THBG_RAT
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 03-AUG-2022, entry version 130.
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};
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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 GlyGen; P35577; 6 sites.
DR PaxDb; P35577; -.
DR UCSC; RGD:619833; rat.
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 Genevisible; P35577; RN.
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:0007568; P:aging; IEP:RGD.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
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; -; 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 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