ID   TTHY_XENTR              Reviewed;         151 AA.
AC   A4QNN7;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Transthyretin {ECO:0000250|UniProtKB:B7ZS96};
DE   AltName: Full=Prealbumin {ECO:0000250|UniProtKB:P02766};
DE   Flags: Precursor;
GN   Name=ttr;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1] {ECO:0000312|EMBL:AAI35937.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Tadpole {ECO:0000312|EMBL:AAI35937.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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 (By
CC       similarity). {ECO:0000250|UniProtKB:B7ZS96}.
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|UniProtKB:B7ZS96}.
CC   -!- DOMAIN: The N-terminus strongly influences thyroid hormone-binding
CC       properties. {ECO:0000250|UniProtKB:B7ZS96}.
CC   -!- SIMILARITY: Belongs to the transthyretin family. {ECO:0000255}.
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DR   EMBL; BC135936; AAI35937.1; -; mRNA.
DR   RefSeq; NP_001096539.1; NM_001103069.1.
DR   AlphaFoldDB; A4QNN7; -.
DR   SMR; A4QNN7; -.
DR   PaxDb; A4QNN7; -.
DR   DNASU; 100125183; -.
DR   Ensembl; ENSXETT00000010246; ENSXETP00000010246; ENSXETG00000004725.
DR   GeneID; 100125183; -.
DR   KEGG; xtr:100125183; -.
DR   CTD; 7276; -.
DR   Xenbase; XB-GENE-479395; ttr.
DR   eggNOG; KOG3006; Eukaryota.
DR   HOGENOM; CLU_115536_2_0_1; -.
DR   InParanoid; A4QNN7; -.
DR   OMA; PFYHHAD; -.
DR   OrthoDB; 1453185at2759; -.
DR   PhylomeDB; A4QNN7; -.
DR   TreeFam; TF300210; -.
DR   Reactome; R-XTR-2453902; The canonical retinoid cycle in rods (twilight vision).
DR   Reactome; R-XTR-3000171; Non-integrin membrane-ECM interactions.
DR   Reactome; R-XTR-6798695; Neutrophil degranulation.
DR   Reactome; R-XTR-975634; Retinoid metabolism and transport.
DR   Proteomes; UP000008143; Chromosome 6.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000004725; Expressed in liver and 7 other tissues.
DR   ExpressionAtlas; A4QNN7; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0070324; F:thyroid hormone binding; ISS:UniProtKB.
DR   GO; GO:0006144; P:purine nucleobase metabolic process; IBA:GO_Central.
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   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.
PE   2: Evidence at transcript level;
KW   Hormone; Reference proteome; Secreted; Signal; Thyroid hormone; Transport.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250|UniProtKB:B7ZS96"
FT   CHAIN           20..151
FT                   /note="Transthyretin"
FT                   /evidence="ECO:0000250|UniProtKB:B7ZS96, ECO:0000255"
FT                   /id="PRO_0000389430"
FT   BINDING         38
FT                   /ligand="L-thyroxine"
FT                   /ligand_id="ChEBI:CHEBI:58448"
FT                   /evidence="ECO:0000250|UniProtKB:P02766"
FT   BINDING         76
FT                   /ligand="L-thyroxine"
FT                   /ligand_id="ChEBI:CHEBI:58448"
FT                   /evidence="ECO:0000250|UniProtKB:P02766"
FT   BINDING         137..141
FT                   /ligand="L-thyroxine"
FT                   /ligand_id="ChEBI:CHEBI:58448"
FT                   /evidence="ECO:0000250|UniProtKB:P02766"
SQ   SEQUENCE   151 AA;  16604 MW;  FBDA1B6CF9E39CB3 CRC64;
     MAFFKSFLLL ALLAIASEAA PGHVSHGEAD SKCPLMVKVL DAVRGIPAAN LLVQVFRNTE
     GNWELISSGK TTELGEIHNI ITDEQFTEGV YKIEFATKTF WRKLGLSPFH EYVDVVFSAN
     DAGHRHYTIA VLLTPYSISS TAVVSEPHDD L