ID   TTHY_MACGI              Reviewed;         149 AA.
AC   Q29616; Q9TRF3;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Transthyretin;
DE   AltName: Full=Prealbumin;
DE   Flags: Precursor;
GN   Name=TTR;
OS   Macropus giganteus (Eastern gray kangaroo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Diprotodontia; Macropodidae; Macropus.
OX   NCBI_TaxID=9317;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   TISSUE=Liver;
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).
RN   [2]
RP   PROTEIN SEQUENCE OF 23-41, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Liver;
RX   PubMed=8359020; DOI=10.1016/0305-0491(93)90235-w;
RA   Schreiber G., Pettersson T.M., Southwell B.R., Aldred A.R., Harms P.J.,
RA   Richardson S.J., Wettenhall R.E., Duan W., Nicol S.C.;
RT   "Transthyretin expression evolved more recently in liver than in brain.";
RL   Comp. Biochem. Physiol. 105B:317-325(1993).
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:0000269|PubMed:8359020}.
CC   -!- TISSUE SPECIFICITY: Detected in liver. {ECO:0000269|PubMed:8359020}.
CC   -!- SIMILARITY: Belongs to the transthyretin family. {ECO:0000305}.
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DR   EMBL; X97689; CAA66279.1; -; mRNA.
DR   EMBL; X97971; CAA66614.1; -; Genomic_DNA.
DR   EMBL; X98220; CAA66880.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q29616; -.
DR   SMR; Q29616; -.
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; Hormone; Secreted;
KW   Signal; Thyroid hormone; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:8359020"
FT   CHAIN           23..149
FT                   /note="Transthyretin"
FT                   /id="PRO_0000035758"
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"
FT   CONFLICT        40
FT                   /note="D -> L (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   149 AA;  16491 MW;  9DBB6E4C0EF91A00 CRC64;
     MAFHSLLLLC LAGLAFVSET AAVHHESEHS KCPLMVKVLD AVRGRPAVNV DVKVFKKTEE
     QTWELFAAGK TNDNGEIHEL TTDDKFGEGL YKVEFDTISY WKALGVSPFH EYADVVFTAN
     DAGHRHYTIA AQLSPYSFST TAIVSNPTE