR EMBL; M25703; AAA97517.1; JOINED; Genomic_DNA.
DR EMBL; M25704; AAA97517.1; JOINED; Genomic_DNA.
DR EMBL; M25705; AAA97517.1; JOINED; Genomic_DNA.
DR EMBL; M25706; AAA97517.1; JOINED; Genomic_DNA.
DR EMBL; M25707; AAA97517.1; JOINED; Genomic_DNA.
DR EMBL; M25708; AAA97517.1; JOINED; Genomic_DNA.
DR EMBL; M25709; AAA97517.1; JOINED; Genomic_DNA.
DR EMBL; M25710; AAA97517.1; JOINED; Genomic_DNA.
DR EMBL; M25711; AAA97517.1; JOINED; Genomic_DNA.
DR EMBL; M25712; AAA97517.1; JOINED; Genomic_DNA.
DR EMBL; M25713; AAA97517.1; JOINED; Genomic_DNA.
DR EMBL; M25714; AAA97517.1; JOINED; Genomic_DNA.
DR EMBL; X17358; CAA35235.1; -; mRNA.
DR EMBL; M17755; AAA61217.2; -; mRNA.
DR EMBL; AF439430; AAL74416.1; -; mRNA.
DR EMBL; AF533528; AAN04471.1; -; mRNA.
DR EMBL; AY136822; AAN11302.1; -; mRNA.
DR EMBL; AF533529; AAN04472.1; -; mRNA.
DR EMBL; AF533530; AAN04473.1; -; mRNA.
DR EMBL; AF533531; AAN04474.1; -; mRNA.
DR EMBL; M55702; AAA61219.1; -; mRNA.
DR EMBL; M55702; AAA61218.1; -; mRNA.
DR CCDS; CCDS1643.1; -. [P07202-1]
DR CCDS; CCDS1644.1; -. [P07202-2]
DR CCDS; CCDS1646.1; -. [P07202-5]
DR PIR; A32413; OPHUIT.
DR RefSeq; NP_000538.3; NM_000547.5. [P07202-1]
DR RefSeq; NP_001193673.1; NM_001206744.1. [P07202-1]
DR RefSeq; NP_001193674.1; NM_001206745.1. [P07202-2]
DR RefSeq; NP_783650.1; NM_175719.3. [P07202-2]
DR RefSeq; NP_783652.1; NM_175721.3. [P07202-4]
DR RefSeq; NP_783653.1; NM_175722.3. [P07202-5]
DR RefSeq; XP_011508683.1; XM_011510381.2.
DR AlphaFoldDB; P07202; -.
DR SMR; P07202; -.
DR BioGRID; 113026; 6.
DR STRING; 9606.ENSP00000318820; -.
DR BindingDB; P07202; -.
DR ChEMBL; CHEMBL1839; -.
DR DrugBank; DB11496; 2-mercaptobenzothiazole.
DR DrugBank; DB00389; Carbimazole.
DR DrugBank; DB00509; Dextrothyroxine.
DR DrugBank; DB05382; Iodine.
DR DrugBank; DB00763; Methimazole.
DR DrugBank; DB00550; Propylthiouracil.
DR DrugBank; DB11085; Resorcinol.
DR DrugBank; DB08604; Triclosan.
DR DrugCentral; P07202; -.
DR Allergome; 9554; Hom s TPO.
DR PeroxiBase; 3318; HsTPO01.
DR GlyGen; P07202; 4 sites.
DR iPTMnet; P07202; -.
DR PhosphoSitePlus; P07202; -.
DR BioMuta; TPO; -.
DR DMDM; 160281455; -.
DR MassIVE; P07202; -.
DR PaxDb; P07202; -.
DR PeptideAtlas; P07202; -.
DR PRIDE; P07202; -.
DR ProteomicsDB; 51964; -. [P07202-1]
DR ProteomicsDB; 51965; -. [P07202-2]
DR ProteomicsDB; 51966; -. [P07202-3]
DR ProteomicsDB; 51967; -. [P07202-4]
DR ProteomicsDB; 51968; -. [P07202-5]
DR ProteomicsDB; 51969; -. [P07202-6]
DR ProteomicsDB; 51970; -. [P07202-7]
DR ProteomicsDB; 51971; -. [P07202-8]
DR ABCD; P07202; 56 sequenced antibodies.
DR Antibodypedia; 2364; 596 antibodies from 35 providers.
DR DNASU; 7173; -.
DR Ensembl; ENST00000329066.9; ENSP00000329869.4; ENSG00000115705.22. [P07202-1]
DR Ensembl; ENST00000345913.8; ENSP00000318820.7; ENSG00000115705.22. [P07202-1]
DR Ensembl; ENST00000346956.7; ENSP00000263886.6; ENSG00000115705.22. [P07202-4]
DR Ensembl; ENST00000382198.5; ENSP00000371633.1; ENSG00000115705.22. [P07202-5]
DR Ensembl; ENST00000382201.7; ENSP00000371636.3; ENSG00000115705.22. [P07202-2]
DR GeneID; 7173; -.
DR KEGG; hsa:7173; -.
DR MANE-Select; ENST00000329066.9; ENSP00000329869.4; NM_001206744.2; NP_001193673.1.
DR UCSC; uc002qwr.4; human. [P07202-1]
DR CTD; 7173; -.
DR DisGeNET; 7173; -.
DR GeneCards; TPO; -.
DR HGNC; HGNC:12015; TPO.
DR HPA; ENSG00000115705; Tissue enriched (thyroid).
DR MalaCards; TPO; -.
DR MIM; 274500; phenotype.
DR MIM; 606765; gene.
DR neXtProt; NX_P07202; -.
DR OpenTargets; ENSG00000115705; -.
DR Orphanet; 95716; Familial thyroid dyshormonogenesis.
DR PharmGKB; PA36694; -.
DR VEuPathDB; HostDB:ENSG00000115705; -.
DR eggNOG; KOG2408; Eukaryota.
DR GeneTree; ENSGT00940000158104; -.
DR InParanoid; P07202; -.
DR OMA; GPYEGYN; -.
DR OrthoDB; 276568at2759; -.
DR PhylomeDB; P07202; -.
DR TreeFam; TF314316; -.
DR BRENDA; 1.11.1.8; 2681.
DR BRENDA; 3.6.1.52; 2681.
DR PathwayCommons; P07202; -.
DR Reactome; R-HSA-209968; Thyroxine biosynthesis.
DR SignaLink; P07202; -.
DR SIGNOR; P07202; -.
DR UniPathway; UPA00194; -.
DR BioGRID-ORCS; 7173; 6 hits in 1064 CRISPR screens.
DR ChiTaRS; TPO; human.
DR GenomeRNAi; 7173; -.
DR Pharos; P07202; Tclin.
DR PRO; PR:P07202; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P07202; protein.
DR Bgee; ENSG00000115705; Expressed in left lobe of thyroid gland and 92 other tissues.
DR ExpressionAtlas; P07202; baseline and differential.
DR Genevisible; P07202; HS.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0004447; F:iodide peroxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
DR GO; GO:0035162; P:embryonic hemopoiesis; IDA:DFLAT.
DR GO; GO:0042446; P:hormone biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR GO; GO:0006590; P:thyroid hormone generation; TAS:Reactome.
DR CDD; cd00033; CCP; 1.
DR Gene3D; 1.10.640.10; -; 1.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR InterPro; IPR029589; TPO.
DR PANTHER; PTHR11475:SF60; PTHR11475:SF60; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF00084; Sushi; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SMART; SM00032; CCP; 1.
DR SMART; SM00181; EGF; 1.
DR SMART; SM00179; EGF_CA; 1.
DR SUPFAM; SSF48113; SSF48113; 1.
DR SUPFAM; SSF57535; SSF57535; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
DR PROSITE; PS50923; SUSHI; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Congenital hypothyroidism; Disease variant;
KW Disulfide bond; EGF-like domain; Glycoprotein; Heme; Hydrogen peroxide;
KW Iron; Membrane; Metal-binding; Oxidoreductase; Peroxidase;
KW Reference proteome; Signal; Sushi; Thyroid hormones biosynthesis;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..933
FT /note="Thyroid peroxidase"
FT /id="PRO_0000023662"
FT TOPO_DOM 19..846
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 847..871
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 872..933
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 740..795
FT /note="Sushi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 796..839
FT /note="EGF-like; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 881..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..933
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 239
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 238
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 321
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 323
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 325
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 327
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 399
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 494
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT SITE 396
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 569
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 142..158
FT /evidence="ECO:0000250"
FT DISULFID 259..269
FT /evidence="ECO:0000250"
FT DISULFID 263..286
FT /evidence="ECO:0000250"
FT DISULFID 598..655
FT /evidence="ECO:0000250"
FT DISULFID 696..721
FT /evidence="ECO:0000250"
FT DISULFID 800..814
FT /evidence="ECO:0000250"
FT DISULFID 808..823
FT /evidence="ECO:0000250"
FT DISULFID 825..838
FT /evidence="ECO:0000250"
FT VAR_SEQ 274..446
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_007268"
FT VAR_SEQ 534..590
FT /note="Missing (in isoform 2, isoform 2-3, isoform 2-4 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:2308857,
FT ECO:0000303|PubMed:3475693"
FT /id="VSP_004665"
FT VAR_SEQ 669..933
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_007270"
FT VAR_SEQ 796..839
FT /note="Missing (in isoform 4 and isoform 2-4)"
FT /evidence="ECO:0000305"
FT /id="VSP_007269"
FT VAR_SEQ 874..933
FT /note="TRTGTKSTLPISETGGGTPELRCGKHQAVGTSPQRAAAQDSEQESAGMEGRD
FT THRLPRAL -> RVLGWKAGILTGCREPSEGKVAGHCRTASCSQNHRTTLFQTQANRKS
FT AGRLFSQHG (in isoform 3 and isoform 2-3)"
FT /evidence="ECO:0000303|PubMed:2383265"
FT /id="VSP_004666"
FT VARIANT 53
FT /note="A -> P (in TDH2A)"
FT /evidence="ECO:0000269|PubMed:12213873"
FT /id="VAR_021622"
FT VARIANT 240
FT /note="D -> N (in TDH2A; loss of activity;
FT dbSNP:rs1427024341)"
FT /evidence="ECO:0000269|PubMed:9924196"
FT /id="VAR_021623"
FT VARIANT 257
FT /note="A -> S (in dbSNP:rs4927611)"
FT /evidence="ECO:0000269|PubMed:7550241, ECO:0000269|Ref.5,
FT ECO:0000269|Ref.6"
FT /id="VAR_006057"
FT VARIANT 307
FT /note="N -> T (in TDH2A)"
FT /evidence="ECO:0000269|PubMed:12938097"
FT /id="VAR_021624"
FT VARIANT 326
FT /note="A -> T (in TDH2A; dbSNP:rs371367459)"
FT /evidence="ECO:0000269|PubMed:11061528"
FT /id="VAR_021625"
FT VARIANT 373
FT /note="A -> S (in dbSNP:rs2280132)"
FT /evidence="ECO:0000269|PubMed:7550241"
FT /id="VAR_006058"
FT VARIANT 378
FT /note="E -> K (in TDH2A; dbSNP:rs1297312788)"
FT /evidence="ECO:0000269|PubMed:16284446"
FT /id="VAR_025784"
FT VARIANT 398
FT /note="S -> T (in dbSNP:rs2175977)"
FT /evidence="ECO:0000269|PubMed:7550241"
FT /id="VAR_006059"
FT VARIANT 412
FT /note="R -> H (in TDH2A; unknown pathological significance;
FT dbSNP:rs1173922703)"
FT /evidence="ECO:0000269|PubMed:27305979"
FT /id="VAR_078336"
FT VARIANT 433
FT /note="V -> M (in TDH2A; dbSNP:rs1035791118)"
FT /evidence="ECO:0000269|PubMed:12938097"
FT /id="VAR_021626"
FT VARIANT 447
FT /note="I -> F (in TDH2A; dbSNP:rs104893669)"
FT /evidence="ECO:0000269|PubMed:11061528,
FT ECO:0000269|PubMed:9024270"
FT /id="VAR_015375"
FT VARIANT 453
FT /note="Y -> D (in TDH2A; dbSNP:rs121908083)"
FT /evidence="ECO:0000269|PubMed:11061528,
FT ECO:0000269|PubMed:16684826, ECO:0000269|PubMed:7550241"
FT /id="VAR_006060"
FT VARIANT 458
FT /note="L -> P (in TDH2A; dbSNP:rs1231870370)"
FT /evidence="ECO:0000269|PubMed:11415848"
FT /id="VAR_021627"
FT VARIANT 491
FT /note="R -> H (in TDH2A; dbSNP:rs201165648)"
FT /evidence="ECO:0000269|PubMed:11415848"
FT /id="VAR_021628"
FT VARIANT 493
FT /note="G -> S (in TDH2A; dbSNP:rs778515113)"
FT /evidence="ECO:0000269|PubMed:11874711"
FT /id="VAR_021629"
FT VARIANT 499
FT /note="P -> L (in TDH2A; dbSNP:rs1169072188)"
FT /evidence="ECO:0000269|PubMed:12938097"
FT /id="VAR_021630"
FT VARIANT 527
FT /note="W -> C (in TDH2A; dbSNP:rs779434941)"
FT /evidence="ECO:0000269|PubMed:11061528"
FT /id="VAR_021631"
FT VARIANT 533
FT /note="G -> C (in TDH2A; partial defect; expression
FT slightly lower in efficiency and more degenerative than
FT wild-type enzyme)"
FT /evidence="ECO:0000269|PubMed:12864797"
FT /id="VAR_027229"
FT VARIANT 574..575
FT /note="Missing (in TDH2A; partial defect; expressed on the
FT plasma membrane surface at less than half the rate of wild-
FT type enzyme)"
FT /id="VAR_027230"
FT VARIANT 590
FT /note="G -> S (in TDH2A; dbSNP:rs121908084)"
FT /evidence="ECO:0000269|PubMed:7550241"
FT /id="VAR_027231"
FT VARIANT 596..933
FT /note="Missing (in TDH2A; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:27305979"
FT /id="VAR_078337"
FT VARIANT 618
FT /note="V -> M (in dbSNP:rs10189135)"
FT /id="VAR_027232"
FT VARIANT 648
FT /note="R -> Q (in TDH2A; dbSNP:rs121908086)"
FT /evidence="ECO:0000269|PubMed:10084596"
FT /id="VAR_013138"
FT VARIANT 660
FT /note="Q -> E (in TDH2A; dbSNP:rs121908088)"
FT /evidence="ECO:0000269|PubMed:10468986"
FT /id="VAR_021632"
FT VARIANT 665
FT /note="R -> W (in TDH2A; fails to localize to the plasma
FT membrane; dbSNP:rs776742629)"
FT /evidence="ECO:0000269|PubMed:11916616"
FT /id="VAR_021633"
FT VARIANT 693
FT /note="R -> W (in TDH2A; dbSNP:rs121908087)"
FT /evidence="ECO:0000269|PubMed:11061528,
FT ECO:0000269|PubMed:12843174"
FT /id="VAR_021634"
FT VARIANT 706
FT /note="M -> V (in dbSNP:rs13431173)"
FT /id="VAR_027233"
FT VARIANT 725
FT /note="T -> P (in dbSNP:rs732609)"
FT /evidence="ECO:0000269|PubMed:12454013,
FT ECO:0000269|PubMed:3453124, ECO:0000269|PubMed:3475693,
FT ECO:0000269|PubMed:7550241, ECO:0000269|Ref.6"
FT /id="VAR_006061"
FT VARIANT 771
FT /note="G -> R (in TDH2A; fails to localize to the plasma
FT membrane; dbSNP:rs138931129)"
FT /evidence="ECO:0000269|PubMed:11916616"
FT /id="VAR_021635"
FT VARIANT 793
FT /note="L -> P (in dbSNP:rs28991293)"
FT /id="VAR_027234"
FT VARIANT 796
FT /note="D -> Y (in TDH2A)"
FT /evidence="ECO:0000269|PubMed:11874711"
FT /id="VAR_021636"
FT VARIANT 799
FT /note="E -> K (in TDH2A; dbSNP:rs121908085)"
FT /evidence="ECO:0000269|PubMed:10084596,
FT ECO:0000269|PubMed:11061528, ECO:0000269|PubMed:7550241"
FT /id="VAR_006062"
FT VARIANT 808
FT /note="C -> R (in TDH2A; dbSNP:rs935058009)"
FT /evidence="ECO:0000269|PubMed:12938097"
FT /id="VAR_021637"
FT VARIANT 839
FT /note="V -> I (in TDH2A; dbSNP:rs146351101)"
FT /evidence="ECO:0000269|PubMed:12490071"
FT /id="VAR_027235"
FT VARIANT 846
FT /note="R -> W (in dbSNP:rs28913014)"
FT /id="VAR_027236"
FT VARIANT 847
FT /note="V -> A (in dbSNP:rs1126799)"
FT /evidence="ECO:0000269|PubMed:12454013,
FT ECO:0000269|PubMed:3453124, ECO:0000269|PubMed:3475693,
FT ECO:0000269|Ref.6"
FT /id="VAR_027237"
FT CONFLICT 70
FT /note="P -> G (in Ref. 5; AAA61217)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="A -> G (in Ref. 5 and 8)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="A -> R (in Ref. 1; AAA61215/AAA61216)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="I -> N (in Ref. 5 and 8)"
FT /evidence="ECO:0000305"
FT CONFLICT 574
FT /note="D -> N (in Ref. 2; CAA68467)"
FT /evidence="ECO:0000305"
FT CONFLICT 732
FT /note="W -> C (in Ref. 7; AAN11302)"
FT /evidence="ECO:0000305"
FT CONFLICT 748
FT /note="V -> M (in Ref. 2 and 7)"
FT /evidence="ECO:0000305"
FT CONFLICT 816
FT /note="N -> S (in Ref. 6; AAL74416)"
FT /evidence="ECO:0000305"
FT CONFLICT 872
FT /note="R -> K (in Ref. 2 and 7)"
FT /evidence="ECO:0000305"
SQ 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
