P06882 · THYG_RAT
- ProteinThyroglobulin
- GeneTg
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2768 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | extracellular space | |
Cellular Component | perinuclear region of cytoplasm | |
Cellular Component | protein-containing complex | |
Molecular Function | anion binding | |
Molecular Function | hormone activity | |
Molecular Function | identical protein binding | |
Molecular Function | protein-containing complex binding | |
Molecular Function | protein-folding chaperone binding | |
Molecular Function | signaling receptor binding | |
Biological Process | cellular response to genistein | |
Biological Process | hormone biosynthetic process | |
Biological Process | iodide transport | |
Biological Process | regulation of myelination | |
Biological Process | response to lipopolysaccharide | |
Biological Process | response to pH | |
Biological Process | thyroid gland development | |
Biological Process | thyroid hormone generation | |
Biological Process | thyroid hormone metabolic process | |
Biological Process | transcytosis |
Keywords
- Molecular function
- Biological process
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameThyroglobulin
- Short namesTg
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionP06882
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
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
- Cellular component
Phenotypes & Variants
Involvement in disease
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 2320 | in hypothyroidism; suppress secretion of Tg | ||||
Sequence: G → R |
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.
Keywords
- Disease
PTM/Processing
Features
Showing features for signal, chain, modified residue, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MMTLVLWVSTLLSSVCLVAA | ||||||
Chain | PRO_0000008638 | 21-2768 | Thyroglobulin | |||
Sequence: NIFEYQVDAQPLRPCELQREKAFLKQDEYVPQCSEDGSFQTVQCQNDGQSCWCVDSDGTEVPGSRQLGRPTACLSFCQLHKQRILLSSYINSTDALYLPQCQDSGNYAPVQCDLQQVQCWCVDTEGMEVYGTRQQGRPTRCPRSCEIRSRRLLHGVGDKSPPQCDADGEFMPVQCKFVNTTDMMIFDLIHNYNRFPDAFVTFSAFRNRFPEVSGYCYCADSQGRELAETGLELLLDEIYDTIFAGLDQASTFTQSTMYRILQRRFLAIQLVISGRFRCPTKCEVEQFTATSFGHPYIPSCHRDGHYQTVQCQMERMCWCVDAQGIEIPGTRQQGQPLFCAKDQSCASERQQALSRLYFETPGYFSPQDLLSSEDRLVPVSGARLDISCPPRIKELFVDSGLLRSIAVERYQQLSESRSLLREAIRAIFPSRELAGLALQFTTNPKRLQQNLFGGTFLVNAAQLNLSGALGTRSTFNFSQFFQQFGLPGFLVRDRATDLAKLLPVSLDSSPTPVPLRVPEKRVAMNKSVVGTFGFKVNLQENQDALKFLVSLMELPEFLVFLQRAVSVPEDRARDLGDVMEMVFSAQACKQTSGRFFVPSCTAEGSYEDIQCYAGECWCVNSQGKEVEGSRVSGGHPRCPTKCEKQRAQMQNLAGAQPAGSSFFVPTCTSEGYFLPVQCFNSECYCVDAEGQVIPGTQSTIGEPKLCPSVCQLQAEQAFLGVVGVLLSNSSMVPPISSVYIPQCSTSGQWMPVQCDGPHEQVFEWYERWNTQNSDGQELTTATLLMKLMSYREVASTNFSLFLQSLYDAGQQSIFPVLAQYPSLQDVPQVVLEGATIQPGENIFLDPYIFWQILNGQLSQYPGPYSDFSMPLEHFNLRSCWCVDEAGQELDGTRTRAGEIPACPGPCEEVKFRVLKFIKETEEIVSASNASSFPLGESFLVAKGIQLTSEELGLPPLYPSREAFSEKFLRGSEYAIRLAAQSTLTFYQKLRASLGESNGTASLLWSGPYMPQCNTIGGWEPVQCHPGTGQCWCVDGWGELIPGSLMARSSQMPQCPTSCELSRANGLISAWKQAGHQRNPGPGDLFTPVCLQTGEYVRQQTSGTGAWCVDPSSGEGVPTNTNSSAQCPGLCDALKSRVLSRKVGLGYTPVCEALDGGFSPVQCDLAQGSCWCVLASGEEVPGTRVVGTQPACESPQCPLPFSGSDVTDGVVFCETASSSGVTTVQQCQLFCRQGLRNVFSPGPLICNLESQRWVTLPLPRACQRPQLWQTMQTQAHFQLLLPPGKMCSIDYSGLLQAFQVFILDELITRGFCQIQVKTFGTLVSRTVCDNSSIQVGCLTAERLGVNATWKLQLEDISVGSLPNLHSIERALMGQDLLGRFANLIQSGKFQLHLDSKTFSADTILYFLNGDRFVTSPMTQLGCLEGFYRVSTTSQDPLGCVKCPEGSFSQDGKCTPCPAGTYQGQAGSSACIPCPRGRTTTITGAFSKTHCVTDCQRDEAGLQCDQNGQYQANQKDMDSGEVFCVDSEGQRLQWLQTEAGLSESQCLMMRKFEKAPESKVIFDASSPVIVKSRVPSANSPLVQCLADCADDEACSFVTVSSMSSEVSCDLYSWTRDNFACVTSDQEEDAVDSLKETSFGSLRCQVKVRNSGKDSLAVYVKKGHEFTASGQKSFEPTGFQNVLSGLYSSVVFSALGTNLTDTHLFCLLACDQDSCCDGFIVTQVKEGPTICGLLSAPDILVCHINDWRDASDTQANGTCAGVTYDQGSRQMTMSLGGQEFLQGLTLLEGTQDSFISFQQVYLWKDSDIGSRPESMGCGRGMVPKSEAPEGADMATELFSPVDITQVIVNTSHSLPSQQYWLSTHLFSAEQANLWCLSRCAQEPVFCQLADIMESSSLYFTCSLYPEAQVCDNDVESNAKNCSQILPRQPTALFQRKVVLNDRVKNFYTRLPFQKLSGISIRDRIPMSEKLISNGFFECERLCDRDPCCTGFGFLNVSQMQGGEMTCLTLNSMGIQTCSEENGATWRILDCGSEDTEVHTYPFGWYQKPAVWSDAPSFCPSAALQSLTEEKVALDSWQTLALSSVIIDPSIKHFDVAHISISATRNFSLAQDFCLQECSRHQDCLVTTLQIQQGVVRCVFYPDIQSCEHSLRSKTCWLLLHEEAAYIYRKSGAPLHQSDGISTPSVHIDSFGQLQGGSQVVKVGTAWKQVYQFLGVPYAAPPLAENRFQAPEVLNWTGSWDATKLRSSCWQPGTRTPTPPQISEDCLYLNVFVPENLVSNASVLVFFHNTVEMEGSGGQLNIDGSILAAVGNLIVVTANYRLGVFGFLSSGSDEVAGNWGLLDQVAALTWVQTHIGAFGGDPQRVTLAADRGGADVASIHLLITRPTRLQLFRKALLMGGSALSPAAIISPDRAQQQAAALAKEVGCPNSSVQEVVSCFRQKPANILNEAQTKLLAVSGPFHYWGPVVDGQYLRELPSRRLKRPLPVKVDLLIGGSQDDGLINRAKAVKQFEESQGRTNSKTAFYQALQNSLGGEDSDARILAAAIWYYSLEHSTDDYASFSRALENATRDYFIICPIVNMASLWARRTRGNVFMYHVPESYGHGSLELLADVQYAFGLPFYSAYQGYFSTEEQSLSLKVMQYFSNFIRSGNPNYPHEFSQKAAEFATPWPDFVPGAGGESYKELSAQLPNRQGLKKADCSFWSKYIQTLKDADGAKDAQLTKSGEEDLEVGPGSEEDFSGSLEPVPKSYSK | ||||||
Modified residue | 25 | Iodotyrosine; alternate | ||||
Sequence: Y | ||||||
Modified residue | 25 | Sulfotyrosine; alternate | ||||
Sequence: Y | ||||||
Modified residue | 25 | Thyroxine; alternate | ||||
Sequence: Y | ||||||
Modified residue | 25 | Triiodothyronine; alternate | ||||
Sequence: Y | ||||||
Disulfide bond | 35↔53 | |||||
Sequence: CELQREKAFLKQDEYVPQC | ||||||
Disulfide bond | 64↔71 | |||||
Sequence: CQNDGQSC | ||||||
Disulfide bond | 73↔93 | |||||
Sequence: CVDSDGTEVPGSRQLGRPTAC | ||||||
Disulfide bond | 97↔121 | |||||
Sequence: CQLHKQRILLSSYINSTDALYLPQC | ||||||
Modified residue | 109 | Iodotyrosine | ||||
Sequence: Y | ||||||
Glycosylation | 111 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 132↔139 | |||||
Sequence: CDLQQVQC | ||||||
Disulfide bond | 141↔161 | |||||
Sequence: CVDTEGMEVYGTRQQGRPTRC | ||||||
Modified residue | 150 | Diiodotyrosine; alternate | ||||
Sequence: Y | ||||||
Modified residue | 150 | Iodotyrosine; alternate | ||||
Sequence: Y | ||||||
Disulfide bond | 165↔184 | |||||
Sequence: CEIRSRRLLHGVGDKSPPQC | ||||||
Disulfide bond | 195↔236 | |||||
Sequence: CKFVNTTDMMIFDLIHNYNRFPDAFVTFSAFRNRFPEVSGYC | ||||||
Glycosylation | 199 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 235 | Iodotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 259 | Iodotyrosine | ||||
Sequence: Y | ||||||
Disulfide bond | 302↔320 | |||||
Sequence: CEVEQFTATSFGHPYIPSC | ||||||
Disulfide bond | 331↔337 | |||||
Sequence: CQMERMC | ||||||
Disulfide bond | 339↔365 | |||||
Sequence: CVDAQGIEIPGTRQQGQPLFCAKDQSC | ||||||
Disulfide bond | 408↔608 | |||||
Sequence: CPPRIKELFVDSGLLRSIAVERYQQLSESRSLLREAIRAIFPSRELAGLALQFTTNPKRLQQNLFGGTFLVNAAQLNLSGALGTRSTFNFSQFFQQFGLPGFLVRDRATDLAKLLPVSLDSSPTPVPLRVPEKRVAMNKSVVGTFGFKVNLQENQDALKFLVSLMELPEFLVFLQRAVSVPEDRARDLGDVMEMVFSAQAC | ||||||
Glycosylation | 484 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 496 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 545 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 631↔636 | |||||
Sequence: CYAGEC | ||||||
Disulfide bond | 638↔658 | |||||
Sequence: CVNSQGKEVEGSRVSGGHPRC | ||||||
Disulfide bond | 662↔687 | |||||
Sequence: CEKQRAQMQNLAGAQPAGSSFFVPTC | ||||||
Disulfide bond | 698↔703 | |||||
Sequence: CFNSEC | ||||||
Modified residue | 704 | Diiodotyrosine; alternate | ||||
Sequence: Y | ||||||
Modified residue | 704 | Iodotyrosine; alternate | ||||
Sequence: Y | ||||||
Modified residue | 704 | Thyroxine; alternate | ||||
Sequence: Y | ||||||
Modified residue | 704 | Triiodothyronine; alternate | ||||
Sequence: Y | ||||||
Disulfide bond | 705↔726 | |||||
Sequence: CVDAEGQVIPGTQSTIGEPKLC | ||||||
Disulfide bond | 730↔763 | |||||
Sequence: CQLQAEQAFLGVVGVLLSNSSMVPPISSVYIPQC | ||||||
Glycosylation | 748 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 774↔899 | |||||
Sequence: CDGPHEQVFEWYERWNTQNSDGQELTTATLLMKLMSYREVASTNFSLFLQSLYDAGQQSIFPVLAQYPSLQDVPQVVLEGATIQPGENIFLDPYIFWQILNGQLSQYPGPYSDFSMPLEHFNLRSC | ||||||
Modified residue | 785 | Iodotyrosine | ||||
Sequence: Y | ||||||
Glycosylation | 817 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 867 | Diiodotyrosine; alternate | ||||
Sequence: Y | ||||||
Modified residue | 867 | Iodotyrosine; alternate | ||||
Sequence: Y | ||||||
Modified residue | 884 | Diiodotyrosine | ||||
Sequence: Y | ||||||
Disulfide bond | 901↔922 | |||||
Sequence: CVDEAGQELDGTRTRAGEIPAC | ||||||
Disulfide bond | 926↔1032 | |||||
Sequence: CEEVKFRVLKFIKETEEIVSASNASSFPLGESFLVAKGIQLTSEELGLPPLYPSREAFSEKFLRGSEYAIRLAAQSTLTFYQKLRASLGESNGTASLLWSGPYMPQC | ||||||
Glycosylation | 948 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 993 | Diiodotyrosine; alternate | ||||
Sequence: Y | ||||||
Modified residue | 993 | Iodotyrosine; alternate | ||||
Sequence: Y | ||||||
Glycosylation | 1017 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1043↔1050 | |||||
Sequence: CHPGTGQC | ||||||
Disulfide bond | 1052↔1074 | |||||
Sequence: CVDGWGELIPGSLMARSSQMPQC | ||||||
Disulfide bond | 1078↔1109 | |||||
Sequence: CELSRANGLISAWKQAGHQRNPGPGDLFTPVC | ||||||
Disulfide bond | 1127↔1146 | |||||
Sequence: CVDPSSGEGVPTNTNSSAQC | ||||||
Glycosylation | 1141 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1150↔1170 | |||||
Sequence: CDALKSRVLSRKVGLGYTPVC | ||||||
Disulfide bond | 1182↔1189 | |||||
Sequence: CDLAQGSC | ||||||
Disulfide bond | 1191↔1211 | |||||
Sequence: CVLASGEEVPGTRVVGTQPAC | ||||||
Disulfide bond | 1216↔1265 | |||||
Sequence: CPLPFSGSDVTDGVVFCETASSSGVTTVQQCQLFCRQGLRNVFSPGPLIC | ||||||
Disulfide bond | 1232↔1246 | |||||
Sequence: CETASSSGVTTVQQC | ||||||
Disulfide bond | 1306↔1356 | |||||
Sequence: CSIDYSGLLQAFQVFILDELITRGFCQIQVKTFGTLVSRTVCDNSSIQVGC | ||||||
Modified residue | 1310 | Iodotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 1310 | Thyroxine | ||||
Sequence: Y | ||||||
Disulfide bond | 1331↔1347 | |||||
Sequence: CQIQVKTFGTLVSRTVC | ||||||
Glycosylation | 1349 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1365 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1441↔1458 | |||||
Sequence: CLEGFYRVSTTSQDPLGC | ||||||
Disulfide bond | 1461↔1472 | |||||
Sequence: CPEGSFSQDGKC | ||||||
Disulfide bond | 1475↔1489 | |||||
Sequence: CPAGTYQGQAGSSAC | ||||||
Disulfide bond | 1492↔1509 | |||||
Sequence: CPRGRTTTITGAFSKTHC | ||||||
Disulfide bond | 1513↔1522 | |||||
Sequence: CQRDEAGLQC | ||||||
Disulfide bond | 1542↔1564 | |||||
Sequence: CVDSEGQRLQWLQTEAGLSESQC | ||||||
Disulfide bond | 1602↔1626 | |||||
Sequence: CLADCADDEACSFVTVSSMSSEVSC | ||||||
Disulfide bond | 1606↔1612 | |||||
Sequence: CADDEAC | ||||||
Disulfide bond | 1638↔1661 | |||||
Sequence: CVTSDQEEDAVDSLKETSFGSLRC | ||||||
Glycosylation | 1715 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1723↔1748 | |||||
Sequence: CLLACDQDSCCDGFIVTQVKEGPTIC | ||||||
Disulfide bond | 1727↔1733 | |||||
Sequence: CDQDSCC | ||||||
Disulfide bond | 1732↔1834 | |||||
Sequence: CCDGFIVTQVKEGPTICGLLSAPDILVCHINDWRDASDTQANGTCAGVTYDQGSRQMTMSLGGQEFLQGLTLLEGTQDSFISFQQVYLWKDSDIGSRPESMGC | ||||||
Disulfide bond | 1759↔1776 | |||||
Sequence: CHINDWRDASDTQANGTC | ||||||
Glycosylation | 1773 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1866 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1892↔1918 | |||||
Sequence: CLSRCAQEPVFCQLADIMESSSLYFTC | ||||||
Disulfide bond | 1896↔1903 | |||||
Sequence: CAQEPVFC | ||||||
Disulfide bond | 1927↔1938 | |||||
Sequence: CDNDVESNAKNC | ||||||
Glycosylation | 1937 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1995↔2023 | |||||
Sequence: CERLCDRDPCCTGFGFLNVSQMQGGEMTC | ||||||
Disulfide bond | 1999↔2005 | |||||
Sequence: CDRDPCC | ||||||
Disulfide bond | 2004↔2075 | |||||
Sequence: CCTGFGFLNVSQMQGGEMTCLTLNSMGIQTCSEENGATWRILDCGSEDTEVHTYPFGWYQKPAVWSDAPSFC | ||||||
Glycosylation | 2012 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2034↔2047 | |||||
Sequence: CSEENGATWRILDC | ||||||
Glycosylation | 2122 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2130↔2154 | |||||
Sequence: CLQECSRHQDCLVTTLQIQQGVVRC | ||||||
Disulfide bond | 2134↔2140 | |||||
Sequence: CSRHQDC | ||||||
Disulfide bond | 2163↔2172 | |||||
Sequence: CEHSLRSKTC | ||||||
Modified residue | 2184 | Iodotyrosine | ||||
Sequence: Y | ||||||
Glycosylation | 2251 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2265↔2282 | |||||
Sequence: CWQPGTRTPTPPQISEDC | ||||||
Glycosylation | 2296 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2443↔2454 | |||||
Sequence: CPNSSVQEVVSC | ||||||
Glycosylation | 2445 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 2541 | Thyroxine | ||||
Sequence: Y | ||||||
Modified residue | 2574 | Diiodotyrosine; alternate | ||||
Sequence: Y | ||||||
Modified residue | 2574 | Iodotyrosine; alternate | ||||
Sequence: Y | ||||||
Modified residue | 2574 | Thyroxine; alternate | ||||
Sequence: Y | ||||||
Modified residue | 2574 | Triiodothyronine; alternate | ||||
Sequence: Y | ||||||
Glycosylation | 2583 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 2588 | Iodotyrosine | ||||
Sequence: Y | ||||||
Disulfide bond | 2592↔2716 | |||||
Sequence: CPIVNMASLWARRTRGNVFMYHVPESYGHGSLELLADVQYAFGLPFYSAYQGYFSTEEQSLSLKVMQYFSNFIRSGNPNYPHEFSQKAAEFATPWPDFVPGAGGESYKELSAQLPNRQGLKKADC | ||||||
Modified residue | 2618 | Iodotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 2698 | Diiodotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 2766 | Diiodotyrosine; alternate | ||||
Sequence: Y | ||||||
Modified residue | 2766 | Iodotyrosine; alternate | ||||
Sequence: Y | ||||||
Modified residue | 2766 | Thyroxine; alternate | ||||
Sequence: Y | ||||||
Modified residue | 2766 | Triiodothyronine; alternate | ||||
Sequence: Y |
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).
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
- PTM
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).
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
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P06882 | Hspa5 P06761 | 6 | EBI-1549657, EBI-916036 | |
BINARY | P06882 | Pdia4 P38659 | 3 | EBI-1549657, EBI-917435 | |
XENO | P06882 | SORT1 Q99523 | 4 | EBI-1549657, EBI-1057058 |
Protein-protein interaction databases
Family & Domains
Features
Showing features for domain, repeat, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 32-93 | Thyroglobulin type-1 1 | ||||
Sequence: LRPCELQREKAFLKQDEYVPQCSEDGSFQTVQCQNDGQSCWCVDSDGTEVPGSRQLGRPTAC | ||||||
Domain | 94-161 | Thyroglobulin type-1 2 | ||||
Sequence: LSFCQLHKQRILLSSYINSTDALYLPQCQDSGNYAPVQCDLQQVQCWCVDTEGMEVYGTRQQGRPTRC | ||||||
Domain | 162-298 | Thyroglobulin type-1 3 | ||||
Sequence: PRSCEIRSRRLLHGVGDKSPPQCDADGEFMPVQCKFVNTTDMMIFDLIHNYNRFPDAFVTFSAFRNRFPEVSGYCYCADSQGRELAETGLELLLDEIYDTIFAGLDQASTFTQSTMYRILQRRFLAIQLVISGRFRC | ||||||
Domain | 299-359 | Thyroglobulin type-1 4 | ||||
Sequence: PTKCEVEQFTATSFGHPYIPSCHRDGHYQTVQCQMERMCWCVDAQGIEIPGTRQQGQPLFC | ||||||
Domain | 605-658 | Thyroglobulin type-1 5 | ||||
Sequence: AQACKQTSGRFFVPSCTAEGSYEDIQCYAGECWCVNSQGKEVEGSRVSGGHPRC | ||||||
Domain | 659-726 | Thyroglobulin type-1 6 | ||||
Sequence: PTKCEKQRAQMQNLAGAQPAGSSFFVPTCTSEGYFLPVQCFNSECYCVDAEGQVIPGTQSTIGEPKLC | ||||||
Domain | 727-922 | Thyroglobulin type-1 7 | ||||
Sequence: PSVCQLQAEQAFLGVVGVLLSNSSMVPPISSVYIPQCSTSGQWMPVQCDGPHEQVFEWYERWNTQNSDGQELTTATLLMKLMSYREVASTNFSLFLQSLYDAGQQSIFPVLAQYPSLQDVPQVVLEGATIQPGENIFLDPYIFWQILNGQLSQYPGPYSDFSMPLEHFNLRSCWCVDEAGQELDGTRTRAGEIPAC | ||||||
Domain | 923-1074 | Thyroglobulin type-1 8 | ||||
Sequence: PGPCEEVKFRVLKFIKETEEIVSASNASSFPLGESFLVAKGIQLTSEELGLPPLYPSREAFSEKFLRGSEYAIRLAAQSTLTFYQKLRASLGESNGTASLLWSGPYMPQCNTIGGWEPVQCHPGTGQCWCVDGWGELIPGSLMARSSQMPQC | ||||||
Domain | 1075-1146 | Thyroglobulin type-1 9 | ||||
Sequence: PTSCELSRANGLISAWKQAGHQRNPGPGDLFTPVCLQTGEYVRQQTSGTGAWCVDPSSGEGVPTNTNSSAQC | ||||||
Domain | 1147-1211 | Thyroglobulin type-1 10 | ||||
Sequence: PGLCDALKSRVLSRKVGLGYTPVCEALDGGFSPVQCDLAQGSCWCVLASGEEVPGTRVVGTQPAC | ||||||
Repeat | 1455-1468 | Type II | ||||
Sequence: PLGCVKCPEGSFSQ | ||||||
Repeat | 1469-1485 | Type II | ||||
Sequence: DGKCTPCPAGTYQGQAG | ||||||
Repeat | 1486-1502 | Type II | ||||
Sequence: SSACIPCPRGRTTTITG | ||||||
Domain | 1510-1564 | Thyroglobulin type-1 11 | ||||
Sequence: VTDCQRDEAGLQCDQNGQYQANQKDMDSGEVFCVDSEGQRLQWLQTEAGLSESQC | ||||||
Repeat | 1602-1722 | Type IIIA | ||||
Sequence: CLADCADDEACSFVTVSSMSSEVSCDLYSWTRDNFACVTSDQEEDAVDSLKETSFGSLRCQVKVRNSGKDSLAVYVKKGHEFTASGQKSFEPTGFQNVLSGLYSSVVFSALGTNLTDTHLF | ||||||
Repeat | 1723-1891 | Type IIIB | ||||
Sequence: CLLACDQDSCCDGFIVTQVKEGPTICGLLSAPDILVCHINDWRDASDTQANGTCAGVTYDQGSRQMTMSLGGQEFLQGLTLLEGTQDSFISFQQVYLWKDSDIGSRPESMGCGRGMVPKSEAPEGADMATELFSPVDITQVIVNTSHSLPSQQYWLSTHLFSAEQANLW | ||||||
Repeat | 1892-1994 | Type IIIA | ||||
Sequence: CLSRCAQEPVFCQLADIMESSSLYFTCSLYPEAQVCDNDVESNAKNCSQILPRQPTALFQRKVVLNDRVKNFYTRLPFQKLSGISIRDRIPMSEKLISNGFFE | ||||||
Repeat | 1995-2127 | Type IIIB | ||||
Sequence: CERLCDRDPCCTGFGFLNVSQMQGGEMTCLTLNSMGIQTCSEENGATWRILDCGSEDTEVHTYPFGWYQKPAVWSDAPSFCPSAALQSLTEEKVALDSWQTLALSSVIIDPSIKHFDVAHISISATRNFSLAQ | ||||||
Repeat | 2128-2185 | Type IIIA | ||||
Sequence: DFCLQECSRHQDCLVTTLQIQQGVVRCVFYPDIQSCEHSLRSKTCWLLLHEEAAYIYR | ||||||
Region | 2188-2768 | Cholinesterase-like (ChEL) | ||||
Sequence: GAPLHQSDGISTPSVHIDSFGQLQGGSQVVKVGTAWKQVYQFLGVPYAAPPLAENRFQAPEVLNWTGSWDATKLRSSCWQPGTRTPTPPQISEDCLYLNVFVPENLVSNASVLVFFHNTVEMEGSGGQLNIDGSILAAVGNLIVVTANYRLGVFGFLSSGSDEVAGNWGLLDQVAALTWVQTHIGAFGGDPQRVTLAADRGGADVASIHLLITRPTRLQLFRKALLMGGSALSPAAIISPDRAQQQAAALAKEVGCPNSSVQEVVSCFRQKPANILNEAQTKLLAVSGPFHYWGPVVDGQYLRELPSRRLKRPLPVKVDLLIGGSQDDGLINRAKAVKQFEESQGRTNSKTAFYQALQNSLGGEDSDARILAAAIWYYSLEHSTDDYASFSRALENATRDYFIICPIVNMASLWARRTRGNVFMYHVPESYGHGSLELLADVQYAFGLPFYSAYQGYFSTEEQSLSLKVMQYFSNFIRSGNPNYPHEFSQKAAEFATPWPDFVPGAGGESYKELSAQLPNRQGLKKADCSFWSKYIQTLKDADGAKDAQLTKSGEEDLEVGPGSEEDFSGSLEPVPKSYSK | ||||||
Region | 2731-2768 | Disordered | ||||
Sequence: GAKDAQLTKSGEEDLEVGPGSEEDFSGSLEPVPKSYSK |
Domain
The cholinesterase-like (ChEL) region is required for dimerization and export from the endoplasmic reticulum.
Sequence similarities
Belongs to the type-B carboxylesterase/lipase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length2,768
- Mass (Da)304,645
- Last updated2001-01-11 v4
- Checksum290DD6943FF23F3D
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0G2JXY8 | A0A0G2JXY8_RAT | Tg | 2720 | ||
A0A8I6AAP3 | A0A8I6AAP3_RAT | Tg | 243 | ||
A0A1W2Q6Q9 | A0A1W2Q6Q9_RAT | Tg | 134 | ||
G3V6V3 | G3V6V3_RAT | Tg | 2768 | ||
A0A8I5ZUP4 | A0A8I5ZUP4_RAT | Tg | 367 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 44 | in Ref. 4; AAA50379 | ||||
Sequence: L → V | ||||||
Sequence conflict | 678 | in Ref. 2; AAF34909 | ||||
Sequence: A → V | ||||||
Sequence conflict | 1492 | in Ref. 2; AAF34909 | ||||
Sequence: C → F | ||||||
Sequence conflict | 1732-1733 | in Ref. 2; AAF34909 | ||||
Sequence: CC → KS | ||||||
Sequence conflict | 1914 | in Ref. 5; CAA26183 | ||||
Sequence: L → F | ||||||
Sequence conflict | 2043 | in Ref. 5; CAA26183 | ||||
Sequence: R → A | ||||||
Sequence conflict | 2081 | in Ref. 5; CAA26183 | ||||
Sequence: Q → K | ||||||
Sequence conflict | 2126 | in Ref. 5; CAA26183 | ||||
Sequence: A → V | ||||||
Sequence conflict | 2153 | in Ref. 5; CAA26183 | ||||
Sequence: R → K | ||||||
Sequence conflict | 2169 | in Ref. 5; CAA26183 | ||||
Sequence: S → N | ||||||
Sequence conflict | 2611 | in Ref. 5; CAA26183 | ||||
Sequence: M → I | ||||||
Sequence conflict | 2658 | in Ref. 5; CAA26183 | ||||
Sequence: Q → H |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |