ID   TTHY_SORAR              Reviewed;         147 AA.
AC   O46654;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Transthyretin;
DE   AltName: Full=Prealbumin;
DE   Flags: Precursor;
GN   Name=TTR;
OS   Sorex araneus (Eurasian common shrew) (European shrew).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Soricidae; Soricinae; Sorex.
OX   NCBI_TaxID=42254;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-25, FUNCTION,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Liver;
RX   PubMed=10908640; DOI=10.1093/oxfordjournals.molbev.a026403;
RA   Prapunpoj P., Richardson S.J., Fumagalli L., Schreiber G.;
RT   "The evolution of the thyroid hormone distributor protein transthyretin in
RT   the order insectivora, class mammalia.";
RL   Mol. Biol. Evol. 17:1199-1209(2000).
CC   -!- FUNCTION: Thyroid hormone-binding protein. Probably transports
CC       thyroxine from the bloodstream to the brain.
CC       {ECO:0000269|PubMed:10908640}.
CC   -!- SUBUNIT: Homotetramer. Dimer of dimers. In the homotetramer, subunits
CC       assemble around a central channel that can accommodate two ligand
CC       molecules. Interacts with RBP4 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10908640}.
CC   -!- TISSUE SPECIFICITY: Detected in serum (at protein level). Detected in
CC       liver. {ECO:0000269|PubMed:10908640}.
CC   -!- SIMILARITY: Belongs to the transthyretin family. {ECO:0000305}.
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DR   EMBL; AJ223149; CAA11130.1; -; mRNA.
DR   RefSeq; NP_001267607.1; NM_001280678.1.
DR   AlphaFoldDB; O46654; -.
DR   SMR; O46654; -.
DR   GeneID; 101549714; -.
DR   KEGG; sara:101549714; -.
DR   CTD; 7276; -.
DR   HOGENOM; CLU_115536_2_0_1; -.
DR   OrthoDB; 1453185at2759; -.
DR   TreeFam; TF300210; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0070324; F:thyroid hormone binding; IEA:InterPro.
DR   GO; GO:0042572; P:retinol metabolic process; IEA:InterPro.
DR   GO; GO:0070327; P:thyroid hormone transport; IEA:InterPro.
DR   Gene3D; 2.60.40.180; -; 1.
DR   InterPro; IPR023418; Thyroxine_BS.
DR   InterPro; IPR030178; Transthyretin.
DR   InterPro; IPR000895; Transthyretin/HIU_hydrolase.
DR   InterPro; IPR023416; Transthyretin/HIU_hydrolase_d.
DR   InterPro; IPR036817; Transthyretin/HIU_hydrolase_sf.
DR   InterPro; IPR023419; Transthyretin_CS.
DR   PANTHER; PTHR10395; PTHR10395; 1.
DR   PANTHER; PTHR10395:SF12; PTHR10395:SF12; 1.
DR   Pfam; PF00576; Transthyretin; 1.
DR   PRINTS; PR00189; TRNSTHYRETIN.
DR   SMART; SM00095; TR_THY; 1.
DR   SUPFAM; SSF49472; SSF49472; 1.
DR   PROSITE; PS00768; TRANSTHYRETIN_1; 1.
DR   PROSITE; PS00769; TRANSTHYRETIN_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Gamma-carboxyglutamic acid; Glycoprotein;
KW   Hormone; Secreted; Signal; Thyroid hormone; Transport.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:10908640"
FT   CHAIN           21..147
FT                   /note="Transthyretin"
FT                   /id="PRO_0000035767"
FT   BINDING         35
FT                   /ligand="L-thyroxine"
FT                   /ligand_id="ChEBI:CHEBI:58448"
FT                   /evidence="ECO:0000250"
FT   BINDING         74
FT                   /ligand="L-thyroxine"
FT                   /ligand_id="ChEBI:CHEBI:58448"
FT                   /evidence="ECO:0000250"
FT   BINDING         135..139
FT                   /ligand="L-thyroxine"
FT                   /ligand_id="ChEBI:CHEBI:58448"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         62
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P02766"
FT   CARBOHYD        118
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   147 AA;  15979 MW;  1CA146DF5E9BC34B CRC64;
     MASRRLLLLC LAGLVLVTEA GPTGTGQSKC PLMVKVLDAV QGSPAVNVAV RVFKKAADET
     WEPFASGKTS EFGELHGLTT DEKFVEGIIK VELDTKTYWK ALGISPFHEY VEVVFHANDS
     GKRRYTIAAL LSPYSYSTTA LVSDPKE