ID   TTHY_TILRU              Reviewed;         150 AA.
AC   P30623;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Transthyretin;
DE   AltName: Full=Prealbumin;
DE   AltName: Full=TBPA;
DE   Flags: Precursor;
GN   Name=TTR;
OS   Tiliqua rugosa (Shingleback lizard) (Trachydosaurus rugosus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Scinciformata; Scincidae;
OC   Egerniinae; Tiliqua.
OX   NCBI_TaxID=8527;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP   FUNCTION, INTERACTION WITH RBP4, AND 3D-STRUCTURE MODELING.
RC   TISSUE=Brain;
RX   PubMed=8238627; DOI=10.1152/ajpregu.1993.265.5.r982;
RA   Achen M.G., Duan W., Pettersson T.M., Harms P.J., Richardson S.J.,
RA   Lawrence M.C., Wettenhall R.E.H., Aldred A.R., Schreiber G.;
RT   "Transthyretin gene expression in choroid plexus first evolved in
RT   reptiles.";
RL   Am. J. Physiol. 265:R982-R989(1993).
CC   -!- FUNCTION: Thyroid hormone-binding protein. Probably transports
CC       thyroxine from the bloodstream to the brain.
CC       {ECO:0000269|PubMed:8238627}.
CC   -!- SUBUNIT: Homotetramer. Dimer of dimers. In the homotetramer, subunits
CC       assemble around a central channel that can accommodate two ligand
CC       molecules (By similarity). Interacts with RBP4. {ECO:0000250,
CC       ECO:0000269|PubMed:8238627}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8238627}.
CC   -!- TISSUE SPECIFICITY: Detected in choroid plexus (at protein level).
CC       Detected in choroid plexus. {ECO:0000269|PubMed:8238627}.
CC   -!- DOMAIN: The N-terminus strongly influences thyroid hormone-binding
CC       properties. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the transthyretin family. {ECO:0000305}.
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DR   EMBL; X66697; CAA47238.1; -; mRNA.
DR   EMBL; M97509; AAA49620.1; -; mRNA.
DR   PIR; I51367; I51367.
DR   PIR; I51375; S25531.
DR   AlphaFoldDB; P30623; -.
DR   SMR; P30623; -.
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   Hormone; Secreted; Signal; Thyroid hormone; Transport.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..150
FT                   /note="Transthyretin"
FT                   /id="PRO_0000035770"
FT   BINDING         38
FT                   /ligand="L-thyroxine"
FT                   /ligand_id="ChEBI:CHEBI:58448"
FT                   /evidence="ECO:0000250"
FT   BINDING         77
FT                   /ligand="L-thyroxine"
FT                   /ligand_id="ChEBI:CHEBI:58448"
FT                   /evidence="ECO:0000250"
FT   BINDING         138..142
FT                   /ligand="L-thyroxine"
FT                   /ligand_id="ChEBI:CHEBI:58448"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   150 AA;  16343 MW;  6C988E00949112EE CRC64;
     MGSSSLLLVC LAGMVYLTEA APLVSHGSID SKCPLMVKVL DAVRGRPATS IAVKVSKMSE
     EGDWKEFANG KTNEFGEIHE LTTDEQFVQG LYKVEFDTSS YWKALGVSPF HEYADVVFSA
     NDSGHRHYTI AALLSPFSYS TTAVVSDPKE