ID   THBG_PIG                Reviewed;         412 AA.
AC   Q9TT35; Q5QGZ0;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 2.
DT   03-AUG-2022, entry version 106.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11850119; DOI=10.1016/s0303-7207(01)00679-7;
RA   Janssen O.E., Lahner H., Grasberger H., Spring S.A., Saller B., Mann K.,
RA   Refetoff S., Einspanier R.;
RT   "Characterization and primary structures of bovine and porcine thyroxine-
RT   binding globulin.";
RL   Mol. Cell. Endocrinol. 186:27-35(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ASN-245.
RX   PubMed=15385420; DOI=10.1095/biolreprod.104.031922;
RA   Nonneman D., Rohrer G.A., Wise T.H., Lunstra D.D., Ford J.J.;
RT   "A variant of porcine thyroxine-binding globulin has reduced affinity for
RT   thyroxine and is associated with testis size.";
RL   Biol. Reprod. 72:214-220(2005).
CC   -!- FUNCTION: Major thyroid hormone transport protein in serum.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
CC   -!- POLYMORPHISM: The allele with Asn-245 has a significantly greater
CC       affinity for thyroxine than the His-245 allele found in Meishan boars.
CC       This polymorphism is a candidate for the causative variation affecting
CC       testis size in boars. {ECO:0000269|PubMed:15385420}.
CC   -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR   EMBL; AF204929; AAF15302.1; -; mRNA.
DR   EMBL; AY550250; AAT40589.1; -; Genomic_DNA.
DR   RefSeq; NP_999223.1; NM_214058.1.
DR   AlphaFoldDB; Q9TT35; -.
DR   SMR; Q9TT35; -.
DR   STRING; 9823.ENSSSCP00000013341; -.
DR   MEROPS; I04.955; -.
DR   PaxDb; Q9TT35; -.
DR   PeptideAtlas; Q9TT35; -.
DR   GeneID; 397125; -.
DR   KEGG; ssc:397125; -.
DR   CTD; 6906; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   InParanoid; Q9TT35; -.
DR   OrthoDB; 1124079at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Glycoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..412
FT                   /note="Thyroxine-binding globulin"
FT                   /id="PRO_0000032439"
FT   BINDING         292
FT                   /ligand="thyroxine"
FT                   /ligand_id="ChEBI:CHEBI:305790"
FT                   /evidence="ECO:0000250"
FT   BINDING         395
FT                   /ligand="thyroxine"
FT                   /ligand_id="ChEBI:CHEBI:305790"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        20
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        35
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        164
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        252
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         245
FT                   /note="H -> N"
FT                   /evidence="ECO:0000269|PubMed:15385420"
FT   CONFLICT        223..224
FT                   /note="SF -> RL (in Ref. 2; AAT40589)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   412 AA;  46215 MW;  C32B797BA27DAF11 CRC64;
     MPLFLYMVLL VLGIHCVQPN ISEGKVTSCL SPQQNATLHK MSSINADFAF NLYRRFAVET
     PDQNIFFSPV SISAALAMLS FGACSSTQTQ ILESLGYNLT EMPMAEIQQG FQHLICSLNF
     PKKELELQMG NALFIEKQLK PLAKFLDDVK NLYETEVFST DFSNVSAAQQ ELNSHVERQT
     KGKIVGLIPD LKPNTIMVLV NYICFKAQWA NPFDPSKTEE GSSFLVDKTT TVQVPMMHQM
     EQYYHLVDTE LNCTVLQMDY SKNALALFVL PNEGQMEWVE GAMSSKILKK WNRLLQKGWI
     DLFVPKFSMS ATYDLGDILL KMGIQDAFAD NADFSGLTKD NGLKLSNAAH KAVLNIGEKG
     TEAIPEVTFL NQPKITLLHP IIQFDRSFLL LILEKSTRSI LFLGKVVDPT EA