ID   TTHY_PETBR              Reviewed;         149 AA.
AC   P49142;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Transthyretin;
DE   AltName: Full=Prealbumin;
DE   Flags: Precursor;
GN   Name=TTR;
OS   Petaurus breviceps (Australian sugar glider).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Diprotodontia; Petauridae; Petaurus.
OX   NCBI_TaxID=34899;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Liver;
RX   PubMed=7851414; DOI=10.1111/j.1432-1033.1995.tb20402.x;
RA   Duan W., Richardson S.J., Babon J.J., Heyes R.J., Southwell B.R.,
RA   Harms P.J., Wettenhall R.E.H., Dziegielewska K.M., Selwood L.,
RA   Bradley A.J., Brack C.M., Schreiber G.;
RT   "Evolution of transthyretin in marsupials.";
RL   Eur. J. Biochem. 227:396-406(1995).
CC   -!- FUNCTION: Thyroid hormone-binding protein. Probably transports
CC       thyroxine from the bloodstream to the brain.
CC       {ECO:0000269|PubMed:7851414}.
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:7851414}.
CC   -!- TISSUE SPECIFICITY: Detected in plasma (at protein level). Detected in
CC       liver. {ECO:0000269|PubMed:7851414}.
CC   -!- SIMILARITY: Belongs to the transthyretin family. {ECO:0000305}.
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DR   EMBL; U12517; AAA86054.1; -; mRNA.
DR   EMBL; X80999; CAA56926.1; -; mRNA.
DR   PIR; S67471; S67471.
DR   AlphaFoldDB; P49142; -.
DR   SMR; P49142; -.
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   Gamma-carboxyglutamic acid; Hormone; Secreted; Signal; Thyroid hormone;
KW   Transport.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..149
FT                   /note="Transthyretin"
FT                   /id="PRO_0000035762"
FT   BINDING         37
FT                   /ligand="L-thyroxine"
FT                   /ligand_id="ChEBI:CHEBI:58448"
FT                   /evidence="ECO:0000250"
FT   BINDING         76
FT                   /ligand="L-thyroxine"
FT                   /ligand_id="ChEBI:CHEBI:58448"
FT                   /evidence="ECO:0000250"
FT   BINDING         137..141
FT                   /ligand="L-thyroxine"
FT                   /ligand_id="ChEBI:CHEBI:58448"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         64
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P02766"
SQ   SEQUENCE   149 AA;  16325 MW;  24793ED63E7C7C2D CRC64;
     MAFHSLLLLC LAGLLFVSEA GPVAHGGEDS KCPLMVKVLD AVRGRPAVNV DVKVFKKTEK
     QTWELFASGK TNDNGEIHEL TSDDKFGEGL YKVEFDTISY WKALGVSPFH EYADVVFTAN
     DAGHRHYTIA AQLSPYSFST TAIVSNPTE