THYG_RAT
ID THYG_RAT Reviewed; 2768 AA.
AC P06882; Q9JKY6; Q9JM94;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 4.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Thyroglobulin;
DE Short=Tg;
DE Flags: Precursor;
GN Name=Tg;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DISEASE, AND VARIANT
RP HYPOTHYROIDISM ARG-2320.
RC STRAIN=Wistar Imamichi;
RX PubMed=11089535; DOI=10.1210/endo.141.11.7794;
RA Hishinuma A., Furudate S., Oh-Ishi M., Nagakubo N., Namatame T., Ieiri T.;
RT "A novel missense mutation (G2320R) in thyroglobulin causes hypothyroidism
RT in rdw rats.";
RL Endocrinology 141:4050-4055(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Fischer 344;
RA Ding M., Jung C.-C., Cheng J.-M., Miyamoto T., Furudate S.I., Agui T.;
RT "A missense mutation in the thyroglobulin gene causes hypothyroidism and
RT dwarfism not associated with goiter in the WIC-rdw rat.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-213.
RC STRAIN=Fischer; TISSUE=Thymocyte;
RX PubMed=2325666; DOI=10.1210/mend-4-1-155;
RA Graves P.N., Davies T.F.;
RT "A second thyroglobulin messenger RNA species (rTg-2) in rat thyrocytes.";
RL Mol. Endocrinol. 4:155-161(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59.
RX PubMed=3455768; DOI=10.1073/pnas.83.2.323;
RA Musti A.M., Avvedimento V.E., Polistina C., Ursini V.M., Obici S.,
RA Nitsch L., Cocozza S., di Lauro R.;
RT "The complete structure of the rat thyroglobulin gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:323-327(1986).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1802-2768.
RX PubMed=3838512; DOI=10.1111/j.1432-1033.1985.tb08799.x;
RA di Lauro R., Obici S., Condliffe D., Ursini V.M., Musti A.M.,
RA Moscatelli C., Avvedimento V.E.;
RT "The sequence of 967 amino acids at the carboxyl-end of rat thyroglobulin.
RT Location and surroundings of two thyroxine-forming sites.";
RL Eur. J. Biochem. 148:7-11(1985).
CC -!- FUNCTION: Acts as a substrate for the production of iodinated thyroid
CC hormones thyroxine (T4) and triiodothyronine (T3) (By similarity). The
CC synthesis of T3 and T4 involves iodination of selected tyrosine
CC residues of TG/thyroglobulin followed by their oxidative coupling (By
CC similarity). Following TG re-internalization and lysosomal-mediated
CC proteolysis, T3 and T4 are released from the polypeptide backbone
CC leading to their secretion into the bloodstream (By similarity). One
CC dimer produces 7 thyroid hormone molecules (By similarity).
CC {ECO:0000250|UniProtKB:F1RRV3, ECO:0000250|UniProtKB:O08710,
CC ECO:0000250|UniProtKB:P01266}.
CC -!- SUBUNIT: Monomer (By similarity). Homodimer (via ChEL region); occurs
CC in the endoplasmic reticulum and is required for export to the Golgi
CC apparatus (By similarity). Homooligomer; disulfide-linked; stored in
CC this form in the thyroid follicle lumen (By similarity).
CC {ECO:0000250|UniProtKB:O08710, ECO:0000250|UniProtKB:P01266}.
CC -!- INTERACTION:
CC P06882; P06761: Hspa5; NbExp=6; IntAct=EBI-1549657, EBI-916036;
CC P06882; P38659: Pdia4; NbExp=3; IntAct=EBI-1549657, EBI-917435;
CC P06882; Q99523: SORT1; Xeno; NbExp=4; IntAct=EBI-1549657, EBI-1057058;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O08710}.
CC Note=Secreted into the thyroid follicle lumen. Localizes to colloid
CC globules, a structure formed in the thyroid follicle lumen consisting
CC of cross-linked TG arranged in concentric layers.
CC {ECO:0000250|UniProtKB:O08710}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in the thyroid gland.
CC {ECO:0000269|PubMed:11089535}.
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 (By similarity). There are 4
CC pairs of iodinated tyrosines used for coupling: acceptor Tyr-25 is
CC coupled to donor Tyr-150 or Tyr-235, acceptor Tyr-2574 is coupled to
CC donor Tyr-2541, acceptor Tyr-2766 in monomer 1 is coupled to donor Tyr-
CC 2766 in monomer 2 and acceptor Tyr-1310 in monomer 1 is coupled to
CC donor Tyr-109 in monomer 2 (By similarity).
CC {ECO:0000250|UniProtKB:F1RRV3, ECO:0000250|UniProtKB:P01266}.
CC -!- PTM: Sulfated tyrosines are desulfated during iodination.
CC {ECO:0000250|UniProtKB:P01266}.
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 thyroxine (T4). Following endocytosis,
CC further processing occurs leading to the release of triiodothyronine
CC (T3) and more T4 hormones. {ECO:0000250|UniProtKB:O08710}.
CC -!- DISEASE: Note=Defects in Tg are a cause of a form of hypothyroidism in
CC rdw rat. {ECO:0000269|PubMed:11089535}.
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}.
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DR EMBL; AB035201; BAA96132.1; -; mRNA.
DR EMBL; AF221622; AAF34909.1; -; mRNA.
DR EMBL; M35965; AAA42089.1; ALT_TERM; mRNA.
DR EMBL; M12559; AAA50379.1; -; Genomic_DNA.
DR EMBL; M12558; AAA50379.1; JOINED; Genomic_DNA.
DR EMBL; X02318; CAA26183.1; -; mRNA.
DR PIR; A22016; UIRT.
DR SMR; P06882; -.
DR CORUM; P06882; -.
DR IntAct; P06882; 4.
DR STRING; 10116.ENSRNOP00000009241; -.
DR ESTHER; ratno-thyro; Thyroglobulin.
DR MEROPS; I31.950; -.
DR MEROPS; S09.978; -.
DR GlyGen; P06882; 22 sites.
DR PaxDb; P06882; -.
DR PRIDE; P06882; -.
DR UCSC; RGD:3848; rat.
DR RGD; 3848; Tg.
DR eggNOG; KOG1214; Eukaryota.
DR InParanoid; P06882; -.
DR PhylomeDB; P06882; -.
DR PRO; PR:P06882; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0043168; F:anion binding; IDA:RGD.
DR GO; GO:0051087; F:chaperone binding; IPI:RGD.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0005102; F:signaling receptor binding; IDA:RGD.
DR GO; GO:0042446; P:hormone biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0015705; P:iodide transport; ISO:RGD.
DR GO; GO:0031641; P:regulation of myelination; ISO:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0009268; P:response to pH; IDA:RGD.
DR GO; GO:0030878; P:thyroid gland development; ISO:RGD.
DR GO; GO:0006590; P:thyroid hormone generation; IDA:RGD.
DR GO; GO:0042403; P:thyroid hormone metabolic process; ISO:RGD.
DR GO; GO:0045056; P:transcytosis; IDA:RGD.
DR CDD; cd00191; TY; 8.
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 Disease variant; Disulfide bond; Glycoprotein; Hormone; Iodination;
KW Reference proteome; Repeat; Secreted; Signal; Sulfation; Thyroid hormone;
KW Thyroid hormones biosynthesis.
FT SIGNAL 1..20
FT /evidence="ECO:0000250|UniProtKB:F1RRV3"
FT CHAIN 21..2768
FT /note="Thyroglobulin"
FT /id="PRO_0000008638"
FT DOMAIN 32..93
FT /note="Thyroglobulin type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 94..161
FT /note="Thyroglobulin type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 162..298
FT /note="Thyroglobulin type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 299..359
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..922
FT /note="Thyroglobulin type-1 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 923..1074
FT /note="Thyroglobulin type-1 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 1075..1146
FT /note="Thyroglobulin type-1 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 1147..1211
FT /note="Thyroglobulin type-1 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT REPEAT 1455..1468
FT /note="Type II"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT REPEAT 1469..1485
FT /note="Type II"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT REPEAT 1486..1502
FT /note="Type II"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DOMAIN 1510..1564
FT /note="Thyroglobulin type-1 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT REPEAT 1602..1722
FT /note="Type IIIA"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT REPEAT 1723..1891
FT /note="Type IIIB"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT REPEAT 1892..1994
FT /note="Type IIIA"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT REPEAT 1995..2127
FT /note="Type IIIB"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT REPEAT 2128..2185
FT /note="Type IIIA"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT REGION 2188..2768
FT /note="Cholinesterase-like (ChEL)"
FT /evidence="ECO:0000250|UniProtKB:O08710"
FT REGION 2731..2768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 25
FT /note="Iodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 25
FT /note="Sulfotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:F1RRV3"
FT MOD_RES 25
FT /note="Thyroxine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 25
FT /note="Triiodothyronine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 109
FT /note="Iodotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 150
FT /note="Diiodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 150
FT /note="Iodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 235
FT /note="Iodotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 259
FT /note="Iodotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 704
FT /note="Diiodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 704
FT /note="Iodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 704
FT /note="Thyroxine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 704
FT /note="Triiodothyronine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 785
FT /note="Iodotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 867
FT /note="Diiodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 867
FT /note="Iodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 884
FT /note="Diiodotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 993
FT /note="Diiodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 993
FT /note="Iodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 1310
FT /note="Iodotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 1310
FT /note="Thyroxine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2184
FT /note="Iodotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2541
FT /note="Thyroxine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2574
FT /note="Diiodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2574
FT /note="Iodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2574
FT /note="Thyroxine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2574
FT /note="Triiodothyronine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2588
FT /note="Iodotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2618
FT /note="Iodotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2698
FT /note="Diiodotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2766
FT /note="Diiodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2766
FT /note="Iodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2766
FT /note="Thyroxine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2766
FT /note="Triiodothyronine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 545
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 748
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 817
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 948
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1017
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1715
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1773
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1866
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1937
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2012
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2583
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 35..53
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 64..71
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 73..93
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 97..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 132..139
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 141..161
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 165..184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 195..236
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 302..320
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 331..337
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 339..365
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 408..608
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 631..636
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 638..658
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 662..687
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 698..703
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 705..726
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 730..763
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 774..899
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 901..922
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 926..1032
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1043..1050
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 1052..1074
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 1078..1109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 1127..1146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 1150..1170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 1182..1189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 1191..1211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 1216..1265
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1232..1246
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1306..1356
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1331..1347
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1441..1458
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1461..1472
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1475..1489
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1492..1509
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1513..1522
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 1542..1564
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 1602..1626
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1606..1612
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1638..1661
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1723..1748
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1727..1733
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1732..1834
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1759..1776
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1892..1918
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1896..1903
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1927..1938
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1995..2023
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1999..2005
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 2004..2075
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 2034..2047
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 2130..2154
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 2134..2140
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 2163..2172
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 2265..2282
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 2443..2454
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 2592..2716
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT VARIANT 2320
FT /note="G -> R (in hypothyroidism; suppress secretion of
FT Tg)"
FT /evidence="ECO:0000269|PubMed:11089535"
FT CONFLICT 44
FT /note="L -> V (in Ref. 4; AAA50379)"
FT /evidence="ECO:0000305"
FT CONFLICT 678
FT /note="A -> V (in Ref. 2; AAF34909)"
FT /evidence="ECO:0000305"
FT CONFLICT 1492
FT /note="C -> F (in Ref. 2; AAF34909)"
FT /evidence="ECO:0000305"
FT CONFLICT 1732..1733
FT /note="CC -> KS (in Ref. 2; AAF34909)"
FT /evidence="ECO:0000305"
FT CONFLICT 1914
FT /note="L -> F (in Ref. 5; CAA26183)"
FT /evidence="ECO:0000305"
FT CONFLICT 2043
FT /note="R -> A (in Ref. 5; CAA26183)"
FT /evidence="ECO:0000305"
FT CONFLICT 2081
FT /note="Q -> K (in Ref. 5; CAA26183)"
FT /evidence="ECO:0000305"
FT CONFLICT 2126
FT /note="A -> V (in Ref. 5; CAA26183)"
FT /evidence="ECO:0000305"
FT CONFLICT 2153
FT /note="R -> K (in Ref. 5; CAA26183)"
FT /evidence="ECO:0000305"
FT CONFLICT 2169
FT /note="S -> N (in Ref. 5; CAA26183)"
FT /evidence="ECO:0000305"
FT CONFLICT 2611
FT /note="M -> I (in Ref. 5; CAA26183)"
FT /evidence="ECO:0000305"
FT CONFLICT 2658
FT /note="Q -> H (in Ref. 5; CAA26183)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2768 AA; 304645 MW; 290DD6943FF23F3D CRC64;
MMTLVLWVST LLSSVCLVAA NIFEYQVDAQ PLRPCELQRE KAFLKQDEYV PQCSEDGSFQ
TVQCQNDGQS CWCVDSDGTE VPGSRQLGRP TACLSFCQLH KQRILLSSYI NSTDALYLPQ
CQDSGNYAPV QCDLQQVQCW CVDTEGMEVY GTRQQGRPTR CPRSCEIRSR RLLHGVGDKS
PPQCDADGEF MPVQCKFVNT TDMMIFDLIH NYNRFPDAFV TFSAFRNRFP EVSGYCYCAD
SQGRELAETG LELLLDEIYD TIFAGLDQAS TFTQSTMYRI LQRRFLAIQL VISGRFRCPT
KCEVEQFTAT SFGHPYIPSC HRDGHYQTVQ CQMERMCWCV DAQGIEIPGT RQQGQPLFCA
KDQSCASERQ QALSRLYFET PGYFSPQDLL SSEDRLVPVS GARLDISCPP RIKELFVDSG
LLRSIAVERY QQLSESRSLL REAIRAIFPS RELAGLALQF TTNPKRLQQN LFGGTFLVNA
AQLNLSGALG TRSTFNFSQF FQQFGLPGFL VRDRATDLAK LLPVSLDSSP TPVPLRVPEK
RVAMNKSVVG TFGFKVNLQE NQDALKFLVS LMELPEFLVF LQRAVSVPED RARDLGDVME
MVFSAQACKQ TSGRFFVPSC TAEGSYEDIQ CYAGECWCVN SQGKEVEGSR VSGGHPRCPT
KCEKQRAQMQ NLAGAQPAGS SFFVPTCTSE GYFLPVQCFN SECYCVDAEG QVIPGTQSTI
GEPKLCPSVC QLQAEQAFLG VVGVLLSNSS MVPPISSVYI PQCSTSGQWM PVQCDGPHEQ
VFEWYERWNT QNSDGQELTT ATLLMKLMSY REVASTNFSL FLQSLYDAGQ QSIFPVLAQY
PSLQDVPQVV LEGATIQPGE NIFLDPYIFW QILNGQLSQY PGPYSDFSMP LEHFNLRSCW
CVDEAGQELD GTRTRAGEIP ACPGPCEEVK FRVLKFIKET EEIVSASNAS SFPLGESFLV
AKGIQLTSEE LGLPPLYPSR EAFSEKFLRG SEYAIRLAAQ STLTFYQKLR ASLGESNGTA
SLLWSGPYMP QCNTIGGWEP VQCHPGTGQC WCVDGWGELI PGSLMARSSQ MPQCPTSCEL
SRANGLISAW KQAGHQRNPG PGDLFTPVCL QTGEYVRQQT SGTGAWCVDP SSGEGVPTNT
NSSAQCPGLC DALKSRVLSR KVGLGYTPVC EALDGGFSPV QCDLAQGSCW CVLASGEEVP
GTRVVGTQPA CESPQCPLPF SGSDVTDGVV FCETASSSGV TTVQQCQLFC RQGLRNVFSP
GPLICNLESQ RWVTLPLPRA CQRPQLWQTM QTQAHFQLLL PPGKMCSIDY SGLLQAFQVF
ILDELITRGF CQIQVKTFGT LVSRTVCDNS SIQVGCLTAE RLGVNATWKL QLEDISVGSL
PNLHSIERAL MGQDLLGRFA NLIQSGKFQL HLDSKTFSAD TILYFLNGDR FVTSPMTQLG
CLEGFYRVST TSQDPLGCVK CPEGSFSQDG KCTPCPAGTY QGQAGSSACI PCPRGRTTTI
TGAFSKTHCV TDCQRDEAGL QCDQNGQYQA NQKDMDSGEV FCVDSEGQRL QWLQTEAGLS
ESQCLMMRKF EKAPESKVIF DASSPVIVKS RVPSANSPLV QCLADCADDE ACSFVTVSSM
SSEVSCDLYS WTRDNFACVT SDQEEDAVDS LKETSFGSLR CQVKVRNSGK DSLAVYVKKG
HEFTASGQKS FEPTGFQNVL SGLYSSVVFS ALGTNLTDTH LFCLLACDQD SCCDGFIVTQ
VKEGPTICGL LSAPDILVCH INDWRDASDT QANGTCAGVT YDQGSRQMTM SLGGQEFLQG
LTLLEGTQDS FISFQQVYLW KDSDIGSRPE SMGCGRGMVP KSEAPEGADM ATELFSPVDI
TQVIVNTSHS LPSQQYWLST HLFSAEQANL WCLSRCAQEP VFCQLADIME SSSLYFTCSL
YPEAQVCDND VESNAKNCSQ ILPRQPTALF QRKVVLNDRV KNFYTRLPFQ KLSGISIRDR
IPMSEKLISN GFFECERLCD RDPCCTGFGF LNVSQMQGGE MTCLTLNSMG IQTCSEENGA
TWRILDCGSE DTEVHTYPFG WYQKPAVWSD APSFCPSAAL QSLTEEKVAL DSWQTLALSS
VIIDPSIKHF DVAHISISAT RNFSLAQDFC LQECSRHQDC LVTTLQIQQG VVRCVFYPDI
QSCEHSLRSK TCWLLLHEEA AYIYRKSGAP LHQSDGISTP SVHIDSFGQL QGGSQVVKVG
TAWKQVYQFL GVPYAAPPLA ENRFQAPEVL NWTGSWDATK LRSSCWQPGT RTPTPPQISE
DCLYLNVFVP ENLVSNASVL VFFHNTVEME GSGGQLNIDG SILAAVGNLI VVTANYRLGV
FGFLSSGSDE VAGNWGLLDQ VAALTWVQTH IGAFGGDPQR VTLAADRGGA DVASIHLLIT
RPTRLQLFRK ALLMGGSALS PAAIISPDRA QQQAAALAKE VGCPNSSVQE VVSCFRQKPA
NILNEAQTKL LAVSGPFHYW GPVVDGQYLR ELPSRRLKRP LPVKVDLLIG GSQDDGLINR
AKAVKQFEES QGRTNSKTAF YQALQNSLGG EDSDARILAA AIWYYSLEHS TDDYASFSRA
LENATRDYFI ICPIVNMASL WARRTRGNVF MYHVPESYGH GSLELLADVQ YAFGLPFYSA
YQGYFSTEEQ SLSLKVMQYF SNFIRSGNPN YPHEFSQKAA EFATPWPDFV PGAGGESYKE
LSAQLPNRQG LKKADCSFWS KYIQTLKDAD GAKDAQLTKS GEEDLEVGPG SEEDFSGSLE
PVPKSYSK
