ID   TTHY_SMIMA              Reviewed;         149 AA.
AC   P49143; Q6LAP2; Q6LAP3;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Transthyretin;
DE   AltName: Full=Prealbumin;
DE   Flags: Precursor;
GN   Name=TTR;
OS   Sminthopsis macroura (Stripe-faced dunnart).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Dasyuromorphia; Dasyuridae; Sminthopsis.
OX   NCBI_TaxID=9302;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Choroid plexus;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 13-32.
RC   TISSUE=Kidney;
RX   PubMed=9208931; DOI=10.1111/j.1432-1033.1997.t01-1-00401.x;
RA   Aldred A.R., Prapunpoj P., Schreiber G.;
RT   "Evolution of shorter and more hydrophilic transthyretin N-termini by
RT   stepwise conversion of exon 2 into intron 1 sequences (shifting the 3'
RT   splice site of intron 1).";
RL   Eur. J. Biochem. 246:401-409(1997).
CC   -!- FUNCTION: Thyroid hormone-binding protein. Probably transports
CC       thyroxine from the bloodstream to the brain (By similarity).
CC       {ECO:0000250}.
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:0000250}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in the choroid plexus.
CC       {ECO:0000269|PubMed:7851414}.
CC   -!- SIMILARITY: Belongs to the transthyretin family. {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; U12518; AAA86055.1; -; mRNA.
DR   EMBL; X80998; CAA56925.1; -; mRNA.
DR   EMBL; X98221; CAA66881.1; -; Genomic_DNA.
DR   EMBL; X98222; CAA66882.1; -; Genomic_DNA.
DR   PIR; S67472; S67472.
DR   AlphaFoldDB; P49143; -.
DR   SMR; P49143; -.
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   2: Evidence at transcript 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_0000035766"
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;  16333 MW;  B355643FA1524B78 CRC64;
     MAFHSLLLLC LAGLVFLSEA GPVAHGAEDS KCPLMVKVLD SVRGSPAVNV DVKVFKKTEE
     QTWELFASGK TNNNGEIHEL TSDDQFGEGL YKVEFDTVSY WKTFGISPFH EYADVVFTAN
     DAGHRHYTIA AQLSPFSFST TAVVSNPKD