ID   TTHY_RABIT              Reviewed;         127 AA.
AC   P07489;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Transthyretin;
DE   AltName: Full=Prealbumin;
GN   Name=TTR;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=3922975; DOI=10.1016/s0021-9258(18)88997-9;
RA   Sundelin J., Melhus H., Das S., Eriksson U., Lind P., Traegaardh L.,
RA   Peterson P.A., Rask L.;
RT   "The primary structure of rabbit and rat prealbumin and a comparison with
RT   the tertiary structure of human prealbumin.";
RL   J. Biol. Chem. 260:6481-6487(1985).
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:3922975}.
CC   -!- TISSUE SPECIFICITY: Detected in serum (at protein level).
CC       {ECO:0000269|PubMed:3922975}.
CC   -!- SIMILARITY: Belongs to the transthyretin family. {ECO:0000305}.
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DR   PIR; B22621; VBRB.
DR   AlphaFoldDB; P07489; -.
DR   SMR; P07489; -.
DR   STRING; 9986.ENSOCUP00000014907; -.
DR   eggNOG; KOG3006; Eukaryota.
DR   InParanoid; P07489; -.
DR   Proteomes; UP000001811; Unplaced.
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; Reference proteome; Secreted; Thyroid hormone; Transport.
FT   CHAIN           1..127
FT                   /note="Transthyretin"
FT                   /id="PRO_0000050602"
FT   BINDING         15
FT                   /ligand="L-thyroxine"
FT                   /ligand_id="ChEBI:CHEBI:58448"
FT                   /evidence="ECO:0000250"
FT   BINDING         54
FT                   /ligand="L-thyroxine"
FT                   /ligand_id="ChEBI:CHEBI:58448"
FT                   /evidence="ECO:0000250"
FT   BINDING         115..119
FT                   /ligand="L-thyroxine"
FT                   /ligand_id="ChEBI:CHEBI:58448"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         42
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P02766"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   127 AA;  13657 MW;  C7FD6A385A9FE62B CRC64;
     GPVGTGDSKC PLMVKVLDAV RGSPAVDVSV HVFKKAADET WEPFASGKTS KTGELHGLTT
     SEKFVEGVYK VELDTKSYWK ALGISPFHEY AEVVFTANDS GHRSYTIAAL LSPFSYSTTA
     VVSNPQE