ID   TTHY_CROPO              Reviewed;         150 AA.
AC   O55245;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Transthyretin;
DE            Short=crocTTR;
DE   AltName: Full=Prealbumin;
DE   Flags: Precursor;
GN   Name=TTR;
OS   Crocodylus porosus (Saltwater crocodile) (Estuarine crocodile).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Longirostres; Crocodylidae;
OC   Crocodylus.
OX   NCBI_TaxID=8502;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-28, FUNCTION, SUBUNIT,
RP   INTERACTION WITH RBP4, SUBCELLULAR LOCATION, DOMAIN, TISSUE SPECIFICITY,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=12228058; DOI=10.1152/ajpregu.00042.2002;
RA   Prapunpoj P., Richardson S.J., Schreiber G.;
RT   "Crocodile transthyretin: structure, function, and evolution.";
RL   Am. J. Physiol. 283:R885-R896(2002).
CC   -!- FUNCTION: Thyroid hormone-binding protein, with a much higher binding
CC       affinity for triiodothyronine (T3) than for thyroxine (T4). Probably
CC       transports triiodothyronine from the bloodstream to the brain.
CC       {ECO:0000269|PubMed:12228058}.
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. {ECO:0000269|PubMed:12228058}.
CC   -!- INTERACTION:
CC       O55245; P02753: RBP4; Xeno; NbExp=2; IntAct=EBI-7038226, EBI-2116134;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12228058}.
CC   -!- TISSUE SPECIFICITY: Strongly expressed in the brain, and to a lesser
CC       extent in the eye. {ECO:0000269|PubMed:12228058}.
CC   -!- DOMAIN: The N-terminus strongly influences thyroid hormone-binding
CC       properties. {ECO:0000269|PubMed:12228058}.
CC   -!- SIMILARITY: Belongs to the transthyretin family. {ECO:0000305}.
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DR   EMBL; AJ223148; CAA11129.1; -; mRNA.
DR   RefSeq; XP_019402943.1; XM_019547398.1.
DR   AlphaFoldDB; O55245; -.
DR   SMR; O55245; -.
DR   IntAct; O55245; 1.
DR   MINT; O55245; -.
DR   Ensembl; ENSCPRT00005025389; ENSCPRP00005021736; ENSCPRG00005015105.
DR   GeneID; 109318267; -.
DR   KEGG; cpoo:109318267; -.
DR   CTD; 7276; -.
DR   GeneTree; ENSGT00940000153229; -.
DR   OrthoDB; 1453185at2759; -.
DR   Proteomes; UP000594220; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR   GO; GO:0070324; F:thyroid hormone binding; IDA:UniProtKB.
DR   GO; GO:0042572; P:retinol metabolic process; IEA:InterPro.
DR   GO; GO:0070327; P:thyroid hormone transport; IC:UniProtKB.
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; Hormone; Reference proteome; Secreted; Signal;
KW   Thyroid hormone; Transport.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:12228058"
FT   CHAIN           21..150
FT                   /note="Transthyretin"
FT                   /id="PRO_0000035769"
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;  16412 MW;  E05DFAA6FBDE22A5 CRC64;
     MAFHSMLLVF LAGLVFLTEA APLVSHGSID SKCPLMVKVL DAVRGSPAAN VAIKVFKKTS
     DGDWQEFAAG KTTEFGEVHE LTSDEKFVEG IYRVEFDTSS YWKALGLSPF HEYADVVFTA
     NDSGHRHYTI AALLSPFSYS TTAVVSDPQE