THYG_HUMAN
ID THYG_HUMAN Reviewed; 2768 AA.
AC P01266; O15274; O43899; Q15593; Q15948; Q9NYR1; Q9NYR2; Q9UMZ0; Q9UNY3;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 5.
DT 03-AUG-2022, entry version 225.
DE RecName: Full=Thyroglobulin {ECO:0000305};
DE Short=Tg;
DE Flags: Precursor;
GN Name=TG {ECO:0000312|HGNC:HGNC:11764};
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] (ISOFORM 1), AND VARIANTS ASP-604; ASP-653;
RP GLN-985 DEL; TYR-1043; THR-1059; GLY-1312; ARG-1437; HIS-1463; THR-1936;
RP GLU-2091; LEU-2149; ARG-2170 AND HIS-2242.
RX PubMed=3595599; DOI=10.1111/j.1432-1033.1987.tb11466.x;
RA Malthiery Y., Lissitzky S.;
RT "Primary structure of human thyroglobulin deduced from the sequence of its
RT 8448-base complementary DNA.";
RL Eur. J. Biochem. 165:491-498(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLY-1312.
RC TISSUE=Thyroid;
RX PubMed=9186272; DOI=10.1530/eje.0.1360508;
RA van de Graaf S.A.R., Pauws E., de Vijlder J.J.M., Ris-Stalpers C.;
RT "The revised 8307 base pair coding sequence of human thyroglobulin
RT transiently expressed in eukaryotic cells.";
RL Eur. J. Endocrinol. 136:508-515(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLU-515.
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-730, AND VARIANTS ASP-604 AND ASP-653.
RX PubMed=3971976; DOI=10.1111/j.1432-1033.1985.tb08717.x;
RA Malthiery Y., Lissitzky S.;
RT "Sequence of the 5'-end quarter of the human-thyroglobulin messenger
RT ribonucleic acid and of its deduced amino-acid sequence.";
RL Eur. J. Biochem. 147:53-58(1985).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-415; 640-737 AND 880-1000, AND
RP VARIANT ALA-734.
RX PubMed=3681978; DOI=10.1016/0022-2836(87)90403-7;
RA Parma J., Christophe D., Pohl V., Vassart G.;
RT "Structural organization of the 5' region of the thyroglobulin gene.
RT Evidence for intron loss and 'exonization' during evolution.";
RL J. Mol. Biol. 196:769-779(1987).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25.
RX PubMed=2991855; DOI=10.1093/nar/13.14.5127;
RA Christophe D., Cabrer B., Bacolla A., Targovnik H.M., Pohl V., Vassart G.;
RT "An unusually long poly(purine)-poly(pyrimidine) sequence is located
RT upstream from the human thyroglobulin gene.";
RL Nucleic Acids Res. 13:5127-5144(1985).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1002-1566 (ISOFORM 1), AND VARIANT
RP GLY-1312.
RX PubMed=11124863; DOI=10.1530/eje.0.1430789;
RA Moya C.M., Mendive F.M., Rivolta C.M., Vassart G., Targovnik H.M.;
RT "Genomic organization of the 5' region of the human thyroglobulin gene.";
RL Eur. J. Endocrinol. 143:789-798(2000).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1645-2768, AND VARIANTS LEU-2149 AND
RP ARG-2170.
RX PubMed=10524569; DOI=10.1089/thy.1999.9.903;
RA Mendive F.M., Rivolta C.M., Vassart G., Targovnik H.M.;
RT "Genomic organization of the 3' region of the human thyroglobulin gene.";
RL Thyroid 9:903-912(1999).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1504-1602 (ISOFORM 2).
RX PubMed=1639210; DOI=10.1016/0303-7207(92)90087-m;
RA Targovnik H.M., Cochaux P., Corach D., Vassart G.;
RT "Identification of a minor Tg mRNA transcript in RNA from normal and
RT goitrous thyroids.";
RL Mol. Cell. Endocrinol. 84:R23-R26(1992).
RN [10]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=2914619; DOI=10.1016/0014-5793(89)80513-7;
RA Marriq C., Lejeune P.J., Venot N., Vinet L.;
RT "Hormone synthesis in human thyroglobulin: possible cleavage of the
RT polypeptide chain at the tyrosine donor site.";
RL FEBS Lett. 242:414-418(1989).
RN [11]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=8269951; DOI=10.1111/j.1432-1033.1993.tb18414.x;
RA Gentile F., Salvatore G.;
RT "Preferential sites of proteolytic cleavage of bovine, human and rat
RT thyroglobulin. The use of limited proteolysis to detect solvent-exposed
RT regions of the primary structure.";
RL Eur. J. Biochem. 218:603-621(1993).
RN [12]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=7793989; DOI=10.1006/abbi.1995.1346;
RA Xiao S., Pollock H.G., Taurog A., Rawitch A.B.;
RT "Characterization of hormonogenic sites in an N-terminal, cyanogen bromide
RT fragment of human thyroglobulin.";
RL Arch. Biochem. Biophys. 320:96-105(1995).
RN [13]
RP PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-76; ASN-198; ASN-484;
RP ASN-529; ASN-748; ASN-816; ASN-947; ASN-1220; ASN-1348; ASN-1349; ASN-1365;
RP ASN-1716; ASN-1774; ASN-2013; ASN-2250; ASN-2295 AND ASN-2582, AND LACK OF
RP GLYCOSYLATION AT ASN-110; ASN-496; ASN-1869 AND ASN-2122.
RX PubMed=8615697; DOI=10.1006/abbi.1996.0093;
RA Yang S.X., Pollock H.G., Rawitch A.B.;
RT "Glycosylation in human thyroglobulin: location of the N-linked
RT oligosaccharide units and comparison with bovine thyroglobulin.";
RL Arch. Biochem. Biophys. 327:61-70(1996).
RN [14]
RP IODINATION AT TYR-24; TYR-149; TYR-258; TYR-704; TYR-785; TYR-866; TYR-883;
RP TYR-992; TYR-1310; TYR-1467; TYR-2184; TYR-2573; TYR-2587; TYR-2617;
RP TYR-2697 AND TYR-2766.
RX PubMed=2760035; DOI=10.1016/s0021-9258(18)80031-x;
RA Lamas L., Anderson P.C., Fox J.W., Dunn J.T.;
RT "Consensus sequences for early iodination and hormonogenesis in human
RT thyroglobulin.";
RL J. Biol. Chem. 264:13541-13545(1989).
RN [15]
RP PRESENCE OF 11TH THYROGLOBULIN TYPE-1 REPEAT.
RX PubMed=8797845; DOI=10.1111/j.1432-1033.1996.0125h.x;
RA Molina F., Bouanani M., Pau B., Granier C.;
RT "Characterization of the type-1 repeat from thyroglobulin, a cysteine-rich
RT module found in proteins from different families.";
RL Eur. J. Biochem. 240:125-133(1996).
RN [16]
RP SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISULFIDE BOND.
RX PubMed=8626858; DOI=10.1210/jcem.81.5.8626858;
RA Berndorfer U., Wilms H., Herzog V.;
RT "Multimerization of thyroglobulin (TG) during extracellular storage:
RT isolation of highly cross-linked TG from human thyroids.";
RL J. Clin. Endocrinol. Metab. 81:1918-1926(1996).
RN [17]
RP SULFATION.
RX PubMed=10448091; DOI=10.1006/bbrc.1999.1173;
RA Nlend M.-C., Cauvi D., Venot N., Chabaud O.;
RT "Sulfated tyrosines of thyroglobulin are involved in thyroid hormone
RT synthesis.";
RL Biochem. Biophys. Res. Commun. 262:193-197(1999).
RN [18]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Thyroid;
RX PubMed=11082042; DOI=10.1242/jcs.113.24.4487;
RA Tepel C., Broemme D., Herzog V., Brix K.;
RT "Cathepsin K in thyroid epithelial cells: sequence, localization and
RT possible function in extracellular proteolysis of thyroglobulin.";
RL J. Cell Sci. 113:4487-4498(2000).
RN [19]
RP GLYCOSYLATION AT SER-2749.
RX PubMed=16679516; DOI=10.1074/jbc.m513382200;
RA Conte M., Arcaro A., D'Angelo D., Gnata A., Mamone G., Ferranti P.,
RA Formisano S., Gentile F.;
RT "A single chondroitin 6-sulfate oligosaccharide unit at Ser-2730 of human
RT thyroglobulin enhances hormone formation and limits proteolytic
RT accessibility at the carboxyl terminus. Potential insights into thyroid
RT homeostasis and autoimmunity.";
RL J. Biol. Chem. 281:22200-22211(2006).
RN [20]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.6 ANGSTROMS), FUNCTION, SUBUNIT,
RP DISULFIDE BONDS, GLYCOSYLATION AT ASN-76; ASN-110; ASN-198; ASN-484;
RP ASN-947; ASN-1220; ASN-1349; ASN-1365; ASN-1716; ASN-1774; ASN-1869;
RP ASN-2013; ASN-2122; ASN-2250; ASN-2295 AND ASN-2582, IODINATION AT TYR-24;
RP TYR-108; TYR-149; TYR-234; TYR-1310; TYR-2540; TYR-2573 AND TYR-2766, AND
RP MUTAGENESIS OF TYR-24; TYR-108; TYR-149; TYR-234; ASP-1309; TYR-1310;
RP TYR-2540; TYR-2573 AND TYR-2766.
RX PubMed=32025030; DOI=10.1038/s41586-020-1995-4;
RA Coscia F., Taler-Vercic A., Chang V.T., Sinn L., O'Reilly F.J., Izore T.,
RA Renko M., Berger I., Rappsilber J., Turk D., Loewe J.;
RT "The structure of human thyroglobulin.";
RL Nature 578:627-630(2020).
RN [21]
RP VARIANT HIS-870.
RX PubMed=8094490; DOI=10.1016/0140-6736(93)90209-y;
RA Corral J., Martin C., Perez R., Sanchez I., Mories M.T., San Millan J.L.,
RA Miralles J.M., Gonzalez-Sarmiento R.;
RT "Thyroglobulin gene point mutation associated with non-endemic simple
RT goitre.";
RL Lancet 341:462-464(1993).
RN [22]
RP VARIANT AITD3 VAL-1028, VARIANTS TDH3 ARG-1264 AND SER-1996, AND VARIANTS
RP HIS-135; ASP-604; ASP-653; ALA-734; GLU-830; GLN-985 DEL; TYR-1043;
RP THR-1059; ARG-1437; HIS-1463; ASN-1838; THR-1936; TRP-1999; GLU-2091;
RP LEU-2149; ARG-2170; HIS-2242; ARG-2501 AND GLN-2530.
RX PubMed=10199792; DOI=10.1210/jcem.84.4.5633;
RA Hishinuma A., Takamatsu J., Ohyama Y., Yokozawa T., Kanno Y., Kuma K.,
RA Yoshida S., Matsuura N., Ieiri T.;
RT "Two novel cysteine substitutions (C1263R and C1995S) of thyroglobulin
RT cause a defect in intracellular transport of thyroglobulin in patients with
RT congenital goiter and the variant type of adenomatous goiter.";
RL J. Clin. Endocrinol. Metab. 84:1438-1444(1999).
RN [23]
RP VARIANT AITD3 VAL-1028, VARIANTS ALA-734 AND TRP-1999, AND INVOLVEMENT IN
RP AITD3.
RX PubMed=14657345; DOI=10.1073/pnas.2434175100;
RA Ban Y., Greenberg D.A., Concepcion E., Skrabanek L., Villanueva R.,
RA Tomer Y.;
RT "Amino acid substitutions in the thyroglobulin gene are associated with
RT susceptibility to human and murine autoimmune thyroid disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:15119-15124(2003).
RN [24]
RP VARIANTS TDH3 TYR-1897 AND GLN-2336.
RX PubMed=16477365; DOI=10.1007/s10038-006-0360-2;
RA Kitanaka S., Takeda A., Sato U., Miki Y., Hishinuma A., Ieiri T.,
RA Igarashi T.;
RT "A novel compound heterozygous mutation in the thyroglobulin gene resulting
RT in congenital goitrous hypothyroidism with high serum triiodothyronine
RT levels.";
RL J. Hum. Genet. 51:379-382(2006).
RN [25]
RP VARIANTS TDH3 TYR-183 AND ASP-2234, AND FUNCTION.
RX PubMed=17532758; DOI=10.1111/j.1365-2265.2007.02889.x;
RA Caputo M., Rivolta C.M., Esperante S.A., Gruneiro-Papendieck L., Chiesa A.,
RA Pellizas C.G., Gonzalez-Sarmiento R., Targovnik H.M.;
RT "Congenital hypothyroidism with goitre caused by new mutations in the
RT thyroglobulin gene.";
RL Clin. Endocrinol. (Oxf.) 67:351-357(2007).
RN [26]
RP VARIANT TDH3 ARG-2375.
RX PubMed=17244789; DOI=10.1210/jc.2006-1242;
RA Kanou Y., Hishinuma A., Tsunekawa K., Seki K., Mizuno Y., Fujisawa H.,
RA Imai T., Miura Y., Nagasaka T., Yamada C., Ieiri T., Murakami M.,
RA Murata Y.;
RT "Thyroglobulin gene mutations producing defective intracellular transport
RT of thyroglobulin are associated with increased thyroidal type 2
RT iodothyronine deiodinase activity.";
RL J. Clin. Endocrinol. Metab. 92:1451-1457(2007).
RN [27]
RP VARIANT TDH3 ASP-2234, CHARACTERIZATION OF VARIANT TDH3 ASP-2234,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19509106; DOI=10.1210/jc.2009-0150;
RA Pardo V., Vono-Toniolo J., Rubio I.G., Knobel M., Possato R.F.,
RA Targovnik H.M., Kopp P., Medeiros-Neto G.;
RT "The p.A2215D thyroglobulin gene mutation leads to deficient synthesis and
RT secretion of the mutated protein and congenital hypothyroidism with wide
RT phenotype variation.";
RL J. Clin. Endocrinol. Metab. 94:2938-2944(2009).
RN [28]
RP VARIANT TDH3 2336-ARG--LYS-2768 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: Acts as a substrate for the production of iodinated thyroid
CC hormones thyroxine (T4) and triiodothyronine (T3) (PubMed:32025030,
CC PubMed:17532758). The synthesis of T3 and T4 involves iodination of
CC selected tyrosine residues of TG/thyroglobulin followed by their
CC oxidative coupling in the thyroid follicle lumen (PubMed:32025030).
CC Following TG re-internalization and lysosomal-mediated proteolysis, T3
CC and T4 are released from the polypeptide backbone leading to their
CC secretion into the bloodstream (PubMed:32025030). One dimer produces 7
CC thyroid hormone molecules (PubMed:32025030).
CC {ECO:0000269|PubMed:17532758, ECO:0000269|PubMed:32025030}.
CC -!- SUBUNIT: Monomer (PubMed:32025030). Homodimer (via ChEL region); occurs
CC in the endoplasmic reticulum and is required for export to the Golgi
CC apparatus (PubMed:32025030). Homooligomer; disulfide-linked; stored in
CC this form in the thyroid follicle lumen (PubMed:8626858).
CC {ECO:0000269|PubMed:32025030, ECO:0000269|PubMed:8626858}.
CC -!- INTERACTION:
CC P01266; Q99523: SORT1; NbExp=3; IntAct=EBI-2800425, EBI-1057058;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11082042,
CC ECO:0000269|PubMed:19509106, ECO:0000269|PubMed:8626858}. Note=Secreted
CC into the thyroid follicle lumen (PubMed:19509106). Localizes to colloid
CC globules, a structure formed in the thyroid follicle lumen consisting
CC of cross-linked TG arranged in concentric layers (PubMed:8626858,
CC PubMed:11082042). {ECO:0000269|PubMed:11082042,
CC ECO:0000269|PubMed:19509106, ECO:0000269|PubMed:8626858}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Major;
CC IsoId=P01266-1; Sequence=Displayed;
CC Name=2; Synonyms=Minor;
CC IsoId=P01266-2; Sequence=VSP_012655;
CC -!- TISSUE SPECIFICITY: Specifically expressed in the thyroid gland.
CC {ECO:0000269|PubMed:11082042, ECO:0000269|PubMed:19509106,
CC ECO:0000269|PubMed:8626858}.
CC -!- DOMAIN: The cholinesterase-like (ChEL) region is required for
CC dimerization and export from the endoplasmic reticulum.
CC {ECO:0000250|UniProtKB:O08710}.
CC -!- PTM: Iodinated on tyrosine residues by TPO (PubMed:2760035,
CC PubMed:32025030). There are 4 pairs of iodinated tyrosines used for
CC coupling: acceptor Tyr-24 is coupled to donor Tyr-149 or Tyr-234,
CC acceptor Tyr-2573 is coupled to donor Tyr-2540, acceptor Tyr-2766 in
CC monomer 1 is coupled to donor Tyr-2766 in monomer 2 and acceptor Tyr-
CC 1310 in monomer 1 is coupled to donor Tyr-108 in monomer 2
CC (PubMed:32025030). {ECO:0000269|PubMed:2760035,
CC ECO:0000269|PubMed:32025030}.
CC -!- PTM: Sulfated tyrosines are desulfated during iodination.
CC {ECO:0000269|PubMed:10448091}.
CC -!- PTM: Undergoes sequential proteolysis by cathepsins to release
CC thyroxine (T4) and triiodothyronine (T3) hormones. In the thyroid
CC follicle lumen, cross-linked TG (storage form) is solubilized by
CC limited proteolysis mediated by cathepsins CTSB and/or CTSL. Partially
CC cleaved TG is further processed by CTSK/cathepsin K and/or CTSL
CC resulting in the release of T4. Following endocytosis, further
CC processing occurs leading to the release of T3 and more T4 hormones.
CC {ECO:0000250|UniProtKB:O08710}.
CC -!- DISEASE: Thyroid dyshormonogenesis 3 (TDH3) [MIM:274700]: A disorder
CC due to thyroid dyshormonogenesis, causing large goiters of elastic and
CC soft consistency in the majority of patients. Although the degree of
CC thyroid dysfunction varies considerably among patients with defective
CC thyroglobulin synthesis, patients usually have a relatively high serum
CC free triiodothyronine (T3) concentration with disproportionately low
CC free tetraiodothyronine (T4) level. The maintenance of relatively high
CC free T3 levels prevents profound tissue hypothyroidism except in brain
CC and pituitary, which are dependent on T4 supply, resulting in
CC neurologic and intellectual defects in some cases.
CC {ECO:0000269|PubMed:10199792, ECO:0000269|PubMed:16477365,
CC ECO:0000269|PubMed:17244789, ECO:0000269|PubMed:17532758,
CC ECO:0000269|PubMed:19509106, ECO:0000269|PubMed:27305979}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Autoimmune thyroid disease 3 (AITD3) [MIM:608175]: A complex
CC autoimmune disorder comprising two related diseases affecting the
CC thyroid: Graves disease and Hashimoto thyroiditis. In both disorders,
CC thyroid-reactive T-cells are formed and infiltrate the thyroid gland.
CC In Graves disease, the majority of the T-cells undergo a Th2
CC differentiation and activate B-cells to produce antibodies against the
CC TSH receptor, which stimulate the thyroid and cause clinical
CC hyperthyroidism. In contrast, Hashimoto thyroiditis is characterized by
CC Th1 switching of the thyroid-infiltrating T-cells, which induces
CC apoptosis of thyroid follicular cells and clinical hypothyroidism.
CC {ECO:0000269|PubMed:10199792, ECO:0000269|PubMed:14657345}.
CC Note=Disease susceptibility is associated with variants affecting the
CC gene represented in this entry.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
CC -!- CAUTION: The cholinesterase-like (ChEL) region lacks the Ser residue of
CC the catalytic triad suggesting that it has no esterase activity.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Thyroglobulin entry;
CC URL="https://en.wikipedia.org/wiki/Thyroglobulin";
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DR EMBL; X05615; CAA29104.1; -; mRNA.
DR EMBL; U93033; AAC51924.1; -; mRNA.
DR EMBL; AF230667; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF235100; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF230666; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF305872; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X02154; CAA26089.1; -; mRNA.
DR EMBL; X06059; CAA29454.1; -; Genomic_DNA.
DR EMBL; X06060; CAA29454.1; JOINED; Genomic_DNA.
DR EMBL; X06061; CAA29454.1; JOINED; Genomic_DNA.
DR EMBL; X06062; CAA29454.1; JOINED; Genomic_DNA.
DR EMBL; X06063; CAA29454.1; JOINED; Genomic_DNA.
DR EMBL; X06064; CAA29454.1; JOINED; Genomic_DNA.
DR EMBL; X06065; CAA29454.1; JOINED; Genomic_DNA.
DR EMBL; X06066; CAA29454.1; JOINED; Genomic_DNA.
DR EMBL; X06067; CAA29455.1; -; Genomic_DNA.
DR EMBL; X06068; CAA29455.1; JOINED; Genomic_DNA.
DR EMBL; X06069; CAA29456.1; -; Genomic_DNA.
DR EMBL; X06070; CAA29456.1; JOINED; Genomic_DNA.
DR EMBL; X02749; CAA26527.1; -; Genomic_DNA.
DR EMBL; AH008122; AAD51647.1; -; Genomic_DNA.
DR EMBL; AH007064; AAC95473.1; -; Genomic_DNA.
DR EMBL; AF080484; AAD50912.2; -; Genomic_DNA.
DR EMBL; AF169654; AAD50912.2; JOINED; Genomic_DNA.
DR EMBL; AF169655; AAD50912.2; JOINED; Genomic_DNA.
DR EMBL; AF169656; AAD50912.2; JOINED; Genomic_DNA.
DR EMBL; AF169657; AAD50912.2; JOINED; Genomic_DNA.
DR EMBL; AF169658; AAD50912.2; JOINED; Genomic_DNA.
DR EMBL; AF169659; AAD50912.2; JOINED; Genomic_DNA.
DR EMBL; AF169661; AAD50912.2; JOINED; Genomic_DNA.
DR EMBL; AF169662; AAD50912.2; JOINED; Genomic_DNA.
DR EMBL; AF169663; AAD50912.2; JOINED; Genomic_DNA.
DR EMBL; AF169664; AAD50912.2; JOINED; Genomic_DNA.
DR EMBL; AF080472; AAD50912.2; JOINED; Genomic_DNA.
DR EMBL; AF080473; AAD50912.2; JOINED; Genomic_DNA.
DR EMBL; AF080474; AAD50912.2; JOINED; Genomic_DNA.
DR EMBL; AF080475; AAD50912.2; JOINED; Genomic_DNA.
DR EMBL; AF080476; AAD50912.2; JOINED; Genomic_DNA.
DR EMBL; AF080477; AAD50912.2; JOINED; Genomic_DNA.
DR EMBL; AF080478; AAD50912.2; JOINED; Genomic_DNA.
DR EMBL; AF080479; AAD50912.2; JOINED; Genomic_DNA.
DR EMBL; AF080480; AAD50912.2; JOINED; Genomic_DNA.
DR EMBL; AF080481; AAD50912.2; JOINED; Genomic_DNA.
DR EMBL; AF080482; AAD50912.2; JOINED; Genomic_DNA.
DR EMBL; AF080483; AAD50912.2; JOINED; Genomic_DNA.
DR EMBL; S40807; AAB22685.1; -; mRNA.
DR CCDS; CCDS34944.1; -. [P01266-1]
DR PIR; A59110; UIHU.
DR RefSeq; NP_003226.4; NM_003235.4. [P01266-1]
DR RefSeq; XP_016869284.1; XM_017013795.1. [P01266-2]
DR PDB; 6SCJ; EM; 3.60 A; A/B=1-2768.
DR PDB; 7B75; EM; 3.20 A; A/B=1-2768.
DR PDBsum; 6SCJ; -.
DR PDBsum; 7B75; -.
DR SMR; P01266; -.
DR BioGRID; 112896; 5.
DR ELM; P01266; -.
DR IntAct; P01266; 4.
DR STRING; 9606.ENSP00000220616; -.
DR DrugBank; DB05382; Iodine.
DR ESTHER; human-TG; Thyroglobulin.
DR MEROPS; I31.950; -.
DR MEROPS; S09.978; -.
DR CarbonylDB; P01266; -.
DR GlyConnect; 600; 21 N-Linked glycans (1 site).
DR GlyGen; P01266; 22 sites, 20 N-linked glycans (2 sites).
DR iPTMnet; P01266; -.
DR PhosphoSitePlus; P01266; -.
DR BioMuta; TG; -.
DR DMDM; 126302607; -.
DR MassIVE; P01266; -.
DR PaxDb; P01266; -.
DR PeptideAtlas; P01266; -.
DR PRIDE; P01266; -.
DR ProteomicsDB; 51364; -. [P01266-1]
DR ProteomicsDB; 51365; -. [P01266-2]
DR ABCD; P01266; 7 sequenced antibodies.
DR Antibodypedia; 860; 1901 antibodies from 44 providers.
DR DNASU; 7038; -.
DR Ensembl; ENST00000220616.9; ENSP00000220616.4; ENSG00000042832.12. [P01266-1]
DR GeneID; 7038; -.
DR KEGG; hsa:7038; -.
DR MANE-Select; ENST00000220616.9; ENSP00000220616.4; NM_003235.5; NP_003226.4.
DR UCSC; uc003ytw.4; human. [P01266-1]
DR CTD; 7038; -.
DR DisGeNET; 7038; -.
DR GeneCards; TG; -.
DR HGNC; HGNC:11764; TG.
DR HPA; ENSG00000042832; Tissue enriched (thyroid).
DR MalaCards; TG; -.
DR MIM; 188450; gene.
DR MIM; 274700; phenotype.
DR MIM; 608175; phenotype.
DR neXtProt; NX_P01266; -.
DR OpenTargets; ENSG00000042832; -.
DR Orphanet; 95716; Familial thyroid dyshormonogenesis.
DR PharmGKB; PA36479; -.
DR VEuPathDB; HostDB:ENSG00000042832; -.
DR eggNOG; KOG1214; Eukaryota.
DR GeneTree; ENSGT00940000159300; -.
DR HOGENOM; CLU_000943_0_0_1; -.
DR InParanoid; P01266; -.
DR OMA; SGPYVPQ; -.
DR OrthoDB; 754103at2759; -.
DR PhylomeDB; P01266; -.
DR TreeFam; TF351833; -.
DR BioCyc; MetaCyc:ENSG00000042832-MON; -.
DR PathwayCommons; P01266; -.
DR SignaLink; P01266; -.
DR SIGNOR; P01266; -.
DR BioGRID-ORCS; 7038; 11 hits in 1076 CRISPR screens.
DR ChiTaRS; TG; human.
DR GeneWiki; Thyroglobulin; -.
DR GenomeRNAi; 7038; -.
DR Pharos; P01266; Tbio.
DR PRO; PR:P01266; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P01266; protein.
DR Bgee; ENSG00000042832; Expressed in left lobe of thyroid gland and 103 other tissues.
DR ExpressionAtlas; P01266; baseline and differential.
DR Genevisible; P01266; HS.
DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0042446; P:hormone biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0015705; P:iodide transport; IEA:Ensembl.
DR GO; GO:0031641; P:regulation of myelination; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; NAS:ProtInc.
DR GO; GO:0030878; P:thyroid gland development; IEP:UniProtKB.
DR GO; GO:0006590; P:thyroid hormone generation; IDA:UniProtKB.
DR CDD; cd00191; TY; 7.
DR Gene3D; 3.40.50.1820; -; 1.
DR Gene3D; 4.10.800.10; -; 10.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR019819; Carboxylesterase_B_CS.
DR InterPro; IPR016324; Thyroglobulin.
DR InterPro; IPR000716; Thyroglobulin_1.
DR InterPro; IPR036857; Thyroglobulin_1_sf.
DR InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR Pfam; PF00135; COesterase; 1.
DR Pfam; PF07699; Ephrin_rec_like; 1.
DR Pfam; PF00086; Thyroglobulin_1; 10.
DR PIRSF; PIRSF001831; Thyroglobulin; 1.
DR SMART; SM00211; TY; 10.
DR SUPFAM; SSF53474; SSF53474; 1.
DR SUPFAM; SSF57610; SSF57610; 11.
DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
DR PROSITE; PS00484; THYROGLOBULIN_1_1; 9.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 11.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Congenital hypothyroidism;
KW Direct protein sequencing; Disease variant; Disulfide bond; Glycoprotein;
KW Hormone; Iodination; Proteoglycan; Reference proteome; Repeat; Secreted;
KW Signal; Sulfation; Thyroid hormone; Thyroid hormones biosynthesis.
FT SIGNAL 1..19
FT /evidence="ECO:0000250|UniProtKB:F1RRV3"
FT CHAIN 20..2768
FT /note="Thyroglobulin"
FT /id="PRO_0000008636"
FT DOMAIN 31..92
FT /note="Thyroglobulin type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 93..160
FT /note="Thyroglobulin type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 161..297
FT /note="Thyroglobulin type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 298..358
FT /note="Thyroglobulin type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 605..658
FT /note="Thyroglobulin type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 659..726
FT /note="Thyroglobulin type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 727..921
FT /note="Thyroglobulin type-1 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 922..1073
FT /note="Thyroglobulin type-1 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 1074..1145
FT /note="Thyroglobulin type-1 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 1146..1210
FT /note="Thyroglobulin type-1 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT REPEAT 1456..1469
FT /note="Type II"
FT /evidence="ECO:0000269|PubMed:8797845"
FT REPEAT 1470..1486
FT /note="Type II"
FT /evidence="ECO:0000269|PubMed:8797845"
FT REPEAT 1487..1503
FT /note="Type II"
FT /evidence="ECO:0000269|PubMed:8797845"
FT DOMAIN 1511..1565
FT /note="Thyroglobulin type-1 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT REPEAT 1603..1723
FT /note="Type IIIA"
FT /evidence="ECO:0000269|PubMed:8797845"
FT REPEAT 1724..1892
FT /note="Type IIIB"
FT /evidence="ECO:0000269|PubMed:8797845"
FT REPEAT 1893..1995
FT /note="Type IIIA"
FT /evidence="ECO:0000269|PubMed:8797845"
FT REPEAT 1996..2129
FT /note="Type IIIB"
FT /evidence="ECO:0000269|PubMed:8797845"
FT REPEAT 2130..2187
FT /note="Type IIIA"
FT /evidence="ECO:0000269|PubMed:8797845"
FT REGION 521..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2188..2768
FT /note="Cholinesterase-like (ChEL)"
FT /evidence="ECO:0000250|UniProtKB:O08710"
FT REGION 2727..2768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 110
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:8615697"
FT SITE 496
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:8615697"
FT SITE 1869
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:8615697"
FT SITE 2122
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:8615697"
FT MOD_RES 24
FT /note="Iodotyrosine; alternate"
FT /evidence="ECO:0000269|PubMed:2760035"
FT MOD_RES 24
FT /note="Sulfotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:F1RRV3"
FT MOD_RES 24
FT /note="Thyroxine; alternate"
FT /evidence="ECO:0000269|PubMed:2760035,
FT ECO:0000305|PubMed:32025030"
FT MOD_RES 24
FT /note="Triiodothyronine; alternate"
FT /evidence="ECO:0000269|PubMed:2760035"
FT MOD_RES 108
FT /note="Iodotyrosine"
FT /evidence="ECO:0000305|PubMed:32025030"
FT MOD_RES 149
FT /note="Diiodotyrosine; alternate"
FT /evidence="ECO:0000269|PubMed:2760035"
FT MOD_RES 149
FT /note="Iodotyrosine; alternate"
FT /evidence="ECO:0000269|PubMed:2760035,
FT ECO:0000305|PubMed:32025030"
FT MOD_RES 234
FT /note="Iodotyrosine"
FT /evidence="ECO:0000305|PubMed:32025030"
FT MOD_RES 258
FT /note="Iodotyrosine"
FT /evidence="ECO:0000269|PubMed:2760035"
FT MOD_RES 704
FT /note="Diiodotyrosine; alternate"
FT /evidence="ECO:0000269|PubMed:2760035"
FT MOD_RES 704
FT /note="Iodotyrosine; alternate"
FT /evidence="ECO:0000269|PubMed:2760035"
FT MOD_RES 704
FT /note="Thyroxine; alternate"
FT /evidence="ECO:0000269|PubMed:2760035"
FT MOD_RES 704
FT /note="Triiodothyronine; alternate"
FT /evidence="ECO:0000269|PubMed:2760035"
FT MOD_RES 785
FT /note="Iodotyrosine"
FT /evidence="ECO:0000269|PubMed:2760035"
FT MOD_RES 866
FT /note="Diiodotyrosine; alternate"
FT /evidence="ECO:0000269|PubMed:2760035"
FT MOD_RES 866
FT /note="Iodotyrosine; alternate"
FT /evidence="ECO:0000269|PubMed:2760035"
FT MOD_RES 883
FT /note="Diiodotyrosine"
FT /evidence="ECO:0000269|PubMed:2760035"
FT MOD_RES 992
FT /note="Diiodotyrosine; alternate"
FT /evidence="ECO:0000269|PubMed:2760035"
FT MOD_RES 992
FT /note="Iodotyrosine; alternate"
FT /evidence="ECO:0000269|PubMed:2760035"
FT MOD_RES 1310
FT /note="Iodotyrosine"
FT /evidence="ECO:0000269|PubMed:2760035"
FT MOD_RES 1310
FT /note="Thyroxine"
FT /evidence="ECO:0000269|PubMed:2760035,
FT ECO:0000305|PubMed:32025030"
FT MOD_RES 1467
FT /note="Diiodotyrosine; alternate"
FT /evidence="ECO:0000269|PubMed:2760035"
FT MOD_RES 1467
FT /note="Iodotyrosine; alternate"
FT /evidence="ECO:0000269|PubMed:2760035"
FT MOD_RES 2184
FT /note="Iodotyrosine"
FT /evidence="ECO:0000269|PubMed:2760035"
FT MOD_RES 2540
FT /note="Iodotyrosine"
FT /evidence="ECO:0000305|PubMed:32025030"
FT MOD_RES 2573
FT /note="Diiodotyrosine; alternate"
FT /evidence="ECO:0000269|PubMed:2760035"
FT MOD_RES 2573
FT /note="Iodotyrosine; alternate"
FT /evidence="ECO:0000269|PubMed:2760035"
FT MOD_RES 2573
FT /note="Thyroxine; alternate"
FT /evidence="ECO:0000269|PubMed:2760035,
FT ECO:0000305|PubMed:32025030"
FT MOD_RES 2573
FT /note="Triiodothyronine; alternate"
FT /evidence="ECO:0000269|PubMed:2760035"
FT MOD_RES 2587
FT /note="Iodotyrosine"
FT /evidence="ECO:0000269|PubMed:2760035"
FT MOD_RES 2617
FT /note="Iodotyrosine"
FT /evidence="ECO:0000269|PubMed:2760035"
FT MOD_RES 2697
FT /note="Diiodotyrosine"
FT /evidence="ECO:0000269|PubMed:2760035"
FT MOD_RES 2766
FT /note="Diiodotyrosine; alternate"
FT /evidence="ECO:0000269|PubMed:2760035"
FT MOD_RES 2766
FT /note="Iodotyrosine; alternate"
FT /evidence="ECO:0000269|PubMed:2760035"
FT MOD_RES 2766
FT /note="Thyroxine; alternate"
FT /evidence="ECO:0000269|PubMed:2760035,
FT ECO:0000305|PubMed:32025030"
FT MOD_RES 2766
FT /note="Triiodothyronine; alternate"
FT /evidence="ECO:0000269|PubMed:2760035"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000269|PubMed:8615697, ECO:0000312|PDB:6SCJ"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000312|PDB:6SCJ"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000269|PubMed:8615697, ECO:0000312|PDB:6SCJ"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000269|PubMed:8615697, ECO:0000312|PDB:6SCJ"
FT CARBOHYD 529
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8615697"
FT CARBOHYD 748
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8615697"
FT CARBOHYD 816
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8615697"
FT CARBOHYD 947
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000269|PubMed:8615697, ECO:0000312|PDB:6SCJ"
FT CARBOHYD 1220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000269|PubMed:8615697, ECO:0000312|PDB:6SCJ"
FT CARBOHYD 1348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:8615697"
FT CARBOHYD 1349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000269|PubMed:8615697, ECO:0000312|PDB:6SCJ"
FT CARBOHYD 1365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000269|PubMed:8615697, ECO:0000312|PDB:6SCJ"
FT CARBOHYD 1716
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000269|PubMed:8615697, ECO:0000312|PDB:6SCJ"
FT CARBOHYD 1774
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000269|PubMed:8615697, ECO:0000312|PDB:6SCJ"
FT CARBOHYD 1869
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000312|PDB:6SCJ"
FT CARBOHYD 2013
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000269|PubMed:8615697, ECO:0000312|PDB:6SCJ"
FT CARBOHYD 2122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000312|PDB:6SCJ"
FT CARBOHYD 2250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000269|PubMed:8615697, ECO:0000312|PDB:6SCJ"
FT CARBOHYD 2295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000269|PubMed:8615697, ECO:0000312|PDB:6SCJ"
FT CARBOHYD 2582
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000269|PubMed:8615697, ECO:0000312|PDB:6SCJ"
FT CARBOHYD 2749
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000269|PubMed:16679516"
FT DISULFID 34..52
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:32025030, ECO:0000312|PDB:6SCJ"
FT DISULFID 63..70
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:32025030, ECO:0000312|PDB:6SCJ"
FT DISULFID 72..92
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:32025030, ECO:0000312|PDB:6SCJ"
FT DISULFID 96..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:32025030, ECO:0000312|PDB:6SCJ"
FT DISULFID 131..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:32025030, ECO:0000312|PDB:6SCJ"
FT DISULFID 140..160
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:32025030, ECO:0000312|PDB:6SCJ"
FT DISULFID 164..183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:32025030, ECO:0000312|PDB:6SCJ"
FT DISULFID 194..235
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:32025030, ECO:0000312|PDB:6SCJ"
FT DISULFID 237..297
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000312|PDB:6SCJ"
FT DISULFID 301..319
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:32025030, ECO:0000312|PDB:6SCJ"
FT DISULFID 330..336
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:32025030, ECO:0000312|PDB:6SCJ"
FT DISULFID 338..358
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:32025030, ECO:0000312|PDB:6SCJ"
FT DISULFID 364..620
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000312|PDB:6SCJ"
FT DISULFID 408..608
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000312|PDB:6SCJ"
FT DISULFID 631..636
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:32025030, ECO:0000312|PDB:6SCJ"
FT DISULFID 638..658
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:32025030, ECO:0000312|PDB:6SCJ"
FT DISULFID 662..687
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:32025030, ECO:0000312|PDB:6SCJ"
FT DISULFID 698..703
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:32025030, ECO:0000312|PDB:6SCJ"
FT DISULFID 705..726
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:32025030, ECO:0000312|PDB:6SCJ"
FT DISULFID 730..763
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:32025030, ECO:0000312|PDB:6SCJ"
FT DISULFID 774..898
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:32025030, ECO:0000312|PDB:6SCJ"
FT DISULFID 900..921
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:32025030, ECO:0000312|PDB:6SCJ"
FT DISULFID 925..1031
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000312|PDB:6SCJ"
FT DISULFID 1042..1049
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:32025030, ECO:0000312|PDB:6SCJ"
FT DISULFID 1051..1073
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:32025030, ECO:0000312|PDB:6SCJ"
FT DISULFID 1077..1108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:32025030, ECO:0000312|PDB:6SCJ"
FT DISULFID 1126..1145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:32025030, ECO:0000312|PDB:6SCJ"
FT DISULFID 1149..1169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:32025030, ECO:0000312|PDB:6SCJ"
FT DISULFID 1181..1188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:32025030, ECO:0000312|PDB:6SCJ"
FT DISULFID 1190..1210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:32025030, ECO:0000312|PDB:6SCJ"
FT DISULFID 1215..1264
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000312|PDB:6SCJ"
FT DISULFID 1231..1245
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000312|PDB:6SCJ"
FT DISULFID 1306..1356
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000312|PDB:6SCJ"
FT DISULFID 1331..1347
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000312|PDB:6SCJ"
FT DISULFID 1440..1459
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000312|PDB:6SCJ"
FT DISULFID 1462..1473
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000312|PDB:6SCJ"
FT DISULFID 1476..1490
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000312|PDB:6SCJ"
FT DISULFID 1493..1510
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000312|PDB:6SCJ"
FT DISULFID 1514..1523
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:32025030, ECO:0000312|PDB:6SCJ"
FT DISULFID 1543..1565
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:32025030, ECO:0000312|PDB:6SCJ"
FT DISULFID 1603..1627
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000312|PDB:6SCJ"
FT DISULFID 1607..1613
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000312|PDB:6SCJ"
FT DISULFID 1639..1662
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000312|PDB:6SCJ"
FT DISULFID 1724..1749
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000312|PDB:6SCJ"
FT DISULFID 1728..1734
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000312|PDB:6SCJ"
FT DISULFID 1733..1835
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000312|PDB:6SCJ"
FT DISULFID 1760..1777
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000312|PDB:6SCJ"
FT DISULFID 1893..1919
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000312|PDB:6SCJ"
FT DISULFID 1897..1904
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000312|PDB:6SCJ"
FT DISULFID 1928..1939
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000312|PDB:6SCJ"
FT DISULFID 1996..2024
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000312|PDB:6SCJ"
FT DISULFID 2000..2006
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000312|PDB:6SCJ"
FT DISULFID 2005..2076
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000312|PDB:6SCJ"
FT DISULFID 2035..2048
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000312|PDB:6SCJ"
FT DISULFID 2130..2154
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000312|PDB:6SCJ"
FT DISULFID 2134..2140
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000312|PDB:6SCJ"
FT DISULFID 2163..2172
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000312|PDB:6SCJ"
FT DISULFID 2264..2281
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:32025030, ECO:0000312|PDB:6SCJ"
FT DISULFID 2442..2453
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000312|PDB:6SCJ"
FT DISULFID 2591..2715
FT /evidence="ECO:0000269|PubMed:32025030,
FT ECO:0000312|PDB:6SCJ"
FT VAR_SEQ 1510..1567
FT /note="CVTDCQRNEAGLQCDQNGQYRASQKDRGSGKAFCVDGEGRRLPWWETEAPLE
FT DSQCLM -> L (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1639210"
FT /id="VSP_012655"
FT VARIANT 135
FT /note="Q -> H (in dbSNP:rs2069546)"
FT /evidence="ECO:0000269|PubMed:10199792"
FT /id="VAR_010212"
FT VARIANT 183
FT /note="C -> Y (in TDH3)"
FT /evidence="ECO:0000269|PubMed:17532758"
FT /id="VAR_063034"
FT VARIANT 515
FT /note="Q -> E (in dbSNP:rs180222)"
FT /evidence="ECO:0000269|PubMed:16421571"
FT /id="VAR_016190"
FT VARIANT 604
FT /note="S -> D (requires 2 nucleotide substitutions;
FT dbSNP:rs2069547)"
FT /evidence="ECO:0000269|PubMed:10199792,
FT ECO:0000269|PubMed:3595599, ECO:0000269|PubMed:3971976"
FT /id="VAR_016852"
FT VARIANT 653
FT /note="G -> D (in dbSNP:rs2069548)"
FT /evidence="ECO:0000269|PubMed:10199792,
FT ECO:0000269|PubMed:3595599, ECO:0000269|PubMed:3971976"
FT /id="VAR_016853"
FT VARIANT 734
FT /note="S -> A (associated with AITD3; dbSNP:rs180223)"
FT /evidence="ECO:0000269|PubMed:10199792,
FT ECO:0000269|PubMed:14657345, ECO:0000269|PubMed:3681978"
FT /id="VAR_010213"
FT VARIANT 777
FT /note="P -> L (in dbSNP:rs3739274)"
FT /id="VAR_049077"
FT VARIANT 815
FT /note="G -> R (in dbSNP:rs16904774)"
FT /id="VAR_049078"
FT VARIANT 830
FT /note="Q -> E (in dbSNP:rs2076737)"
FT /evidence="ECO:0000269|PubMed:10199792"
FT /id="VAR_010214"
FT VARIANT 870
FT /note="Q -> H (in dbSNP:rs2229843)"
FT /evidence="ECO:0000269|PubMed:8094490"
FT /id="VAR_002365"
FT VARIANT 985
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:10199792,
FT ECO:0000269|PubMed:3595599"
FT /id="VAR_016854"
FT VARIANT 988
FT /note="R -> P (in dbSNP:rs16893332)"
FT /id="VAR_049079"
FT VARIANT 1028
FT /note="M -> V (in AITD3; unknown pathological significance;
FT dbSNP:rs853326)"
FT /evidence="ECO:0000269|PubMed:10199792,
FT ECO:0000269|PubMed:14657345"
FT /id="VAR_010215"
FT VARIANT 1043
FT /note="H -> Y (in dbSNP:rs143983705)"
FT /evidence="ECO:0000269|PubMed:10199792,
FT ECO:0000269|PubMed:3595599"
FT /id="VAR_016855"
FT VARIANT 1059
FT /note="I -> T (in dbSNP:rs1016185504)"
FT /evidence="ECO:0000269|PubMed:10199792,
FT ECO:0000269|PubMed:3595599"
FT /id="VAR_016856"
FT VARIANT 1063
FT /note="L -> M (in dbSNP:rs11992497)"
FT /id="VAR_049080"
FT VARIANT 1222
FT /note="S -> L (in dbSNP:rs12549018)"
FT /id="VAR_049081"
FT VARIANT 1264
FT /note="C -> R (in TDH3; autosomal recessive;
FT dbSNP:rs2076738)"
FT /evidence="ECO:0000269|PubMed:10199792"
FT /id="VAR_010216"
FT VARIANT 1312
FT /note="D -> G (in dbSNP:rs2069556)"
FT /evidence="ECO:0000269|PubMed:11124863,
FT ECO:0000269|PubMed:3595599, ECO:0000269|PubMed:9186272"
FT /id="VAR_010217"
FT VARIANT 1437
FT /note="W -> R (in dbSNP:rs2069558)"
FT /evidence="ECO:0000269|PubMed:10199792,
FT ECO:0000269|PubMed:3595599"
FT /id="VAR_016857"
FT VARIANT 1463
FT /note="P -> H"
FT /evidence="ECO:0000269|PubMed:10199792,
FT ECO:0000269|PubMed:3595599"
FT /id="VAR_016858"
FT VARIANT 1740
FT /note="T -> K (in dbSNP:rs16904791)"
FT /id="VAR_049082"
FT VARIANT 1838
FT /note="D -> N (in dbSNP:rs2069561)"
FT /evidence="ECO:0000269|PubMed:10199792"
FT /id="VAR_010218"
FT VARIANT 1897
FT /note="C -> Y (in TDH3; dbSNP:rs121912649)"
FT /evidence="ECO:0000269|PubMed:16477365"
FT /id="VAR_063035"
FT VARIANT 1936
FT /note="A -> T (in dbSNP:rs2069562)"
FT /evidence="ECO:0000269|PubMed:10199792,
FT ECO:0000269|PubMed:3595599"
FT /id="VAR_016859"
FT VARIANT 1974
FT /note="M -> T (in dbSNP:rs56230101)"
FT /id="VAR_061173"
FT VARIANT 1996
FT /note="C -> S (in TDH3; autosomal recessive;
FT dbSNP:rs2076739)"
FT /evidence="ECO:0000269|PubMed:10199792"
FT /id="VAR_010219"
FT VARIANT 1999
FT /note="R -> W (benign variant; dbSNP:rs2076740)"
FT /evidence="ECO:0000269|PubMed:10199792,
FT ECO:0000269|PubMed:14657345"
FT /id="VAR_010220"
FT VARIANT 2091
FT /note="D -> E"
FT /evidence="ECO:0000269|PubMed:10199792,
FT ECO:0000269|PubMed:3595599"
FT /id="VAR_016860"
FT VARIANT 2149
FT /note="P -> L (in dbSNP:rs2069564)"
FT /evidence="ECO:0000269|PubMed:10199792,
FT ECO:0000269|PubMed:10524569, ECO:0000269|PubMed:3595599"
FT /id="VAR_016861"
FT VARIANT 2170
FT /note="Q -> R (in dbSNP:rs2069565)"
FT /evidence="ECO:0000269|PubMed:10199792,
FT ECO:0000269|PubMed:10524569, ECO:0000269|PubMed:3595599"
FT /id="VAR_016862"
FT VARIANT 2234
FT /note="A -> D (in TDH3; reduces thyroglobulin synthesis and
FT secretion; promotes thyroglobulin retention within the
FT endoplasmic reticulum; dbSNP:rs370991693)"
FT /evidence="ECO:0000269|PubMed:17532758,
FT ECO:0000269|PubMed:19509106"
FT /id="VAR_063036"
FT VARIANT 2242
FT /note="R -> H (in dbSNP:rs2069566)"
FT /evidence="ECO:0000269|PubMed:10199792,
FT ECO:0000269|PubMed:3595599"
FT /id="VAR_016863"
FT VARIANT 2336..2768
FT /note="Missing (in TDH3; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:27305979"
FT /id="VAR_078338"
FT VARIANT 2336
FT /note="R -> Q (in TDH3; dbSNP:rs121912650)"
FT /evidence="ECO:0000269|PubMed:16477365"
FT /id="VAR_063037"
FT VARIANT 2375
FT /note="G -> R (in TDH3; dbSNP:rs137854434)"
FT /evidence="ECO:0000269|PubMed:17244789"
FT /id="VAR_063038"
FT VARIANT 2455
FT /note="R -> H (in dbSNP:rs2272707)"
FT /id="VAR_049083"
FT VARIANT 2469
FT /note="L -> P (in dbSNP:rs2069568)"
FT /id="VAR_049084"
FT VARIANT 2501
FT /note="W -> R (in dbSNP:rs2069569)"
FT /evidence="ECO:0000269|PubMed:10199792"
FT /id="VAR_010221"
FT VARIANT 2526
FT /note="F -> L (in dbSNP:rs12114109)"
FT /id="VAR_049085"
FT VARIANT 2530
FT /note="R -> Q (in dbSNP:rs1133076)"
FT /evidence="ECO:0000269|PubMed:10199792"
FT /id="VAR_010222"
FT VARIANT 2616
FT /note="N -> S (in dbSNP:rs10091530)"
FT /id="VAR_049086"
FT MUTAGEN 24
FT /note="Y->F: Abolishes thyroxine (T4) production; when
FT associated with F-1310, F-2573 and F-2766."
FT /evidence="ECO:0000269|PubMed:32025030"
FT MUTAGEN 108
FT /note="Y->F: Severe loss of thyroxine (T4) production; when
FT associated with F-149 or F-234, and F-2540 and F-2766.
FT Abolishes thyroxine (T4) production; when associated with
FT F-149, F-234, F-2540 and F-2766."
FT /evidence="ECO:0000269|PubMed:32025030"
FT MUTAGEN 149
FT /note="Y->F: Severe loss of thyroxine (T4) production; when
FT associated with F-108, F-2540 and F-2766. Abolishes
FT thyroxine (T4) production; when associated with F-108, F-
FT 234, F-2540 and F-2766."
FT /evidence="ECO:0000269|PubMed:32025030"
FT MUTAGEN 234
FT /note="Y->F: Severe loss of thyroxine (T4) production; when
FT associated with F-108, F-2540 and F-2766. Abolishes
FT thyroxine (T4) production; when associated with F-108, F-
FT 149, F-2540 and F-2766."
FT /evidence="ECO:0000269|PubMed:32025030"
FT MUTAGEN 1309
FT /note="D->S: Abolishes thyroxine (T4) production."
FT /evidence="ECO:0000269|PubMed:32025030"
FT MUTAGEN 1310
FT /note="Y->F: Abolishes thyroxine (T4) production; when
FT associated with F-24, F-2573 and F-2766."
FT /evidence="ECO:0000269|PubMed:32025030"
FT MUTAGEN 2540
FT /note="Y->F: Severe loss of thyroxine (T4) production; when
FT associated with F-149 or F-234, and F-108 and F-2766.
FT Abolishes thyroxine (T4) production; when associated with
FT F-108, F-149, F-234 and F-2766."
FT /evidence="ECO:0000269|PubMed:32025030"
FT MUTAGEN 2573
FT /note="Y->F: Abolishes thyroxine (T4) production; when
FT associated with F-24, F-1310 and F-2766."
FT /evidence="ECO:0000269|PubMed:32025030"
FT MUTAGEN 2766
FT /note="Y->F: Abolishes thyroxine (T4) production; when
FT associated with F-24, F-1310 and F-2573."
FT /evidence="ECO:0000269|PubMed:32025030"
FT MUTAGEN 2766
FT /note="Y->F: Severe loss of thyroxine (T4) production; when
FT associated with F-149 or F-234, and F-108 and F-2540.
FT Abolishes thyroxine (T4) production; when associated with
FT F-108, F-149, F-234 and F-2540."
FT /evidence="ECO:0000269|PubMed:32025030"
FT CONFLICT 23..25
FT /note="EYQ -> GKF (in Ref. 6; CAA26527)"
FT /evidence="ECO:0000305"
FT CONFLICT 848
FT /note="Missing (in Ref. 13; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 984..985
FT /note="EQ -> DR (in Ref. 5; CAA29456)"
FT /evidence="ECO:0000305"
FT CONFLICT 1359..1360
FT /note="Missing (in Ref. 13; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1717
FT /note="L -> A (in Ref. 13; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1776
FT /note="T -> S (in Ref. 13; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 2019
FT /note="G -> H (in Ref. 13; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 2287
FT /note="F -> P (in Ref. 13; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 33..43
FT /evidence="ECO:0007829|PDB:7B75"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 95..104
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 163..170
FT /evidence="ECO:0007829|PDB:7B75"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:7B75"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 221..227
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 275..290
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 300..311
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 321..325
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 327..330
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 365..375
FT /evidence="ECO:0007829|PDB:7B75"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 413..417
FT /evidence="ECO:0007829|PDB:7B75"
FT TURN 418..420
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 422..426
FT /evidence="ECO:0007829|PDB:7B75"
FT TURN 427..429
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 436..447
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 451..460
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 467..471
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 476..481
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 558..572
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 575..585
FT /evidence="ECO:0007829|PDB:7B75"
FT TURN 589..591
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 595..604
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 605..607
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 628..632
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 635..639
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 641..643
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 651..654
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 661..673
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 689..691
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 700..704
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 729..745
FT /evidence="ECO:0007829|PDB:7B75"
FT TURN 754..756
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 764..768
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 771..773
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 779..791
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 792..794
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 797..805
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 867..869
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 877..879
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 894..896
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 899..901
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 924..948
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 955..961
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 968..970
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 979..985
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 991..1008
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1033..1035
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1039..1042
FT /evidence="ECO:0007829|PDB:7B75"
FT TURN 1044..1046
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1048..1051
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1054..1056
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 1076..1086
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1090..1093
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1095..1097
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1102..1104
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1110..1114
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1116..1119
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1124..1127
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1129..1131
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1133..1135
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1137..1139
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1142..1144
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 1148..1157
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1163..1165
FT /evidence="ECO:0007829|PDB:7B75"
FT TURN 1171..1173
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1203..1207
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1218..1220
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1227..1230
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1246..1249
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1254..1258
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1289..1295
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 1301..1303
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 1315..1327
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1331..1337
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1340..1345
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1365..1371
FT /evidence="ECO:0007829|PDB:7B75"
FT TURN 1372..1374
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1377..1380
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 1383..1391
FT /evidence="ECO:0007829|PDB:7B75"
FT TURN 1393..1395
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 1396..1404
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1437..1439
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1442..1446
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 1454..1456
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1459..1461
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1466..1475
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1484..1486
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1494..1496
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1500..1502
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 1507..1509
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 1513..1516
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1527..1529
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1531..1539
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1541..1543
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1546..1549
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 1553..1556
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 1576..1578
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1596..1598
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 1599..1606
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1621..1624
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1683..1686
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1691..1693
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1697..1700
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1708..1710
FT /evidence="ECO:0007829|PDB:7B75"
FT TURN 1712..1714
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 1719..1730
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1731..1733
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1736..1741
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1747..1752
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1756..1764
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1815..1821
FT /evidence="ECO:0007829|PDB:7B75"
FT TURN 1826..1828
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1831..1834
FT /evidence="ECO:0007829|PDB:7B75"
FT TURN 1848..1850
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1855..1858
FT /evidence="ECO:0007829|PDB:7B75"
FT TURN 1868..1870
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1876..1880
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1882..1884
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 1889..1899
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1905..1910
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1912..1915
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1917..1922
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1940..1945
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1948..1953
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1972..1975
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 1977..1983
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 1989..2002
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 2008..2014
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 2017..2019
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 2022..2029
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 2032..2034
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 2037..2039
FT /evidence="ECO:0007829|PDB:7B75"
FT TURN 2051..2053
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 2093..2096
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 2098..2100
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 2101..2103
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 2110..2116
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 2123..2136
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 2142..2147
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 2149..2157
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 2161..2164
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 2171..2178
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 2181..2185
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 2193..2195
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 2198..2203
FT /evidence="ECO:0007829|PDB:7B75"
FT TURN 2204..2206
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 2207..2210
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 2212..2218
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 2221..2227
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 2238..2241
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 2253..2256
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 2273..2277
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 2286..2291
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 2296..2302
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 2312..2314
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 2320..2326
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 2328..2333
FT /evidence="ECO:0007829|PDB:7B75"
FT TURN 2338..2341
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 2346..2350
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 2354..2368
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 2370..2372
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 2375..2385
FT /evidence="ECO:0007829|PDB:7B75"
FT TURN 2386..2393
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 2394..2397
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 2408..2414
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 2426..2440
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 2447..2454
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 2459..2471
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 2475..2477
FT /evidence="ECO:0007829|PDB:7B75"
FT TURN 2484..2487
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 2492..2495
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 2496..2498
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 2506..2509
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 2518..2520
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 2521..2530
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 2537..2547
FT /evidence="ECO:0007829|PDB:7B75"
FT TURN 2549..2552
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 2554..2563
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 2573..2588
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 2590..2602
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 2608..2613
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 2622..2624
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 2626..2631
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 2634..2636
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 2641..2644
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 2646..2664
FT /evidence="ECO:0007829|PDB:7B75"
FT TURN 2673..2675
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 2697..2699
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 2701..2703
FT /evidence="ECO:0007829|PDB:7B75"
FT STRAND 2706..2708
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 2712..2719
FT /evidence="ECO:0007829|PDB:7B75"
FT HELIX 2721..2726
FT /evidence="ECO:0007829|PDB:7B75"
SQ SEQUENCE 2768 AA; 304790 MW; 69A87D935F1BAA72 CRC64;
MALVLEIFTL LASICWVSAN IFEYQVDAQP LRPCELQRET AFLKQADYVP QCAEDGSFQT
VQCQNDGRSC WCVGANGSEV LGSRQPGRPV ACLSFCQLQK QQILLSGYIN STDTSYLPQC
QDSGDYAPVQ CDVQQVQCWC VDAEGMEVYG TRQLGRPKRC PRSCEIRNRR LLHGVGDKSP
PQCSAEGEFM PVQCKFVNTT DMMIFDLVHS YNRFPDAFVT FSSFQRRFPE VSGYCHCADS
QGRELAETGL ELLLDEIYDT IFAGLDLPST FTETTLYRIL QRRFLAVQSV ISGRFRCPTK
CEVERFTATS FGHPYVPSCR RNGDYQAVQC QTEGPCWCVD AQGKEMHGTR QQGEPPSCAE
GQSCASERQQ ALSRLYFGTS GYFSQHDLFS SPEKRWASPR VARFATSCPP TIKELFVDSG
LLRPMVEGQS QQFSVSENLL KEAIRAIFPS RGLARLALQF TTNPKRLQQN LFGGKFLVNV
GQFNLSGALG TRGTFNFSQF FQQLGLASFL NGGRQEDLAK PLSVGLDSNS STGTPEAAKK
DGTMNKPTVG SFGFEINLQE NQNALKFLAS LLELPEFLLF LQHAISVPED VARDLGDVME
TVLSSQTCEQ TPERLFVPSC TTEGSYEDVQ CFSGECWCVN SWGKELPGSR VRGGQPRCPT
DCEKQRARMQ SLMGSQPAGS TLFVPACTSE GHFLPVQCFN SECYCVDAEG QAIPGTRSAI
GKPKKCPTPC QLQSEQAFLR TVQALLSNSS MLPTLSDTYI PQCSTDGQWR QVQCNGPPEQ
VFELYQRWEA QNKGQDLTPA KLLVKIMSYR EAASGNFSLF IQSLYEAGQQ DVFPVLSQYP
SLQDVPLAAL EGKRPQPREN ILLEPYLFWQ ILNGQLSQYP GSYSDFSTPL AHFDLRNCWC
VDEAGQELEG MRSEPSKLPT CPGSCEEAKL RVLQFIRETE EIVSASNSSR FPLGESFLVA
KGIRLRNEDL GLPPLFPPRE AFAEQFLRGS DYAIRLAAQS TLSFYQRRRF SPDDSAGASA
LLRSGPYMPQ CDAFGSWEPV QCHAGTGHCW CVDEKGGFIP GSLTARSLQI PQCPTTCEKS
RTSGLLSSWK QARSQENPSP KDLFVPACLE TGEYARLQAS GAGTWCVDPA SGEELRPGSS
SSAQCPSLCN VLKSGVLSRR VSPGYVPACR AEDGGFSPVQ CDQAQGSCWC VMDSGEEVPG
TRVTGGQPAC ESPRCPLPFN ASEVVGGTIL CETISGPTGS AMQQCQLLCR QGSWSVFPPG
PLICSLESGR WESQLPQPRA CQRPQLWQTI QTQGHFQLQL PPGKMCSADY ADLLQTFQVF
ILDELTARGF CQIQVKTFGT LVSIPVCNNS SVQVGCLTRE RLGVNVTWKS RLEDIPVASL
PDLHDIERAL VGKDLLGRFT DLIQSGSFQL HLDSKTFPAE TIRFLQGDHF GTSPRTWFGC
SEGFYQVLTS EASQDGLGCV KCPEGSYSQD EECIPCPVGF YQEQAGSLAC VPCPVGRTTI
SAGAFSQTHC VTDCQRNEAG LQCDQNGQYR ASQKDRGSGK AFCVDGEGRR LPWWETEAPL
EDSQCLMMQK FEKVPESKVI FDANAPVAVR SKVPDSEFPV MQCLTDCTED EACSFFTVST
TEPEISCDFY AWTSDNVACM TSDQKRDALG NSKATSFGSL RCQVKVRSHG QDSPAVYLKK
GQGSTTTLQK RFEPTGFQNM LSGLYNPIVF SASGANLTDA HLFCLLACDR DLCCDGFVLT
QVQGGAIICG LLSSPSVLLC NVKDWMDPSE AWANATCPGV TYDQESHQVI LRLGDQEFIK
SLTPLEGTQD TFTNFQQVYL WKDSDMGSRP ESMGCRKDTV PRPASPTEAG LTTELFSPVD
LNQVIVNGNQ SLSSQKHWLF KHLFSAQQAN LWCLSRCVQE HSFCQLAEIT ESASLYFTCT
LYPEAQVCDD IMESNAQGCR LILPQMPKAL FRKKVILEDK VKNFYTRLPF QKLMGISIRN
KVPMSEKSIS NGFFECERRC DADPCCTGFG FLNVSQLKGG EVTCLTLNSL GIQMCSEENG
GAWRILDCGS PDIEVHTYPF GWYQKPIAQN NAPSFCPLVV LPSLTEKVSL DSWQSLALSS
VVVDPSIRHF DVAHVSTAAT SNFSAVRDLC LSECSQHEAC LITTLQTQPG AVRCMFYADT
QSCTHSLQGQ NCRLLLREEA THIYRKPGIS LLSYEASVPS VPISTHGRLL GRSQAIQVGT
SWKQVDQFLG VPYAAPPLAE RRFQAPEPLN WTGSWDASKP RASCWQPGTR TSTSPGVSED
CLYLNVFIPQ NVAPNASVLV FFHNTMDREE SEGWPAIDGS FLAAVGNLIV VTASYRVGVF
GFLSSGSGEV SGNWGLLDQV AALTWVQTHI RGFGGDPRRV SLAADRGGAD VASIHLLTAR
ATNSQLFRRA VLMGGSALSP AAVISHERAQ QQAIALAKEV SCPMSSSQEV VSCLRQKPAN
VLNDAQTKLL AVSGPFHYWG PVIDGHFLRE PPARALKRSL WVEVDLLIGS SQDDGLINRA
KAVKQFEESR GRTSSKTAFY QALQNSLGGE DSDARVEAAA TWYYSLEHST DDYASFSRAL
ENATRDYFII CPIIDMASAW AKRARGNVFM YHAPENYGHG SLELLADVQF ALGLPFYPAY
EGQFSLEEKS LSLKIMQYFS HFIRSGNPNY PYEFSRKVPT FATPWPDFVP RAGGENYKEF
SELLPNRQGL KKADCSFWSK YISSLKTSAD GAKGGQSAES EEEELTAGSG LREDLLSLQE
PGSKTYSK
