| IED ID |
IndEnz0018001518 |
| Enzyme Type ID |
peroxidase001518 |
| Protein Name |
Thyroglobulin
|
| Gene Name |
TG |
| Organism |
Sus scrofa (Pig) |
| Taxonomic Lineage |
cellular organisms
Eukaryota
Opisthokonta
Metazoa
Eumetazoa
Bilateria
Deuterostomia
Chordata
Craniata
Vertebrata
Gnathostomata (jawed vertebrates)
Teleostomi
Euteleostomi
Sarcopterygii
Dipnotetrapodomorpha
Tetrapoda
Amniota
Mammalia
Theria
Eutheria
Boreoeutheria
Laurasiatheria
Artiodactyla
Suina
Suidae (pigs)
Sus
Sus scrofa (Pig)
|
| Enzyme Sequence |
MALALWVFALLGSACLVSANIFEYQVDAQPLRPCELQRERAFLKRADYVPQCAEDGSFQTVQCKKDGGSCWCVDADGREVPGSRQPGRPVACLSFCQLQKQQILLSSYINSTATSYLPQCQDSGAYAPVQCDVRREQCWCVDAEGMEVYGTRRLGRPARCPGSCEIRNRRLLHGVGDKSPPQCSADGTFLPVQCKFVNTTDMMFFDLVHSYNRFPDAFVTFSSFRSRFPEVSGYCHCADSQGRELAGTGLELLLDEIYDTVFAGLDLASSFTETTLYRILQRRFLAVQLVTSGRFRCPTKCEVERFAATSFGHPYVPSCGRDGEYQAGQCQQEGLCWCVDAQGQEIPGTRRPSEPLSCAEGQSCPSERRRALSRLHLGPSGYSGQRGSFLAAERGPVSQTVPSFAASCPLPLKELFVESGILQPVVQGQKKEVTAATESLLKEGLRGIFPSRELARLALQFTANPKRLQQNLFGGRFLANVGQFNLSGALGTRGTFNFSHFFQQLGLPGFQKRQALADPAKSLSVGLDSNPATEAPEALKMGVAMNKTVVGSFGFEVNLQENRNALTFLSSLLELPEFLLFLQHAISVPEDIARDLGDVMEMALSSQGCEQTPGSLFVPSCTAEGSYEDVQCFAGECWCVDARGRELAGSRARGGRPRCPTACEKQRERMQSLLGRQPAGSSVFVPSCTREGHFLPVQCFSSDCYCVDADGQPIPGTRTAPGEPKQCPTPCQLQAEQAFLGTVRGLISNPSEPPVLSSIYIPQCSASGQWRRVQCDGPPEQAFEWYERWGAQSRSGQELTPAELLMKIMSYREAASGSFRLFIQNLYEAGQQGIFPGLARYSSLQDVPLAVLEGNLTQATGNILLEPYLFWQILNGQLPRYPGPYSDFSAPLAHLDLRSCWCVDEAGRKLEGTQTEPSKVPACPGSCEEVKLRVLQFIKEAEEIVMVSNSSQFPLGESFLAAKGIRLTDEELALPPLSPSRETFLEKFLSGSDYAIRLAAQSTFSFYQRRRVALSDAPRTSGPLQPYPYVPQCDALGSWEPVQCHAATGHCWCVDGEGAYLPASLAARSPQVLQCPTPCETSRVRGLLSAWKQAGSQVRPSPKDLFIPACTETGEFARLQASEASTWCVDPASGEAMPPGTNSSAPCPGLCEVLQRGVPSRRASPGTTPACRAEDGGFAPVQCDPAQGSCWCVLGSGEEVPGTRVAGSQPACERPQLWQTIQTRGQFQLQLPPGKVCSADYAGLLPTFQVVILDELTARGFCRIQVTTARTPVSIPVCDDSTVRVGCLSLDRLGVNVTWTLRLEDAPPASLPDLRDIEEALAGKDLVGRFADLIQSGTFQLHLDSRTFPADPSIHFLQGNSLGTSPRTRFGCVEGSRQVPATSNTSQDPLGCVRCPEGSYFQEEQCIPCPAGFYQEQTGSLACAPCPAGTTTTSVGAFSQTHCVTACQRDEAGLQCDQDGQYRASQRDRASGKAFCVDSEGRRLPWSETQAPLVDAQCLMMRKFEKLPESKVIFTADVAVLGSIVPDSESSLMQCLADCARDEACSFLTVSLEGSEGSCDFYAWTSDNIACTSSGQEEDALGTSKATSLGSLTCQVKVRPGDGVAPAVYLKKGQEFATIGQKRFEQTGFQNALSGLYSPVVFSASGASLTEAHLFCLLACDRDSCCDGFILTQVQGGPIICGLLSSPDVLLCHVRDWRDPSEAQADATCPGVTYDQDSRQGTLRLGGQEFKSLTPREGARDTFTSFQQVYLWKDSDMGSRSESMGCRRDMQPRPESPEETDLTAELFSPVDLNQVIVSENRSLPSQQHRLFKHLFSLQQAHLWCLSRCVQEPSFCQLAEITDSSPLYLTCTLYPEAQVCDDVMEASPRGCRRILPRRPNALFQRRVVLQDRVKNFYTRLPFQKLTGLSIRHKVPMADKAISSGFFECERLCDVDPCCTGFGFLNVSQLKGGEVTCLTLNSLGLQTCSEENGGSWRLLACGSPDTEVRTYPFGWYQKPAVQNDAPSFCPSAALPPVPEKVALDSWQPLPPSSVVVDPSIRNFDVAHISTAAVGDFSAARERCLLECSRHQACLVTTLQTRPGAVRCMFYADTQSCTHSLQAQNCQLLLREEATHIYRKPDIPLPGLGSSAPTVTIATHGQLLGTSQAIQLGASWKQVDQFLGVPYAAPPLAESRFRAPEPLNWTGTWDATKPRASCWQPGIRPATAPGVSEDCLYLSVFVPQSLTPNSSVLVFFHNGAEGPLAMAVDGSFLAAVGNLIVVTASYRTGVFGFLSSGSSEVSGNWGLLDQVAALTWVQTHIGVFGGDPRRVALAADRGGADVAGIHLLTSRATNSRLFRRAVLMGGSVLSPAAVIRPDRAQQQAAALAKEVGCPPRPSQKWYPASAGACQPPNDAQMQLLAVSGPFHYWGPVVDGQLLREAPARALQRPPRAKLDLLIGSSQDDGLIDRAKAVKRFEESQGRTSSKTAFYQALQNSLGGEAGDPGVQAAATWYYSLEHDTDDYASFSRALEAATRDYFIICPVIDMASHWARTARGNVFMYHAPESYSHGSLELLADVRYAFGLPFYPAYEGQFTQEEKSLSLKIMQYFSNFVRSGNPNYPHEFSRKAPEFAAPWPDFVPGDGAESYKELSVLLPNRQGLKKADCSFWSKYILSLKASADEAEDGPLAESEEEDRPGLTEDLLGLPELASKSYSK |
| Enzyme Length |
2692 |
| Uniprot Accession Number |
F1RRV3 |
| Absorption |
|
| Active Site |
|
| Activity Regulation |
|
| Binding Site |
|
| Calcium Binding |
|
| catalytic Activity |
|
| DNA Binding |
|
| EC Number |
|
| Enzyme Function |
FUNCTION: Acts as a substrate for the production of iodinated thyroid hormones thyroxine (T4) and triiodothyronine (T3) (PubMed:7021557). The synthesis of T3 and T4 involves iodination of selected tyrosine residues of TG/thyroglobulin followed by their oxidative coupling (PubMed:7021557). 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). {ECO:0000250|UniProtKB:O08710, ECO:0000250|UniProtKB:P01266, ECO:0000269|PubMed:7021557}. |
| Temperature Dependency |
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| PH Dependency |
|
| Pathway |
|
| nucleotide Binding |
|
| Features |
Chain (1); Disulfide bond (54); Domain (11); Glycosylation (15); Modified residue (36); Region (2); Repeat (8); Sequence conflict (30); Signal peptide (1) |
| Keywords |
Direct protein sequencing;Disulfide bond;Glycoprotein;Hormone;Iodination;Reference proteome;Repeat;Secreted;Signal;Sulfation;Thyroid hormone;Thyroid hormones biosynthesis |
| Interact With |
|
| Induction |
|
| Subcellular Location |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12387814}. Note=Secreted into the follicular lumina of the thyroid (PubMed:12387814). Localizes to colloid globules, a structure formed in the thyroid follicle lumen consisting of cross-linked TG arranged in concentric layers (By similarity). {ECO:0000250|UniProtKB:P01266, ECO:0000269|PubMed:12387814}. |
| Modified Residue |
MOD_RES 24; /note=Iodotyrosine; alternate; /evidence=ECO:0000250|UniProtKB:P01266; MOD_RES 24; /note=Sulfotyrosine; alternate; /evidence=ECO:0000269|PubMed:12387814; MOD_RES 24; /note=Thyroxine; alternate; /evidence=ECO:0000250|UniProtKB:P01266; MOD_RES 24; /note=Triiodothyronine; alternate; /evidence=ECO:0000250|UniProtKB:P01266; MOD_RES 108; /note=Iodotyrosine; /evidence=ECO:0000250|UniProtKB:P01266; MOD_RES 149; /note=Diiodotyrosine; alternate; /evidence=ECO:0000250|UniProtKB:P01266; MOD_RES 149; /note=Iodotyrosine; alternate; /evidence=ECO:0000250|UniProtKB:P01266; MOD_RES 234; /note=Iodotyrosine; /evidence=ECO:0000250|UniProtKB:P01266; MOD_RES 258; /note=Iodotyrosine; /evidence=ECO:0000250|UniProtKB:P01266; MOD_RES 705; /note=Diiodotyrosine; alternate; /evidence=ECO:0000250|UniProtKB:P01266; MOD_RES 705; /note=Iodotyrosine; alternate; /evidence=ECO:0000250|UniProtKB:P01266; MOD_RES 705; /note=Thyroxine; alternate; /evidence=ECO:0000250|UniProtKB:P01266; MOD_RES 705; /note=Triiodothyronine; alternate; /evidence=ECO:0000250|UniProtKB:P01266; MOD_RES 786; /note=Iodotyrosine; /evidence=ECO:0000250|UniProtKB:P01266; MOD_RES 868; /note=Diiodotyrosine; alternate; /evidence=ECO:0000250|UniProtKB:P01266; MOD_RES 868; /note=Iodotyrosine; alternate; /evidence=ECO:0000250|UniProtKB:P01266; MOD_RES 885; /note=Diiodotyrosine; /evidence=ECO:0000250|UniProtKB:P01266; MOD_RES 994; /note=Diiodotyrosine; alternate; /evidence=ECO:0000250|UniProtKB:P01266; MOD_RES 994; /note=Iodotyrosine; alternate; /evidence=ECO:0000250|UniProtKB:P01266; MOD_RES 1241; /note=Iodotyrosine; /evidence=ECO:0000250|UniProtKB:P01266; MOD_RES 1241; /note=Thyroxine; /evidence=ECO:0000250|UniProtKB:P01266; MOD_RES 1400; /note=Diiodotyrosine; alternate; /evidence=ECO:0000250|UniProtKB:P01266; MOD_RES 1400; /note=Iodotyrosine; alternate; /evidence=ECO:0000250|UniProtKB:P01266; MOD_RES 2115; /note=Iodotyrosine; /evidence=ECO:0000250|UniProtKB:P01266; MOD_RES 2467; /note=Thyroxine; /evidence=ECO:0000250|UniProtKB:P01266; MOD_RES 2500; /note=Diiodotyrosine; alternate; /evidence=ECO:0000250|UniProtKB:P01266; MOD_RES 2500; /note=Iodotyrosine; alternate; /evidence=ECO:0000250|UniProtKB:P01266; MOD_RES 2500; /note=Thyroxine; alternate; /evidence=ECO:0000250|UniProtKB:P01266; MOD_RES 2500; /note=Triiodothyronine; alternate; /evidence=ECO:0000250|UniProtKB:P01266; MOD_RES 2514; /note=Iodotyrosine; /evidence=ECO:0000250|UniProtKB:P01266; MOD_RES 2544; /note=Iodotyrosine; /evidence=ECO:0000250|UniProtKB:P01266; MOD_RES 2624; /note=Diiodotyrosine; /evidence=ECO:0000250|UniProtKB:P01266; MOD_RES 2690; /note=Diiodotyrosine; alternate; /evidence=ECO:0000250|UniProtKB:P01266; MOD_RES 2690; /note=Iodotyrosine; alternate; /evidence=ECO:0000250|UniProtKB:P01266; MOD_RES 2690; /note=Thyroxine; alternate; /evidence=ECO:0000250|UniProtKB:P01266; MOD_RES 2690; /note=Triiodothyronine; alternate; /evidence=ECO:0000250|UniProtKB:P01266 |
| Post Translational Modification |
PTM: Iodinated on tyrosine residues by TPO (PubMed:12325367). There are 4 pairs of iodinated tyrosines used for coupling: acceptor Tyr-24 is coupled to donor Tyr-149 or Tyr-234, acceptor Tyr-2500 is coupled to donor Tyr-2467, acceptor Tyr-2690 in monomer 1 is coupled to donor Tyr-2690 in monomer 2 and acceptor Tyr-1241 in monomer 1 is coupled to donor Tyr-108 in monomer 2 (By similarity). {ECO:0000250|UniProtKB:P01266, ECO:0000269|PubMed:12325367}.; PTM: Sulfated tyrosines are desulfated during iodination. {ECO:0000250|UniProtKB:P01266}.; PTM: Undergoes sequential proteolysis by cathepsins to release thyroxine (T4) and triiodothyronine (T3) hormones (By similarity). In the thyroid follicle lumen, cross-linked TG (storage form) is solubilized by limited proteolysis mediated by cathepsins CTSB and/or CTSL (By similarity). Partially cleaved TG is further processed by CTSK/cathepsin K and/or CTSL resulting in the release of T4 (PubMed:11082042). Following endocytosis, further processing occurs leading to the release of T3 and more T4 hormones (By similarity). {ECO:0000250|UniProtKB:O08710, ECO:0000269|PubMed:11082042}. |
| Signal Peptide |
SIGNAL 1..19; /evidence=ECO:0000269|PubMed:12387814 |
| Structure 3D |
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| Cross Reference PDB |
- |
| Mapped Pubmed ID |
- |
| Motif |
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| Gene Encoded By |
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| Mass |
293,030 |
| Kinetics |
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| Metal Binding |
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| Rhea ID |
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| Cross Reference Brenda |
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