THBG_HUMAN
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 03-AUG-2022, entry version 214.
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}.
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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; 9.
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; DB08899; Enzalutamide.
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 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; P05543; -.
DR PeptideAtlas; P05543; -.
DR PRIDE; P05543; -.
DR ProteomicsDB; 51845; -.
DR Antibodypedia; 452; 453 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 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; 1124079at2759; -.
DR PhylomeDB; P05543; -.
DR TreeFam; TF343201; -.
DR PathwayCommons; P05543; -.
DR SignaLink; P05543; -.
DR BioGRID-ORCS; 6906; 11 hits in 688 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 tissues.
DR Genevisible; P05543; HS.
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:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:0070327; P:thyroid hormone transport; IMP:UniProtKB.
DR Gene3D; 2.30.39.10; -; 1.
DR Gene3D; 3.30.497.10; -; 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; PTHR11461; 1.
DR Pfam; PF00079; Serpin; 1.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; SSF56574; 1.
DR PROSITE; PS00284; SERPIN; 1.
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
