ID THBG_HUMAN Reviewed; 415 AA. AC P05543; D3DUX1; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 2. DT 24-JAN-2024, entry version 222. DE RecName: Full=Thyroxine-binding globulin; DE AltName: Full=Serpin A7; DE AltName: Full=T4-binding globulin; DE Flags: Precursor; GN Name=SERPINA7; Synonyms=TBG; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX PubMed=3094014; DOI=10.1073/pnas.83.20.7708; RA Flink I.L., Bayley T.J., Gustafson T.A., Markham B.E., Morkin E.; RT "Complete amino acid sequence of human thyroxine-binding globulin deduced RT from cloned DNA: close homology to the serine antiproteases."; RL Proc. Natl. Acad. Sci. U.S.A. 83:7708-7712(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8268226; DOI=10.1016/0167-4781(93)90013-4; RA Akbari M.T., Kapadi A., Farmer M.J., Fitch N.J.S., McCann K.P., RA Kordestani S., Flink I.L., Sheppard M.C., Ramsden D.B.; RT "The structure of the human thyroxine binding globulin (TBG) gene."; RL Biochim. Biophys. Acta 1216:446-454(1993). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8232304; DOI=10.1210/mend.7.8.8232304; RA Hayashi Y., Mori Y., Janssen O.E., Sunthornthepvarakul T., Weiss R.E., RA Takeda K., Weinberg M., Seo H., Bell G.I., Refetoff S.; RT "Human thyroxine-binding globulin gene: complete sequence and RT transcriptional regulation."; RL Mol. Endocrinol. 7:1049-1060(1993). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP PROTEIN SEQUENCE OF 21-40. RX PubMed=414747; DOI=10.1016/0006-291x(77)91135-4; RA Cheng S.-Y.; RT "Partial amino acid sequence of human thyroxine-binding globulin. Further RT evidence for a single polypeptide chain."; RL Biochem. Biophys. Res. Commun. 79:1212-1218(1977). RN [8] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-36 AND ASN-165. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., RA Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [9] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-36, AND STRUCTURE OF RP CARBOHYDRATES. RC TISSUE=Cerebrospinal fluid; RX PubMed=19838169; DOI=10.1038/nmeth.1392; RA Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., RA Larson G.; RT "Enrichment of glycopeptides for glycan structure and attachment site RT identification."; RL Nat. Methods 6:809-811(2009). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 39-415 IN COMPLEX WITH THYROXINE. RX PubMed=16938877; DOI=10.1073/pnas.0604080103; RA Zhou A., Wei Z., Read R.J., Carrell R.W.; RT "Structural mechanism for the carriage and release of thyroxine in the RT blood."; RL Proc. Natl. Acad. Sci. U.S.A. 103:13321-13326(2006). RN [12] RP REVIEW ON VARIANTS. RX PubMed=18407078; DOI=10.1016/1043-2760(92)90043-z; RA Janssen O.E., Bertenshaw R., Takeda K., Weiss R., Refetoff S.; RT "Molecular basis of inherited thyroxine-binding globulin defects."; RL Trends Endocrinol. Metab. 3:49-53(1992). RN [13] RP POLYMORPHISM, AND VARIANT PRO-247. RX PubMed=2155256; DOI=10.1210/jcem-70-3-804; RA Mori Y., Takeda K., Charbonneau M., Refetoff S.; RT "Replacement of Leu227 by Pro in thyroxine-binding globulin (TBG) is RT associated with complete TBG deficiency in three of eight families with RT this inherited defect."; RL J. Clin. Endocrinol. Metab. 70:804-809(1990). RN [14] RP POLYMORPHISM, AND VARIANT ASN-116. RX PubMed=2501669; DOI=10.1210/mend-3-3-575; RA Mori Y., Seino S., Takeda K., Flink I.L., Murata Y., Bell G.I., RA Refetoff S.; RT "A mutation causing reduced biological activity and stability of thyroxine- RT binding globulin probably as a result of abnormal glycosylation of the RT molecule."; RL Mol. Endocrinol. 3:575-579(1989). RN [15] RP POLYMORPHISM, AND VARIANT LEU-383. RX PubMed=1294376; DOI=10.1507/endocrj1954.39.577; RA Shirotani T., Kishikawa H., Wake N., Miyamura N., Hashimoto Y., RA Motoyoshi S., Yamaguchi K., Shichiri M.; RT "Thyroxine-binding globulin variant (TBG-Kumamoto): identification of a RT point mutation and genotype analysis of its family."; RL Endocrinol. Jpn. 39:577-584(1992). RN [16] RP POLYMORPHISM, AND VARIANT PRO-133. RX PubMed=1906047; DOI=10.1007/bf00204164; RA Janssen O.E., Takeda K., Refetoff S.; RT "Sequence of the variant thyroxine-binding globulin (TBG) in a Montreal RT family with partial TBG deficiency."; RL Hum. Genet. 87:119-122(1991). RN [17] RP POLYMORPHISM, AND VARIANT TYR-351. RX PubMed=1901689; RA Bertenshaw R., Takeda K., Refetoff S.; RT "Sequencing of the variant thyroxine-binding globulin (TBG)-Quebec reveals RT two nucleotide substitutions."; RL Am. J. Hum. Genet. 48:741-744(1991). RN [18] RP POLYMORPHISM, AND VARIANTS THR-43 AND PHE-303. RX PubMed=1515456; DOI=10.1016/0925-4439(92)90105-v; RA Bertenshaw R., Sarne D., Tornari J., Weinberg M., Refetoff S.; RT "Sequencing of the variant thyroxine-binding globulin (TBG)-San Diego RT reveals two nucleotide substitutions."; RL Biochim. Biophys. Acta 1139:307-310(1992). RN [19] RP VARIANT TBG-A THR-211. RX PubMed=2495303; DOI=10.1172/jci114021; RA Takeda K., Mori Y., Sobieszczyk S., Seo H., Dick M., Watson F., Flink I.L., RA Seino S., Bell G.I., Refetoff S.; RT "Sequence of the variant thyroxine-binding globulin of Australian RT aborigines. Only one of two amino acid replacements is responsible for its RT altered properties."; RL J. Clin. Invest. 83:1344-1348(1989). RN [20] RP VARIANT TBG-S ASN-191. RX PubMed=2115061; DOI=10.1007/bf03349576; RA Waltz M.R., Pullman T.N., Takeda K., Sobieszczyk P., Refetoff S.; RT "Molecular basis for the properties of the thyroxine-binding globulin-slow RT variant in American blacks."; RL J. Endocrinol. Invest. 13:343-349(1990). CC -!- FUNCTION: Major thyroid hormone transport protein in serum. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma. CC -!- POLYMORPHISM: Genetic variants in SERPINA7 influence the serum levels CC of thyroxine-binding globulin and define the thyroxine-binding globulin CC quantitative trait locus (TBGQTL) [MIM:300932]. Individuals with low or CC high serum levels of thyroxine-binding globulin show, respectively, CC reduced or elevated protein-bound iodine but are euthyroid and do not CC manifest major metabolic alterations (PubMed:1294376, PubMed:1515456, CC PubMed:1901689, PubMed:1906047, PubMed:2155256, PubMed:2501669). Two CC qualitative TBG variants occur in particular populations. TBG-A is CC found in 40% of Australian aborigines, it has reduced affinity for CC thyroxine and triiodothyroxine and increased susceptibility to CC inactivation by heat or acid (PubMed:2495303). TBG-S ('s' for slow CC shift on isoelectic focusing) is found in blacks, Eskimos, Melanesians, CC Polynesians and Indonesians, but not in Caucasians; TBG-S is slightly CC more thermolabile (PubMed:2115061). {ECO:0000269|PubMed:1294376, CC ECO:0000269|PubMed:1515456, ECO:0000269|PubMed:1901689, CC ECO:0000269|PubMed:1906047, ECO:0000269|PubMed:2115061, CC ECO:0000269|PubMed:2155256, ECO:0000269|PubMed:2495303, CC ECO:0000269|PubMed:2501669}. CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M14091; AAA60616.1; -; mRNA. DR EMBL; X64171; CAA45509.1; -; Genomic_DNA. DR EMBL; L13470; AAA16067.1; -; Genomic_DNA. DR EMBL; Z83850; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471120; EAX02747.1; -; Genomic_DNA. DR EMBL; CH471120; EAX02748.1; -; Genomic_DNA. DR EMBL; BC020747; AAH20747.1; -; mRNA. DR CCDS; CCDS14518.1; -. DR PIR; A47224; A47224. DR RefSeq; NP_000345.2; NM_000354.5. DR PDB; 2CEO; X-ray; 2.80 A; A/B=39-415. DR PDB; 2RIV; X-ray; 1.50 A; A=33-386, B=376-415. DR PDB; 2RIW; X-ray; 2.04 A; A=39-386, B=376-415. DR PDB; 2XN3; X-ray; 2.09 A; A=33-386, B=377-415. DR PDB; 2XN5; X-ray; 1.70 A; A=32-380, B=381-415. DR PDB; 2XN6; X-ray; 1.29 A; A=32-380, B=381-415. DR PDB; 2XN7; X-ray; 1.43 A; A=32-380, B=381-415. DR PDB; 4X30; X-ray; 1.55 A; A=21-415. DR PDB; 4YIA; X-ray; 1.58 A; A=1-386, B=382-415. DR PDBsum; 2CEO; -. DR PDBsum; 2RIV; -. DR PDBsum; 2RIW; -. DR PDBsum; 2XN3; -. DR PDBsum; 2XN5; -. DR PDBsum; 2XN6; -. DR PDBsum; 2XN7; -. DR PDBsum; 4X30; -. DR PDBsum; 4YIA; -. DR AlphaFoldDB; P05543; -. DR SMR; P05543; -. DR BioGRID; 112769; 10. DR IntAct; P05543; 4. DR STRING; 9606.ENSP00000329374; -. DR ChEMBL; CHEMBL3843; -. DR DrugBank; DB01629; 5-fluorouridine. DR DrugBank; DB11100; Allantoin. DR DrugBank; DB00023; Asparaginase Escherichia coli. DR DrugBank; DB00636; Clofibrate. DR DrugBank; DB00286; Conjugated estrogens. DR DrugBank; DB09130; Copper. DR DrugBank; DB01219; Dantrolene. DR DrugBank; DB01452; Diamorphine. DR DrugBank; DB09381; Esterified estrogens. DR DrugBank; DB00754; Ethotoin. DR DrugBank; DB08984; Etofenamate. DR DrugBank; DB00322; Floxuridine. DR DrugBank; DB00544; Fluorouracil. DR DrugBank; DB01320; Fosphenytoin. DR DrugBank; DB00695; Furosemide. DR DrugBank; DB01109; Heparin. DR DrugBank; DB00451; Levothyroxine. DR DrugBank; DB00279; Liothyronine. DR DrugBank; DB12425; Liothyronine I-131. DR DrugBank; DB01583; Liotrix. DR DrugBank; DB00939; Meclofenamic acid. DR DrugBank; DB00532; Mephenytoin. DR DrugBank; DB00648; Mitotane. DR DrugBank; DB13396; Neocitrullamon. DR DrugBank; DB00627; Niacin. DR DrugBank; DB05235; NRP409. DR DrugBank; DB00059; Pegaspargase. DR DrugBank; DB00252; Phenytoin. DR DrugBank; DB09317; Synthetic Conjugated Estrogens, A. DR DrugBank; DB09318; Synthetic Conjugated Estrogens, B. DR DrugBank; DB00675; Tamoxifen. DR DrugBank; DB09256; Tegafur. DR DrugBank; DB09100; Thyroid, porcine. DR MEROPS; I04.955; -. DR GlyConnect; 750; 13 N-Linked glycans (3 sites). DR GlyCosmos; P05543; 6 sites, 18 glycans. DR GlyGen; P05543; 5 sites, 17 N-linked glycans (3 sites), 1 O-linked glycan (1 site). DR iPTMnet; P05543; -. DR PhosphoSitePlus; P05543; -. DR BioMuta; SERPINA7; -. DR DMDM; 1351236; -. DR EPD; P05543; -. DR jPOST; P05543; -. DR MassIVE; P05543; -. DR MaxQB; P05543; -. DR PaxDb; 9606-ENSP00000329374; -. DR PeptideAtlas; P05543; -. DR ProteomicsDB; 51845; -. DR Pumba; P05543; -. DR Antibodypedia; 452; 476 antibodies from 33 providers. DR DNASU; 6906; -. DR Ensembl; ENST00000327674.8; ENSP00000329374.4; ENSG00000123561.15. DR Ensembl; ENST00000372563.2; ENSP00000361644.1; ENSG00000123561.15. DR GeneID; 6906; -. DR KEGG; hsa:6906; -. DR MANE-Select; ENST00000372563.2; ENSP00000361644.1; NM_000354.6; NP_000345.2. DR UCSC; uc004eme.3; human. DR AGR; HGNC:11583; -. DR CTD; 6906; -. DR DisGeNET; 6906; -. DR GeneCards; SERPINA7; -. DR HGNC; HGNC:11583; SERPINA7. DR HPA; ENSG00000123561; Tissue enriched (liver). DR MalaCards; SERPINA7; -. DR MIM; 300932; phenotype. DR MIM; 314200; gene. DR neXtProt; NX_P05543; -. DR OpenTargets; ENSG00000123561; -. DR Orphanet; 209893; NON RARE IN EUROPE: Congenital isolated thyroxine-binding globulin deficiency. DR PharmGKB; PA36347; -. DR VEuPathDB; HostDB:ENSG00000123561; -. DR eggNOG; KOG2392; Eukaryota. DR GeneTree; ENSGT00940000161113; -. DR HOGENOM; CLU_023330_2_1_1; -. DR InParanoid; P05543; -. DR OMA; CFKAQWA; -. DR OrthoDB; 3218836at2759; -. DR PhylomeDB; P05543; -. DR TreeFam; TF343201; -. DR PathwayCommons; P05543; -. DR SignaLink; P05543; -. DR BioGRID-ORCS; 6906; 11 hits in 762 CRISPR screens. DR EvolutionaryTrace; P05543; -. DR GenomeRNAi; 6906; -. DR Pharos; P05543; Tbio. DR PRO; PR:P05543; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; P05543; Protein. DR Bgee; ENSG00000123561; Expressed in liver and 49 other cell types or tissues. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central. DR GO; GO:0070327; P:thyroid hormone transport; IMP:UniProtKB. DR CDD; cd19555; serpinA7_TBG; 1. DR Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 1. DR Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 1. DR Gene3D; 2.10.310.10; Serpins superfamily; 1. DR InterPro; IPR023795; Serpin_CS. DR InterPro; IPR023796; Serpin_dom. DR InterPro; IPR000215; Serpin_fam. DR InterPro; IPR036186; Serpin_sf. DR InterPro; IPR042178; Serpin_sf_1. DR InterPro; IPR042185; Serpin_sf_2. DR PANTHER; PTHR11461; SERINE PROTEASE INHIBITOR, SERPIN; 1. DR PANTHER; PTHR11461:SF375; THYROXINE-BINDING GLOBULIN; 1. DR Pfam; PF00079; Serpin; 1. DR PRINTS; PR00780; LEUSERPINII. DR SMART; SM00093; SERPIN; 1. DR SUPFAM; SSF56574; Serpins; 1. DR PROSITE; PS00284; SERPIN; 1. DR Genevisible; P05543; HS. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Glycoprotein; Reference proteome; KW Secreted; Signal. FT SIGNAL 1..20 FT /evidence="ECO:0000269|PubMed:414747" FT CHAIN 21..415 FT /note="Thyroxine-binding globulin" FT /id="PRO_0000032436" FT BINDING 293 FT /ligand="thyroxine" FT /ligand_id="ChEBI:CHEBI:305790" FT /evidence="ECO:0000269|PubMed:16938877" FT BINDING 398 FT /ligand="thyroxine" FT /ligand_id="ChEBI:CHEBI:305790" FT /evidence="ECO:0000269|PubMed:16938877" FT CARBOHYD 36 FT /note="N-linked (GlcNAc...) (complex) asparagine" FT /evidence="ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19838169" FT CARBOHYD 99 FT /note="N-linked (GlcNAc...) asparagine" FT CARBOHYD 116 FT /note="N-linked (GlcNAc...) asparagine; in variant Gary" FT /evidence="ECO:0000305" FT CARBOHYD 165 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952" FT CARBOHYD 253 FT /note="N-linked (GlcNAc...) asparagine" FT VARIANT 43 FT /note="S -> T (associated with F-303 in San Diego; partial FT thyroxine-binding globulin deficiency; dbSNP:rs72554662)" FT /evidence="ECO:0000269|PubMed:1515456" FT /id="VAR_007102" FT VARIANT 116 FT /note="I -> N (gary; severe thyroxine-binding globulin FT deficiency; dbSNP:rs28933689)" FT /evidence="ECO:0000269|PubMed:2501669" FT /id="VAR_007103" FT VARIANT 133 FT /note="A -> P (montreal/TBG-M; partial thyroxine-binding FT globulin deficiency; dbSNP:rs28933688)" FT /evidence="ECO:0000269|PubMed:1906047" FT /id="VAR_007104" FT VARIANT 191 FT /note="D -> N (tBG-S/Slow; dbSNP:rs1050086)" FT /evidence="ECO:0000269|PubMed:2115061" FT /id="VAR_007105" FT VARIANT 211 FT /note="A -> T (tBG-A/Aborigine; dbSNP:rs2234036)" FT /evidence="ECO:0000269|PubMed:2495303" FT /id="VAR_007106" FT VARIANT 247 FT /note="L -> P (cD5; complete thyroxine-binding globulin FT deficiency; dbSNP:rs28937312)" FT /evidence="ECO:0000269|PubMed:2155256" FT /id="VAR_007107" FT VARIANT 303 FT /note="L -> F (associated with T-43 in San Diego; FT dbSNP:rs1804495)" FT /evidence="ECO:0000269|PubMed:1515456" FT /id="VAR_007108" FT VARIANT 351 FT /note="H -> Y (quebec; partial thyroxine-binding globulin FT deficiency; dbSNP:rs72554659)" FT /evidence="ECO:0000269|PubMed:1901689" FT /id="VAR_007109" FT VARIANT 383 FT /note="P -> L (kumamoto; partial thyroxine-binding globulin FT deficiency; dbSNP:rs72554658)" FT /evidence="ECO:0000269|PubMed:1294376" FT /id="VAR_007110" FT CONFLICT 30..31 FT /note="CH -> DS (in Ref. 7; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 38 FT /note="T -> S (in Ref. 7; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 197 FT /note="I -> T (in Ref. 1; AAA60616)" FT /evidence="ECO:0000305" FT HELIX 40..60 FT /evidence="ECO:0007829|PDB:2XN6" FT STRAND 66..68 FT /evidence="ECO:0007829|PDB:2XN6" FT HELIX 70..82 FT /evidence="ECO:0007829|PDB:2XN6" FT HELIX 86..95 FT /evidence="ECO:0007829|PDB:2XN6" FT TURN 100..102 FT /evidence="ECO:0007829|PDB:2XN6" FT HELIX 105..120 FT /evidence="ECO:0007829|PDB:2XN6" FT STRAND 126..137 FT /evidence="ECO:0007829|PDB:2XN6" FT HELIX 144..153 FT /evidence="ECO:0007829|PDB:2XN6" FT STRAND 156..161 FT /evidence="ECO:0007829|PDB:2XN6" FT HELIX 166..180 FT /evidence="ECO:0007829|PDB:2XN6" FT TURN 181..183 FT /evidence="ECO:0007829|PDB:2XN6" FT STRAND 198..212 FT /evidence="ECO:0007829|PDB:2XN6" FT HELIX 216..218 FT /evidence="ECO:0007829|PDB:2XN6" FT STRAND 220..228 FT /evidence="ECO:0007829|PDB:2XN6" FT STRAND 231..249 FT /evidence="ECO:0007829|PDB:2XN6" FT TURN 250..253 FT /evidence="ECO:0007829|PDB:2XN6" FT STRAND 254..272 FT /evidence="ECO:0007829|PDB:2XN6" FT HELIX 277..283 FT /evidence="ECO:0007829|PDB:2XN6" FT HELIX 286..295 FT /evidence="ECO:0007829|PDB:2XN6" FT STRAND 297..306 FT /evidence="ECO:0007829|PDB:2XN6" FT STRAND 308..315 FT /evidence="ECO:0007829|PDB:2XN6" FT HELIX 317..323 FT /evidence="ECO:0007829|PDB:2XN6" FT HELIX 327..329 FT /evidence="ECO:0007829|PDB:2XN6" FT TURN 336..338 FT /evidence="ECO:0007829|PDB:2XN6" FT STRAND 339..342 FT /evidence="ECO:0007829|PDB:4X30" FT STRAND 344..357 FT /evidence="ECO:0007829|PDB:2XN6" FT STRAND 359..374 FT /evidence="ECO:0007829|PDB:2XN6" FT STRAND 384..386 FT /evidence="ECO:0007829|PDB:2XN6" FT STRAND 391..397 FT /evidence="ECO:0007829|PDB:2XN6" FT TURN 398..401 FT /evidence="ECO:0007829|PDB:2XN6" FT STRAND 402..410 FT /evidence="ECO:0007829|PDB:2XN6" SQ SEQUENCE 415 AA; 46325 MW; 8B24EF8C7CEF8F0A CRC64; MSPFLYLVLL VLGLHATIHC ASPEGKVTAC HSSQPNATLY KMSSINADFA FNLYRRFTVE TPDKNIFFSP VSISAALVML SFGACCSTQT EIVETLGFNL TDTPMVEIQH GFQHLICSLN FPKKELELQI GNALFIGKHL KPLAKFLNDV KTLYETEVFS TDFSNISAAK QEINSHVEMQ TKGKVVGLIQ DLKPNTIMVL VNYIHFKAQW ANPFDPSKTE DSSSFLIDKT TTVQVPMMHQ MEQYYHLVDM ELNCTVLQMD YSKNALALFV LPKEGQMESV EAAMSSKTLK KWNRLLQKGW VDLFVPKFSI SATYDLGATL LKMGIQHAYS ENADFSGLTE DNGLKLSNAA HKAVLHIGEK GTEAAAVPEV ELSDQPENTF LHPIIQIDRS FMLLILERST RSILFLGKVV NPTEA //