ID   THBG_RAT                Reviewed;         418 AA.
AC   P35577;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 2.
DT   24-JAN-2024, entry version 135.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7988464; DOI=10.1210/endo.135.6.7988464;
RA   Tani Y., Mori Y., Miura Y., Okamoto H., Inagaki A., Saito H., Oiso Y.;
RT   "Molecular cloning of the rat thyroxine-binding globulin gene and analysis
RT   of its promoter activity.";
RL   Endocrinology 135:2731-2736(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 10-418, AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Liver;
RX   PubMed=1903654; DOI=10.1021/bi00236a012;
RA   Imamura S., Mori Y., Murata Y., Yamamori I., Miura Y., Oiso Y., Seo H.,
RA   Matsui N., Refetoff S.;
RT   "Molecular cloning and primary structure of rat thyroxine-binding
RT   globulin.";
RL   Biochemistry 30:5406-5411(1991).
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   -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA42205.1; Type=Erroneous initiation; Evidence={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; M63991; AAA42205.1; ALT_INIT; mRNA.
DR   PIR; A39567; A39567.
DR   AlphaFoldDB; P35577; -.
DR   SMR; P35577; -.
DR   STRING; 10116.ENSRNOP00000014739; -.
DR   MEROPS; I04.955; -.
DR   GlyCosmos; P35577; 6 sites, No reported glycans.
DR   GlyGen; P35577; 6 sites.
DR   PhosphoSitePlus; P35577; -.
DR   PaxDb; 10116-ENSRNOP00000014739; -.
DR   UCSC; RGD:619833; rat.
DR   AGR; RGD:619833; -.
DR   RGD; 619833; Serpina7.
DR   eggNOG; KOG2392; Eukaryota.
DR   HOGENOM; CLU_023330_2_1_1; -.
DR   InParanoid; P35577; -.
DR   PhylomeDB; P35577; -.
DR   PRO; PR:P35577; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0042562; F:hormone binding; IDA:RGD.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0015349; F:thyroid hormone transmembrane transporter activity; TAS:RGD.
DR   GO; GO:0009791; P:post-embryonic development; IDA:RGD.
DR   GO; GO:0051412; P:response to corticosterone; IEP:RGD.
DR   GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR   GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR   GO; GO:0034695; P:response to prostaglandin E; IEP:RGD.
DR   GO; GO:0048545; P:response to steroid hormone; IEP:RGD.
DR   GO; GO:0033189; P:response to vitamin A; IDA:RGD.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IDA:RGD.
DR   GO; GO:0070327; P:thyroid hormone transport; ISO:RGD.
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   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; Serpins; 1.
DR   PROSITE; PS00284; SERPIN; 1.
DR   Genevisible; P35577; RN.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..20
FT   CHAIN           21..418
FT                   /note="Thyroxine-binding globulin"
FT                   /id="PRO_0000032440"
FT   BINDING         296
FT                   /ligand="thyroxine"
FT                   /ligand_id="ChEBI:CHEBI:305790"
FT                   /evidence="ECO:0000250"
FT   BINDING         401
FT                   /ligand="thyroxine"
FT                   /ligand_id="ChEBI:CHEBI:305790"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        24
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        39
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        168
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        227
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        256
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   418 AA;  46938 MW;  3B1984814A388D19 CRC64;
     MSMFFYLFLL VLGLQATIHC APHNSSEGKV TTCHLPQQNA TLYKMPSINA DFAFRLYRKL
     SVENPDLNIF FSPVSISAAL AMLSFGSGSS TQTQILEVLG FNLTDTPVKE LQQGFQHLIC
     SLNFPNNELE LQMGNAVFIG QQLKPLAKFL DDVKTLYETE VFSTDFSNVS AAQHEINSYV
     EKQTKGKIVG LIQDLKLNII MILVNYIHFK AQWANPFRVS KTEESSNFSV DKSTTVQVPM
     MHQLEQYYHY VDVELNCTVL QMDYSANALA LFVLPKEGHM EWVEAAMSSK TLKKWNHLLQ
     KGWVELFVPK FSISATYDLG STLQKMGMRD AFAESADFPG ITKDNGLKLS YAFHKAVLHI
     GEEGTKEGAS PEAGSLDQPE VAPLHAVIRL DRTFLLMILE KRTRSVLFLG KVVDPTKE
//