P06882 · THYG_RAT

Function

function

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 (By similarity).
One dimer produces 7 thyroid hormone molecules (By similarity).

Caution

The cholinesterase-like (ChEL) region lacks the Ser residue of the catalytic triad suggesting that it has no esterase activity.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentextracellular space
Cellular Componentperinuclear region of cytoplasm
Cellular Componentprotein-containing complex
Molecular Functionanion binding
Molecular Functionhormone activity
Molecular Functionidentical protein binding
Molecular Functionprotein-containing complex binding
Molecular Functionprotein-folding chaperone binding
Molecular Functionsignaling receptor binding
Biological Processcellular response to genistein
Biological Processhormone biosynthetic process
Biological Processiodide transport
Biological Processregulation of myelination
Biological Processresponse to lipopolysaccharide
Biological Processresponse to pH
Biological Processthyroid gland development
Biological Processthyroid hormone generation
Biological Processthyroid hormone metabolic process
Biological Processtranscytosis

Keywords

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Thyroglobulin
  • Short names
    Tg

Gene names

    • Name
      Tg

Organism names

  • Taxonomic identifier
  • Strains
    • Wistar Imamichi
    • Fischer 344
    • Fischer
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    P06882
  • Secondary accessions
    • Q9JKY6
    • Q9JM94

Proteomes

Organism-specific databases

Subcellular Location

Secreted
Note: Secreted into the thyroid follicle lumen. Localizes to colloid globules, a structure formed in the thyroid follicle lumen consisting of cross-linked TG arranged in concentric layers.

Keywords

Phenotypes & Variants

Involvement in disease

  • Defects in Tg are a cause of a form of hypothyroidism in rdw rat

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variant2320in hypothyroidism; suppress secretion of Tg

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 1 variant from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Keywords

PTM/Processing

Features

Showing features for signal, chain, modified residue, disulfide bond, glycosylation.

TypeIDPosition(s)Description
Signal1-20
ChainPRO_000000863821-2768Thyroglobulin
Modified residue25Iodotyrosine; alternate
Modified residue25Sulfotyrosine; alternate
Modified residue25Thyroxine; alternate
Modified residue25Triiodothyronine; alternate
Disulfide bond35↔53
Disulfide bond64↔71
Disulfide bond73↔93
Disulfide bond97↔121
Modified residue109Iodotyrosine
Glycosylation111N-linked (GlcNAc...) asparagine
Disulfide bond132↔139
Disulfide bond141↔161
Modified residue150Diiodotyrosine; alternate
Modified residue150Iodotyrosine; alternate
Disulfide bond165↔184
Disulfide bond195↔236
Glycosylation199N-linked (GlcNAc...) asparagine
Modified residue235Iodotyrosine
Modified residue259Iodotyrosine
Disulfide bond302↔320
Disulfide bond331↔337
Disulfide bond339↔365
Disulfide bond408↔608
Glycosylation484N-linked (GlcNAc...) asparagine
Glycosylation496N-linked (GlcNAc...) asparagine
Glycosylation545N-linked (GlcNAc...) asparagine
Disulfide bond631↔636
Disulfide bond638↔658
Disulfide bond662↔687
Disulfide bond698↔703
Modified residue704Diiodotyrosine; alternate
Modified residue704Iodotyrosine; alternate
Modified residue704Thyroxine; alternate
Modified residue704Triiodothyronine; alternate
Disulfide bond705↔726
Disulfide bond730↔763
Glycosylation748N-linked (GlcNAc...) asparagine
Disulfide bond774↔899
Modified residue785Iodotyrosine
Glycosylation817N-linked (GlcNAc...) asparagine
Modified residue867Diiodotyrosine; alternate
Modified residue867Iodotyrosine; alternate
Modified residue884Diiodotyrosine
Disulfide bond901↔922
Disulfide bond926↔1032
Glycosylation948N-linked (GlcNAc...) asparagine
Modified residue993Diiodotyrosine; alternate
Modified residue993Iodotyrosine; alternate
Glycosylation1017N-linked (GlcNAc...) asparagine
Disulfide bond1043↔1050
Disulfide bond1052↔1074
Disulfide bond1078↔1109
Disulfide bond1127↔1146
Glycosylation1141N-linked (GlcNAc...) asparagine
Disulfide bond1150↔1170
Disulfide bond1182↔1189
Disulfide bond1191↔1211
Disulfide bond1216↔1265
Disulfide bond1232↔1246
Disulfide bond1306↔1356
Modified residue1310Iodotyrosine
Modified residue1310Thyroxine
Disulfide bond1331↔1347
Glycosylation1349N-linked (GlcNAc...) asparagine
Glycosylation1365N-linked (GlcNAc...) asparagine
Disulfide bond1441↔1458
Disulfide bond1461↔1472
Disulfide bond1475↔1489
Disulfide bond1492↔1509
Disulfide bond1513↔1522
Disulfide bond1542↔1564
Disulfide bond1602↔1626
Disulfide bond1606↔1612
Disulfide bond1638↔1661
Glycosylation1715N-linked (GlcNAc...) asparagine
Disulfide bond1723↔1748
Disulfide bond1727↔1733
Disulfide bond1732↔1834
Disulfide bond1759↔1776
Glycosylation1773N-linked (GlcNAc...) asparagine
Glycosylation1866N-linked (GlcNAc...) asparagine
Disulfide bond1892↔1918
Disulfide bond1896↔1903
Disulfide bond1927↔1938
Glycosylation1937N-linked (GlcNAc...) asparagine
Disulfide bond1995↔2023
Disulfide bond1999↔2005
Disulfide bond2004↔2075
Glycosylation2012N-linked (GlcNAc...) asparagine
Disulfide bond2034↔2047
Glycosylation2122N-linked (GlcNAc...) asparagine
Disulfide bond2130↔2154
Disulfide bond2134↔2140
Disulfide bond2163↔2172
Modified residue2184Iodotyrosine
Glycosylation2251N-linked (GlcNAc...) asparagine
Disulfide bond2265↔2282
Glycosylation2296N-linked (GlcNAc...) asparagine
Disulfide bond2443↔2454
Glycosylation2445N-linked (GlcNAc...) asparagine
Modified residue2541Thyroxine
Modified residue2574Diiodotyrosine; alternate
Modified residue2574Iodotyrosine; alternate
Modified residue2574Thyroxine; alternate
Modified residue2574Triiodothyronine; alternate
Glycosylation2583N-linked (GlcNAc...) asparagine
Modified residue2588Iodotyrosine
Disulfide bond2592↔2716
Modified residue2618Iodotyrosine
Modified residue2698Diiodotyrosine
Modified residue2766Diiodotyrosine; alternate
Modified residue2766Iodotyrosine; alternate
Modified residue2766Thyroxine; alternate
Modified residue2766Triiodothyronine; alternate

Post-translational modification

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-2574 is coupled to donor Tyr-2541, acceptor Tyr-2766 in monomer 1 is coupled to donor Tyr-2766 in monomer 2 and acceptor Tyr-1310 in monomer 1 is coupled to donor Tyr-109 in monomer 2 (By similarity).
Sulfated tyrosines are desulfated during iodination.
Undergoes sequential proteolysis by cathepsins to release thyroxine (T4) and triiodothyronine (T3) hormones. In the thyroid follicle lumen, cross-linked TG (storage form) is solubilized by limited proteolysis mediated by cathepsins CTSB and/or CTSL. Partially cleaved TG is further processed by CTSK/cathepsin K and/or CTSL resulting in the release of thyroxine (T4). Following endocytosis, further processing occurs leading to the release of triiodothyronine (T3) and more T4 hormones.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Specifically expressed in the thyroid gland.

Interaction

Subunit

Monomer (By similarity).
Homodimer (via ChEL region); occurs in the endoplasmic reticulum and is required for export to the Golgi apparatus (By similarity).
Homooligomer; disulfide-linked; stored in this form in the thyroid follicle lumen (By similarity).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P06882Hspa5 P067616EBI-1549657, EBI-916036
BINARY P06882Pdia4 P386593EBI-1549657, EBI-917435
XENO P06882SORT1 Q995234EBI-1549657, EBI-1057058

Protein-protein interaction databases

Structure

3D structure databases

Family & Domains

Features

Showing features for domain, repeat, region.

TypeIDPosition(s)Description
Domain32-93Thyroglobulin type-1 1
Domain94-161Thyroglobulin type-1 2
Domain162-298Thyroglobulin type-1 3
Domain299-359Thyroglobulin type-1 4
Domain605-658Thyroglobulin type-1 5
Domain659-726Thyroglobulin type-1 6
Domain727-922Thyroglobulin type-1 7
Domain923-1074Thyroglobulin type-1 8
Domain1075-1146Thyroglobulin type-1 9
Domain1147-1211Thyroglobulin type-1 10
Repeat1455-1468Type II
Repeat1469-1485Type II
Repeat1486-1502Type II
Domain1510-1564Thyroglobulin type-1 11
Repeat1602-1722Type IIIA
Repeat1723-1891Type IIIB
Repeat1892-1994Type IIIA
Repeat1995-2127Type IIIB
Repeat2128-2185Type IIIA
Region2188-2768Cholinesterase-like (ChEL)
Region2731-2768Disordered

Domain

The cholinesterase-like (ChEL) region is required for dimerization and export from the endoplasmic reticulum.

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    2,768
  • Mass (Da)
    304,645
  • Last updated
    2001-01-11 v4
  • Checksum
    290DD6943FF23F3D
MMTLVLWVSTLLSSVCLVAANIFEYQVDAQPLRPCELQREKAFLKQDEYVPQCSEDGSFQTVQCQNDGQSCWCVDSDGTEVPGSRQLGRPTACLSFCQLHKQRILLSSYINSTDALYLPQCQDSGNYAPVQCDLQQVQCWCVDTEGMEVYGTRQQGRPTRCPRSCEIRSRRLLHGVGDKSPPQCDADGEFMPVQCKFVNTTDMMIFDLIHNYNRFPDAFVTFSAFRNRFPEVSGYCYCADSQGRELAETGLELLLDEIYDTIFAGLDQASTFTQSTMYRILQRRFLAIQLVISGRFRCPTKCEVEQFTATSFGHPYIPSCHRDGHYQTVQCQMERMCWCVDAQGIEIPGTRQQGQPLFCAKDQSCASERQQALSRLYFETPGYFSPQDLLSSEDRLVPVSGARLDISCPPRIKELFVDSGLLRSIAVERYQQLSESRSLLREAIRAIFPSRELAGLALQFTTNPKRLQQNLFGGTFLVNAAQLNLSGALGTRSTFNFSQFFQQFGLPGFLVRDRATDLAKLLPVSLDSSPTPVPLRVPEKRVAMNKSVVGTFGFKVNLQENQDALKFLVSLMELPEFLVFLQRAVSVPEDRARDLGDVMEMVFSAQACKQTSGRFFVPSCTAEGSYEDIQCYAGECWCVNSQGKEVEGSRVSGGHPRCPTKCEKQRAQMQNLAGAQPAGSSFFVPTCTSEGYFLPVQCFNSECYCVDAEGQVIPGTQSTIGEPKLCPSVCQLQAEQAFLGVVGVLLSNSSMVPPISSVYIPQCSTSGQWMPVQCDGPHEQVFEWYERWNTQNSDGQELTTATLLMKLMSYREVASTNFSLFLQSLYDAGQQSIFPVLAQYPSLQDVPQVVLEGATIQPGENIFLDPYIFWQILNGQLSQYPGPYSDFSMPLEHFNLRSCWCVDEAGQELDGTRTRAGEIPACPGPCEEVKFRVLKFIKETEEIVSASNASSFPLGESFLVAKGIQLTSEELGLPPLYPSREAFSEKFLRGSEYAIRLAAQSTLTFYQKLRASLGESNGTASLLWSGPYMPQCNTIGGWEPVQCHPGTGQCWCVDGWGELIPGSLMARSSQMPQCPTSCELSRANGLISAWKQAGHQRNPGPGDLFTPVCLQTGEYVRQQTSGTGAWCVDPSSGEGVPTNTNSSAQCPGLCDALKSRVLSRKVGLGYTPVCEALDGGFSPVQCDLAQGSCWCVLASGEEVPGTRVVGTQPACESPQCPLPFSGSDVTDGVVFCETASSSGVTTVQQCQLFCRQGLRNVFSPGPLICNLESQRWVTLPLPRACQRPQLWQTMQTQAHFQLLLPPGKMCSIDYSGLLQAFQVFILDELITRGFCQIQVKTFGTLVSRTVCDNSSIQVGCLTAERLGVNATWKLQLEDISVGSLPNLHSIERALMGQDLLGRFANLIQSGKFQLHLDSKTFSADTILYFLNGDRFVTSPMTQLGCLEGFYRVSTTSQDPLGCVKCPEGSFSQDGKCTPCPAGTYQGQAGSSACIPCPRGRTTTITGAFSKTHCVTDCQRDEAGLQCDQNGQYQANQKDMDSGEVFCVDSEGQRLQWLQTEAGLSESQCLMMRKFEKAPESKVIFDASSPVIVKSRVPSANSPLVQCLADCADDEACSFVTVSSMSSEVSCDLYSWTRDNFACVTSDQEEDAVDSLKETSFGSLRCQVKVRNSGKDSLAVYVKKGHEFTASGQKSFEPTGFQNVLSGLYSSVVFSALGTNLTDTHLFCLLACDQDSCCDGFIVTQVKEGPTICGLLSAPDILVCHINDWRDASDTQANGTCAGVTYDQGSRQMTMSLGGQEFLQGLTLLEGTQDSFISFQQVYLWKDSDIGSRPESMGCGRGMVPKSEAPEGADMATELFSPVDITQVIVNTSHSLPSQQYWLSTHLFSAEQANLWCLSRCAQEPVFCQLADIMESSSLYFTCSLYPEAQVCDNDVESNAKNCSQILPRQPTALFQRKVVLNDRVKNFYTRLPFQKLSGISIRDRIPMSEKLISNGFFECERLCDRDPCCTGFGFLNVSQMQGGEMTCLTLNSMGIQTCSEENGATWRILDCGSEDTEVHTYPFGWYQKPAVWSDAPSFCPSAALQSLTEEKVALDSWQTLALSSVIIDPSIKHFDVAHISISATRNFSLAQDFCLQECSRHQDCLVTTLQIQQGVVRCVFYPDIQSCEHSLRSKTCWLLLHEEAAYIYRKSGAPLHQSDGISTPSVHIDSFGQLQGGSQVVKVGTAWKQVYQFLGVPYAAPPLAENRFQAPEVLNWTGSWDATKLRSSCWQPGTRTPTPPQISEDCLYLNVFVPENLVSNASVLVFFHNTVEMEGSGGQLNIDGSILAAVGNLIVVTANYRLGVFGFLSSGSDEVAGNWGLLDQVAALTWVQTHIGAFGGDPQRVTLAADRGGADVASIHLLITRPTRLQLFRKALLMGGSALSPAAIISPDRAQQQAAALAKEVGCPNSSVQEVVSCFRQKPANILNEAQTKLLAVSGPFHYWGPVVDGQYLRELPSRRLKRPLPVKVDLLIGGSQDDGLINRAKAVKQFEESQGRTNSKTAFYQALQNSLGGEDSDARILAAAIWYYSLEHSTDDYASFSRALENATRDYFIICPIVNMASLWARRTRGNVFMYHVPESYGHGSLELLADVQYAFGLPFYSAYQGYFSTEEQSLSLKVMQYFSNFIRSGNPNYPHEFSQKAAEFATPWPDFVPGAGGESYKELSAQLPNRQGLKKADCSFWSKYIQTLKDADGAKDAQLTKSGEEDLEVGPGSEEDFSGSLEPVPKSYSK

Computationally mapped potential isoform sequences

There are 5 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0G2JXY8A0A0G2JXY8_RATTg2720
A0A8I6AAP3A0A8I6AAP3_RATTg243
A0A1W2Q6Q9A0A1W2Q6Q9_RATTg134
G3V6V3G3V6V3_RATTg2768
A0A8I5ZUP4A0A8I5ZUP4_RATTg367

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict44in Ref. 4; AAA50379
Sequence conflict678in Ref. 2; AAF34909
Sequence conflict1492in Ref. 2; AAF34909
Sequence conflict1732-1733in Ref. 2; AAF34909
Sequence conflict1914in Ref. 5; CAA26183
Sequence conflict2043in Ref. 5; CAA26183
Sequence conflict2081in Ref. 5; CAA26183
Sequence conflict2126in Ref. 5; CAA26183
Sequence conflict2153in Ref. 5; CAA26183
Sequence conflict2169in Ref. 5; CAA26183
Sequence conflict2611in Ref. 5; CAA26183
Sequence conflict2658in Ref. 5; CAA26183

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB035201
EMBL· GenBank· DDBJ
BAA96132.1
EMBL· GenBank· DDBJ
mRNA
AF221622
EMBL· GenBank· DDBJ
AAF34909.1
EMBL· GenBank· DDBJ
mRNA
M35965
EMBL· GenBank· DDBJ
AAA42089.1
EMBL· GenBank· DDBJ
mRNA Different termination.
M12559
EMBL· GenBank· DDBJ
AAA50379.1
EMBL· GenBank· DDBJ
Genomic DNA
M12558
EMBL· GenBank· DDBJ
AAA50379.1
EMBL· GenBank· DDBJ
Genomic DNA
X02318
EMBL· GenBank· DDBJ
CAA26183.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp