UniProtKB - O08710 (THYG_MOUSE)
Protein
Thyroglobulin
Gene
Tg
Organism
Mus musculus (Mouse)
Status
Functioni
Acts as a substrate for the production of iodinated thyroid hormones thyroxine (T4) and triiodothyronine (T3) (By similarity). The synthesis of T3 and T4 involves iodination of selected tyrosine residues of TG/thyroglobulin followed by their oxidative coupling (By similarity). Following TG re-internalization and lysosomal-mediated proteolysis, T3 and T4 are released from the polypeptide backbone leading to their secretion into the bloodstream (Probable). One dimer produces 7 thyroid hormone molecules (By similarity).By similarity1 Publication
Caution
The cholinesterase-like (ChEL) region lacks the Ser residue of the catalytic triad suggesting that it has no esterase activity.Curated
GO - Molecular functioni
- anion binding Source: MGI
- chaperone binding Source: MGI
- hormone activity Source: UniProtKB-KW
- identical protein binding Source: UniProtKB
- protein-containing complex binding Source: MGI
- signaling receptor binding Source: MGI
GO - Biological processi
- hormone biosynthetic process Source: UniProtKB-KW
- iodide transport Source: MGI
- regulation of myelination Source: MGI
- response to pH Source: MGI
- thyroid gland development Source: Ensembl
- thyroid hormone generation Source: UniProtKB
- thyroid hormone metabolic process Source: MGI
- transcytosis Source: MGI
Keywordsi
Molecular function | Hormone, Thyroid hormone |
Biological process | Thyroid hormones biosynthesis |
Protein family/group databases
ESTHERi | mouse-thyro, Thyroglobulin |
MEROPSi | S09.978 |
Names & Taxonomyi
Protein namesi | Recommended name: ThyroglobulinShort name: Tg |
Gene namesi | Name:Tg Synonyms:Tgn |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:98733, Tg |
Subcellular locationi
Endoplasmic reticulum
- endoplasmic reticulum Source: MGI
Extracellular region or secreted
- extracellular space Source: MGI
Golgi apparatus
- Golgi apparatus Source: MGI
Other locations
- perinuclear region of cytoplasm Source: MGI
- protein-containing complex Source: MGI
Keywords - Cellular componenti
SecretedPathology & Biotechi
Involvement in diseasei
Congenital goiter (cog) is caused by a hypertrophy of the thyroid gland (goiter). Mice have reduced growth rate, hypothyroidism due to reduced production of the thyroid hormones thyroxine (T4) and triiodothyronine (T3), and lack colloid globules, a structure in the thyroid follicle lumen that is enriched in Tg/thyroglobulin.1 Publication
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 2318 | G → R: Impairs secretion. 1 Publication | 1 |
Keywords - Diseasei
Disease variantPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 20 | By similarityAdd BLAST | 20 | |
ChainiPRO_0000008637 | 21 – 2766 | ThyroglobulinAdd BLAST | 2746 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 25 | Iodotyrosine; alternateBy similarity | 1 | |
Modified residuei | 25 | Sulfotyrosine; alternateBy similarity | 1 | |
Modified residuei | 25 | Thyroxine; alternateBy similarity | 1 | |
Modified residuei | 25 | Triiodothyronine; alternateBy similarity | 1 | |
Disulfide bondi | 35 ↔ 53 | PROSITE-ProRule annotation | ||
Disulfide bondi | 64 ↔ 71 | PROSITE-ProRule annotation | ||
Disulfide bondi | 73 ↔ 93 | PROSITE-ProRule annotation | ||
Disulfide bondi | 97 ↔ 121 | PROSITE-ProRule annotation | ||
Modified residuei | 109 | IodotyrosineBy similarity | 1 | |
Glycosylationi | 111 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 132 ↔ 139 | PROSITE-ProRule annotation | ||
Disulfide bondi | 141 ↔ 161 | PROSITE-ProRule annotation | ||
Modified residuei | 150 | Diiodotyrosine; alternateBy similarity | 1 | |
Modified residuei | 150 | Iodotyrosine; alternateBy similarity | 1 | |
Disulfide bondi | 165 ↔ 184 | PROSITE-ProRule annotation | ||
Disulfide bondi | 195 ↔ 236 | PROSITE-ProRule annotation | ||
Glycosylationi | 199 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 235 | IodotyrosineBy similarity | 1 | |
Modified residuei | 259 | IodotyrosineBy similarity | 1 | |
Disulfide bondi | 302 ↔ 320 | PROSITE-ProRule annotation | ||
Disulfide bondi | 331 ↔ 337 | PROSITE-ProRule annotation | ||
Disulfide bondi | 339 ↔ 359 | PROSITE-ProRule annotation | ||
Disulfide bondi | 365 ↔ 620 | By similarity | ||
Disulfide bondi | 408 ↔ 608 | By similarity | ||
Glycosylationi | 484 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 496 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 631 ↔ 636 | PROSITE-ProRule annotation | ||
Disulfide bondi | 638 ↔ 658 | PROSITE-ProRule annotation | ||
Disulfide bondi | 662 ↔ 687 | PROSITE-ProRule annotation | ||
Disulfide bondi | 698 ↔ 703 | PROSITE-ProRule annotation | ||
Modified residuei | 704 | Diiodotyrosine; alternateBy similarity | 1 | |
Modified residuei | 704 | Iodotyrosine; alternateBy similarity | 1 | |
Modified residuei | 704 | Thyroxine; alternateBy similarity | 1 | |
Modified residuei | 704 | Triiodothyronine; alternateBy similarity | 1 | |
Disulfide bondi | 705 ↔ 726 | PROSITE-ProRule annotation | ||
Disulfide bondi | 730 ↔ 763 | PROSITE-ProRule annotation | ||
Glycosylationi | 748 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 774 ↔ 899 | PROSITE-ProRule annotation | ||
Modified residuei | 785 | IodotyrosineBy similarity | 1 | |
Glycosylationi | 817 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 867 | Diiodotyrosine; alternateBy similarity | 1 | |
Modified residuei | 867 | Iodotyrosine; alternateBy similarity | 1 | |
Modified residuei | 884 | DiiodotyrosineBy similarity | 1 | |
Disulfide bondi | 901 ↔ 922 | PROSITE-ProRule annotation | ||
Disulfide bondi | 926 ↔ 1032 | By similarity | ||
Glycosylationi | 948 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 993 | Diiodotyrosine; alternateBy similarity | 1 | |
Modified residuei | 993 | Iodotyrosine; alternateBy similarity | 1 | |
Disulfide bondi | 1043 ↔ 1050 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1052 ↔ 1074 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1078 ↔ 1109 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1127 ↔ 1146 | PROSITE-ProRule annotation | ||
Glycosylationi | 1141 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1150 ↔ 1170 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1182 ↔ 1189 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1191 ↔ 1211 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1216 ↔ 1265 | By similarity | ||
Disulfide bondi | 1232 ↔ 1246 | By similarity | ||
Disulfide bondi | 1306 ↔ 1356 | By similarity | ||
Modified residuei | 1310 | IodotyrosineBy similarity | 1 | |
Modified residuei | 1310 | ThyroxineBy similarity | 1 | |
Disulfide bondi | 1331 ↔ 1347 | By similarity | ||
Glycosylationi | 1349 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1365 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1441 ↔ 1458 | By similarity | ||
Disulfide bondi | 1461 ↔ 1472 | By similarity | ||
Disulfide bondi | 1475 ↔ 1489 | By similarity | ||
Disulfide bondi | 1492 ↔ 1509 | By similarity | ||
Disulfide bondi | 1513 ↔ 1522 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1542 ↔ 1564 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1602 ↔ 1626 | By similarity | ||
Disulfide bondi | 1606 ↔ 1612 | By similarity | ||
Disulfide bondi | 1638 ↔ 1661 | By similarity | ||
Glycosylationi | 1715 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1723 ↔ 1748 | By similarity | ||
Disulfide bondi | 1727 ↔ 1733 | By similarity | ||
Glycosylationi | 1729 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1732 ↔ 1834 | By similarity | ||
Disulfide bondi | 1759 ↔ 1776 | By similarity | ||
Glycosylationi | 1773 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1864 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1890 ↔ 1916 | By similarity | ||
Disulfide bondi | 1894 ↔ 1901 | By similarity | ||
Disulfide bondi | 1925 ↔ 1936 | By similarity | ||
Glycosylationi | 1935 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1993 ↔ 2021 | By similarity | ||
Disulfide bondi | 1997 ↔ 2003 | By similarity | ||
Disulfide bondi | 2002 ↔ 2073 | By similarity | ||
Glycosylationi | 2010 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 2032 ↔ 2045 | By similarity | ||
Glycosylationi | 2120 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 2128 ↔ 2152 | By similarity | ||
Disulfide bondi | 2132 ↔ 2138 | By similarity | ||
Disulfide bondi | 2161 ↔ 2170 | By similarity | ||
Modified residuei | 2182 | IodotyrosineBy similarity | 1 | |
Glycosylationi | 2249 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 2263 ↔ 2280 | PROSITE-ProRule annotation | ||
Glycosylationi | 2294 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 2441 ↔ 2452 | By similarity | ||
Modified residuei | 2539 | ThyroxineBy similarity | 1 | |
Modified residuei | 2572 | Diiodotyrosine; alternateBy similarity | 1 | |
Modified residuei | 2572 | Iodotyrosine; alternateBy similarity | 1 | |
Modified residuei | 2572 | Thyroxine; alternateBy similarity | 1 | |
Modified residuei | 2572 | Triiodothyronine; alternateBy similarity | 1 | |
Glycosylationi | 2581 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 2586 | IodotyrosineBy similarity | 1 | |
Disulfide bondi | 2590 ↔ 2714 | By similarity | ||
Modified residuei | 2616 | IodotyrosineBy similarity | 1 | |
Modified residuei | 2696 | DiiodotyrosineBy similarity | 1 | |
Modified residuei | 2764 | Diiodotyrosine; alternateBy similarity | 1 | |
Modified residuei | 2764 | Iodotyrosine; alternateBy similarity | 1 | |
Modified residuei | 2764 | Thyroxine; alternateBy similarity | 1 | |
Modified residuei | 2764 | Triiodothyronine; alternateBy similarity | 1 |
Post-translational modificationi
Iodinated on tyrosine residues by TPO (By similarity). There are 4 pairs of iodinated tyrosines used for coupling: acceptor Tyr-25 is coupled to donor Tyr-150 or Tyr-235, acceptor Tyr-2572 is coupled to donor Tyr-2539, acceptor Tyr-2764 in monomer 1 is coupled to donor Tyr-2764 in monomer 2 and acceptor Tyr-1310 in monomer 1 is coupled to donor Tyr-109 in monomer 2 (By similarity).By similarity
Sulfated tyrosines are desulfated during iodination.By similarity
Undergoes sequential proteolysis by cathepsins to release thyroxine (T4) and triiodothyronine (T3) hormones (PubMed:12782676). In the thyroid follicle lumen, cross-linked TG (storage form) is solubilized by limited proteolysis mediated by cathepsins CTSB and/or CTSL (PubMed:12782676). Partially cleaved TG is further processed by CTSK/cathepsin K and/or CTSL resulting in the release of T4 (PubMed:12782676). Following endocytosis, further processing occurs leading to the release of T3 and more T4 hormones (Probable).1 Publication1 Publication
Keywords - PTMi
Disulfide bond, Glycoprotein, Iodination, SulfationProteomic databases
CPTACi | non-CPTAC-3953 |
EPDi | O08710 |
MaxQBi | O08710 |
PaxDbi | O08710 |
PRIDEi | O08710 |
ProteomicsDBi | 262987 |
PTM databases
GlyGeni | O08710, 20 sites |
iPTMneti | O08710 |
PhosphoSitePlusi | O08710 |
Expressioni
Tissue specificityi
Specifically expressed in the thyroid gland.1 Publication
Gene expression databases
Bgeei | ENSMUSG00000053469, Expressed in thyroid gland and 71 other tissues |
ExpressionAtlasi | O08710, baseline and differential |
Genevisiblei | O08710, MM |
Interactioni
Subunit structurei
Monomer (PubMed:12782676). Homodimer (via ChEL region); occurs in the endoplasmic reticulum and is required for export to the Golgi apparatus (PubMed:19276074, PubMed:12782676). Homooligomer; disulfide-linked; stored in this form in the thyroid follicle lumen (By similarity).
By similarity2 PublicationsGO - Molecular functioni
- chaperone binding Source: MGI
- hormone activity Source: UniProtKB-KW
- identical protein binding Source: UniProtKB
- signaling receptor binding Source: MGI
Protein-protein interaction databases
BioGRIDi | 204170, 3 interactors |
IntActi | O08710, 1 interactor |
STRINGi | 10090.ENSMUSP00000070239 |
Miscellaneous databases
RNActi | O08710, protein |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 32 – 93 | Thyroglobulin type-1 1PROSITE-ProRule annotationAdd BLAST | 62 | |
Domaini | 94 – 161 | Thyroglobulin type-1 2PROSITE-ProRule annotationAdd BLAST | 68 | |
Domaini | 162 – 298 | Thyroglobulin type-1 3PROSITE-ProRule annotationAdd BLAST | 137 | |
Domaini | 299 – 359 | Thyroglobulin type-1 4PROSITE-ProRule annotationAdd BLAST | 61 | |
Domaini | 605 – 658 | Thyroglobulin type-1 5PROSITE-ProRule annotationAdd BLAST | 54 | |
Domaini | 659 – 726 | Thyroglobulin type-1 6PROSITE-ProRule annotationAdd BLAST | 68 | |
Domaini | 727 – 922 | Thyroglobulin type-1 7PROSITE-ProRule annotationAdd BLAST | 196 | |
Domaini | 923 – 1074 | Thyroglobulin type-1 8PROSITE-ProRule annotationAdd BLAST | 152 | |
Domaini | 1075 – 1146 | Thyroglobulin type-1 9PROSITE-ProRule annotationAdd BLAST | 72 | |
Domaini | 1147 – 1211 | Thyroglobulin type-1 10PROSITE-ProRule annotationAdd BLAST | 65 | |
Repeati | 1455 – 1468 | Type IIBy similarityAdd BLAST | 14 | |
Repeati | 1469 – 1485 | Type IIBy similarityAdd BLAST | 17 | |
Repeati | 1486 – 1502 | Type IIBy similarityAdd BLAST | 17 | |
Domaini | 1510 – 1564 | Thyroglobulin type-1 11PROSITE-ProRule annotationAdd BLAST | 55 | |
Repeati | 1602 – 1722 | Type IIIABy similarityAdd BLAST | 121 | |
Repeati | 1723 – 1889 | Type IIIBBy similarityAdd BLAST | 167 | |
Repeati | 1890 – 1992 | Type IIIABy similarityAdd BLAST | 103 | |
Repeati | 1993 – 2125 | Type IIIBBy similarityAdd BLAST | 133 | |
Repeati | 2126 – 2183 | Type IIIABy similarityAdd BLAST | 58 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 2186 – 2766 | Cholinesterase-like (ChEL)1 PublicationAdd BLAST | 581 |
Domaini
The cholinesterase-like (ChEL) region is required for dimerization and export from the endoplasmic reticulum.1 Publication
Sequence similaritiesi
Belongs to the type-B carboxylesterase/lipase family.Curated
Keywords - Domaini
Repeat, SignalPhylogenomic databases
eggNOGi | KOG1214, Eukaryota |
GeneTreei | ENSGT00940000159300 |
HOGENOMi | CLU_000943_0_0_1 |
InParanoidi | O08710 |
OMAi | DEQCIPC |
OrthoDBi | 754103at2759 |
TreeFami | TF351833 |
Family and domain databases
CDDi | cd00191, TY, 7 hits |
Gene3Di | 3.40.50.1820, 1 hit 4.10.800.10, 7 hits |
InterProi | View protein in InterPro IPR029058, AB_hydrolase IPR002018, CarbesteraseB IPR019819, Carboxylesterase_B_CS IPR016324, Thyroglobulin IPR000716, Thyroglobulin_1 IPR036857, Thyroglobulin_1_sf IPR011641, Tyr-kin_ephrin_A/B_rcpt-like |
Pfami | View protein in Pfam PF00135, COesterase, 1 hit PF07699, Ephrin_rec_like, 1 hit PF00086, Thyroglobulin_1, 10 hits |
PIRSFi | PIRSF001831, Thyroglobulin, 1 hit |
SMARTi | View protein in SMART SM00211, TY, 10 hits |
SUPFAMi | SSF53474, SSF53474, 1 hit SSF57610, SSF57610, 11 hits |
PROSITEi | View protein in PROSITE PS00941, CARBOXYLESTERASE_B_2, 1 hit PS00484, THYROGLOBULIN_1_1, 9 hits PS51162, THYROGLOBULIN_1_2, 11 hits |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All
O08710-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MTALVLWVST LLSSVCLVAA NIFEYQVDAQ PLRPCELQRE KAFLKQAEYV
60 70 80 90 100
PQCSEDGSFQ TVQCQNDGQS CWCVDSDGRE VPGSRQLGRP TVCLSFCQLH
110 120 130 140 150
KQRILLGSYI NSTDALYLPQ CQDSGNYAPV QCDLQRVQCW CVDTEGMEVY
160 170 180 190 200
GTRQQGRPTR CPRSCEIRNR RLLHGVGDRS PPQCTADGEF MPVQCKFVNT
210 220 230 240 250
TDMMIFDLIH NYNRFPDAFV TFSSFRGRFP EVSGYCYCAD SQGRELAETG
260 270 280 290 300
LELLLDEIYD TIFAGLDQAS TFTQSTMYRI LQRRFLAIQL VISGRFRCPT
310 320 330 340 350
KCEVEQFAAT RFGHSYIPRC HRDGHYQTVQ CQTEGMCWCV DAQGREVPGT
360 370 380 390 400
RQQGQPPSCA ADQSCALERQ QALSRFYFET PDYFSPQDLL SSEDRLAPVS
410 420 430 440 450
GVRSDTSCPP RIKELFVDSG LLRSIAVEHY QRLSESRSLL REAIRAVFPS
460 470 480 490 500
RELAGLALQF TTNPKRLQQN LFGGTFLANA AQFNLSGALG TRSTFNFSQF
510 520 530 540 550
FQQFGLPGFL NRDRVTTLAK LLPVRLDSSS TPETLRVSEK TVAMNKRVVG
560 570 580 590 600
NFGFKVNLQE NQDALKFLVS LLELPEFLVF LQRAVSVPED IARDLGDVME
610 620 630 640 650
MVFSAQACKQ MPGKFFVPSC TAGGSYEDIQ CYAGECWCVD SRGKELDGSR
660 670 680 690 700
VRGGRPRCPT KCEKQRAQMQ SLASAQPAGS SFFVPTCTRE GYFLPVQCFN
710 720 730 740 750
SECYCVDTEG QVIPGTQSTV GEAKQCPSVC QLQAEQAFLG VVGVLLSNSS
760 770 780 790 800
MVPSISNVYI PQCSASGQWR HVQCDGPHEQ VFEWYERWKT QNGDGQELTP
810 820 830 840 850
AALLMKIVSY REVASRNFSL FLQSLYDAGQ QRIFPVLAQY PSLQDVPQVV
860 870 880 890 900
LEGATTPPGE NIFLDPYIFW QILNGQLSQY PGPYSDFNMP LEHFNLRSCW
910 920 930 940 950
CVDEAGQKLD GTQTKPGEIP ACPGPCEEVK LRVLKFIKET EEIVSASNAS
960 970 980 990 1000
SFPLGESFLV AKGIQLTSEE LDLPPQFPSR DAFSEKFLRG GEYAIRLAAQ
1010 1020 1030 1040 1050
STLTFYQSLR ASLGKSDGAA SLLWSGPYMP QCNMIGGWEP VQCHAGTGQC
1060 1070 1080 1090 1100
WCVDGRGEFI PGSLMSRSSQ MPQCPTNCEL SRASGLISAW KQAGPQRNPG
1110 1120 1130 1140 1150
PGDLFIPVCL QTGEYVRKQT SGTGTWCVDP ASGEGMPVNT NGSAQCPGLC
1160 1170 1180 1190 1200
DVLKSRALSR KVGLGYSPVC EALDGAFSPV QCDLAQGSCW CVLGSGEEVP
1210 1220 1230 1240 1250
GTRVVGTQPA CESPQCPLPF SGSDVADGVI FCETASSSGV TTVQQCQLLC
1260 1270 1280 1290 1300
RQGLRSAFSP GPLICSLESQ HWVTLPPPRA CQRPQLWQTM QTQAHFQLLL
1310 1320 1330 1340 1350
PPGKMCSVDY SGLLQAFQVF ILDELIARGF CQIQVKTFGT LVSSTVCDNS
1360 1370 1380 1390 1400
SIQVGCLTAE RLGVNVTWKL QLEDISVGSL PDLYSIERAV TGQDLLGRFA
1410 1420 1430 1440 1450
DLIQSGRFQL HLDSKTFSAD TTLYFLNGDS FVTSPRTQLG CMEGFYRVPT
1460 1470 1480 1490 1500
TRQDALGCVK CPEGSFSQDG RCTPCPAGTY QEQAGSSACI PCPRGRTTIT
1510 1520 1530 1540 1550
TGAFSKTHCV TDCQKNEAGL QCDQNGQYQA SQKNRDSGEV FCVDSEGRKL
1560 1570 1580 1590 1600
QWLQTEAGLS ESQCLMIRKF DKAPESKVIF DANSPVIVKS SVPSADSPLV
1610 1620 1630 1640 1650
QCLTDCANDE ACSFLTVSTM ESEVSCDFYS WTRDNFACVT SDQEQDAMGS
1660 1670 1680 1690 1700
LKATSFGSLR CQVKVRNSGK DSLAVYVKKG YESTAAGQKS FEPTGFQNVL
1710 1720 1730 1740 1750
SGLYSPVVFS ASGANLTDTH TYCLLACDND SCCDGFIITQ VKGGPTICGL
1760 1770 1780 1790 1800
LSSPDILLCH INDWRDTSAT QANATCAGVT YDQGSRQMTL SLGGQEFLQG
1810 1820 1830 1840 1850
LALLEGTQDS FTSFQQVYLW KDSDMGSRPE SMGCERGMVP RSDFPGDMAT
1860 1870 1880 1890 1900
ELFSPVDITQ VIVNTSHSLP SQQYWLFTHL FSAEQANLWC LSRCAQEPIF
1910 1920 1930 1940 1950
CQLADITKSS SLYFTCFLYP EAQVCDNVME SNAKNCSQIL PHQPTALFRR
1960 1970 1980 1990 2000
KVVLNDRVKN FYTRLPFQKL TGISIRDKVP MSGKLISNGF FECERLCDRD
2010 2020 2030 2040 2050
PCCTGFGFLN VSQLQGGEVT CLTLNSMGIQ TCNEESGATW RILDCGSEDT
2060 2070 2080 2090 2100
EVHTYPFGWY QKPAVWSDTP SFCPSAALQS LTEEKVTSDS WQTLALSSVI
2110 2120 2130 2140 2150
VDPSIKHFDV AHISTAATSN FSMAQDFCLQ QCSRHQDCLV TTLQIQPGVV
2160 2170 2180 2190 2200
RCVFYPDIQN CIHSLRSHTC WLLLHEEATY IYRKSGIPLV QSDVTSTPSV
2210 2220 2230 2240 2250
RIDSFGQLQG GSQVIKVGTA WKQVYRFLGV PYAAPPLADN RFRAPEVLNW
2260 2270 2280 2290 2300
TGSWDATKPR ASCWQPGTRT PTPPQINEDC LYLNVFVPEN LVSNASVLVF
2310 2320 2330 2340 2350
FHNTMEMEGS GGQLTIDGSI LAAVGNFIVV TANYRLGVFG FLSSGSDEVA
2360 2370 2380 2390 2400
GNWGLLDQVA ALTWVQSHIG AFGGDPQRVT LAADRSGADV ASIHLLISRP
2410 2420 2430 2440 2450
TRLQLFRKAL LMGGSALSPA AIISPERAQQ QAAALAKEVG CPTSSIQEVV
2460 2470 2480 2490 2500
SCLRQKPANI LNDAQTKLLA VSGPFHYWGP VVDGQYLREL PSRRLKRPLP
2510 2520 2530 2540 2550
VKVDLLIGGS QDDGLINRAK AVKQFEESQG RTNSKTAFYQ ALQNSLGGED
2560 2570 2580 2590 2600
SDARILAAAV WYYSLEHSTD DYASFSRALE NATRDYFIIC PMVNMASLWA
2610 2620 2630 2640 2650
RRTRGNVFMY HVPESYGHGS LELLADVQYA FGLPFYSAYQ GQFSTEEQSL
2660 2670 2680 2690 2700
SLKVMQYFSN FIRSGNPNYP HEFSRKAAEF ATPWPDFIPG AGGESYKELS
2710 2720 2730 2740 2750
AQLPNRQGLK QADCSFWSKY IQTLKDADGA KDAQLTKSEE EDLEVGPGLE
2760
EDLSGSLEPV PKSYSK
Computationally mapped potential isoform sequencesi
There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA6P7M8 | A6P7M8_MOUSE | Kidney thyroglobulin variant | Tg kTg | 367 | Annotation score: | ||
F6XYF6 | F6XYF6_MOUSE | Thyroglobulin | Tg | 1,147 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 80 | E → K in AAC32268 (PubMed:9707574).Curated | 1 | |
Sequence conflicti | 80 | E → K in AAC32269 (Ref. 3) Curated | 1 | |
Sequence conflicti | 92 | V → I in AAC32268 (PubMed:9707574).Curated | 1 | |
Sequence conflicti | 92 | V → I in AAC32269 (Ref. 3) Curated | 1 | |
Sequence conflicti | 1327 | A → T in AAB53204 (PubMed:9344706).Curated | 1 | |
Sequence conflicti | 1427 | N → S in AAB53204 (PubMed:9344706).Curated | 1 | |
Sequence conflicti | 1436 – 1442 | RTQLGCM → GLSLDVL in AAB53204 (PubMed:9344706).Curated | 7 | |
Sequence conflicti | 1721 | T → I in AAB53204 (PubMed:9344706).Curated | 1 | |
Sequence conflicti | 1813 | S → T in AAB53204 (PubMed:9344706).Curated | 1 | |
Sequence conflicti | 1957 – 1959 | RVK → KVN in AAC32268 (PubMed:9707574).Curated | 3 | |
Sequence conflicti | 1957 – 1959 | RVK → KVN in AAC32269 (Ref. 3) Curated | 3 | |
Sequence conflicti | 2090 | S → SS in AAB53204 (PubMed:9344706).Curated | 1 | |
Sequence conflicti | 2407 | R → K in AAC32268 (PubMed:9707574).Curated | 1 | |
Sequence conflicti | 2407 | R → K in AAC32269 (Ref. 3) Curated | 1 | |
Sequence conflicti | 2414 | G → S in AAC32268 (PubMed:9707574).Curated | 1 | |
Sequence conflicti | 2414 | G → S in AAC32269 (Ref. 3) Curated | 1 | |
Sequence conflicti | 2427 | R → K in AAC32268 (PubMed:9707574).Curated | 1 | |
Sequence conflicti | 2427 | R → K in AAC32269 (Ref. 3) Curated | 1 | |
Sequence conflicti | 2434 | A → T in AAC32268 (PubMed:9707574).Curated | 1 | |
Sequence conflicti | 2434 | A → T in AAC32269 (Ref. 3) Curated | 1 | |
Sequence conflicti | 2443 – 2453 | TSSIQEVVSCL → NFIHPGSGIMF in AAC32268 (PubMed:9707574).CuratedAdd BLAST | 11 | |
Sequence conflicti | 2443 – 2453 | TSSIQEVVSCL → NFIHPGSGIMF in AAC32269 (Ref. 3) CuratedAdd BLAST | 11 | |
Sequence conflicti | 2728 | D → GN in AAB53204 (PubMed:9344706).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 2283 | L → P in cog; impairs secretion due to ER retention. 1 Publication | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U76389 mRNA Translation: AAB53204.1 AF076186 mRNA Translation: AAC32268.1 AF076187 mRNA Translation: AAC32269.1 CH466545 Genomic DNA Translation: EDL29374.1 BC111467 mRNA Translation: AAI11468.1 |
CCDSi | CCDS37091.1 |
RefSeqi | NP_033401.2, NM_009375.2 |
Genome annotation databases
Ensembli | ENSMUST00000065916; ENSMUSP00000070239; ENSMUSG00000053469 |
GeneIDi | 21819 |
KEGGi | mmu:21819 |
UCSCi | uc007wap.1, mouse |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U76389 mRNA Translation: AAB53204.1 AF076186 mRNA Translation: AAC32268.1 AF076187 mRNA Translation: AAC32269.1 CH466545 Genomic DNA Translation: EDL29374.1 BC111467 mRNA Translation: AAI11468.1 |
CCDSi | CCDS37091.1 |
RefSeqi | NP_033401.2, NM_009375.2 |
3D structure databases
SMRi | O08710 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 204170, 3 interactors |
IntActi | O08710, 1 interactor |
STRINGi | 10090.ENSMUSP00000070239 |
Protein family/group databases
ESTHERi | mouse-thyro, Thyroglobulin |
MEROPSi | S09.978 |
PTM databases
GlyGeni | O08710, 20 sites |
iPTMneti | O08710 |
PhosphoSitePlusi | O08710 |
Proteomic databases
CPTACi | non-CPTAC-3953 |
EPDi | O08710 |
MaxQBi | O08710 |
PaxDbi | O08710 |
PRIDEi | O08710 |
ProteomicsDBi | 262987 |
Protocols and materials databases
ABCDi | O08710, 5 sequenced antibodies |
Antibodypediai | 860, 1771 antibodies |
Genome annotation databases
Ensembli | ENSMUST00000065916; ENSMUSP00000070239; ENSMUSG00000053469 |
GeneIDi | 21819 |
KEGGi | mmu:21819 |
UCSCi | uc007wap.1, mouse |
Organism-specific databases
CTDi | 7038 |
MGIi | MGI:98733, Tg |
Phylogenomic databases
eggNOGi | KOG1214, Eukaryota |
GeneTreei | ENSGT00940000159300 |
HOGENOMi | CLU_000943_0_0_1 |
InParanoidi | O08710 |
OMAi | DEQCIPC |
OrthoDBi | 754103at2759 |
TreeFami | TF351833 |
Miscellaneous databases
BioGRID-ORCSi | 21819, 1 hit in 53 CRISPR screens |
ChiTaRSi | Tg, mouse |
PROi | PR:O08710 |
RNActi | O08710, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000053469, Expressed in thyroid gland and 71 other tissues |
ExpressionAtlasi | O08710, baseline and differential |
Genevisiblei | O08710, MM |
Family and domain databases
CDDi | cd00191, TY, 7 hits |
Gene3Di | 3.40.50.1820, 1 hit 4.10.800.10, 7 hits |
InterProi | View protein in InterPro IPR029058, AB_hydrolase IPR002018, CarbesteraseB IPR019819, Carboxylesterase_B_CS IPR016324, Thyroglobulin IPR000716, Thyroglobulin_1 IPR036857, Thyroglobulin_1_sf IPR011641, Tyr-kin_ephrin_A/B_rcpt-like |
Pfami | View protein in Pfam PF00135, COesterase, 1 hit PF07699, Ephrin_rec_like, 1 hit PF00086, Thyroglobulin_1, 10 hits |
PIRSFi | PIRSF001831, Thyroglobulin, 1 hit |
SMARTi | View protein in SMART SM00211, TY, 10 hits |
SUPFAMi | SSF53474, SSF53474, 1 hit SSF57610, SSF57610, 11 hits |
PROSITEi | View protein in PROSITE PS00941, CARBOXYLESTERASE_B_2, 1 hit PS00484, THYROGLOBULIN_1_1, 9 hits PS51162, THYROGLOBULIN_1_2, 11 hits |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | THYG_MOUSE | |
Accessioni | O08710Primary (citable) accession number: O08710 Secondary accession number(s): O88590, Q2NKY1, Q9QWY7 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1997 |
Last sequence update: | July 27, 2011 | |
Last modified: | April 7, 2021 | |
This is version 175 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - SIMILARITY comments
Index of protein domains and families