TTHY_LITCT
ID TTHY_LITCT Reviewed; 153 AA.
AC P31779; O93483;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Transthyretin;
DE AltName: Full=Prealbumin;
DE AltName: Full=THBP;
DE AltName: Full=Tadpole T3-binding protein;
DE Short=T-T3BP;
DE Flags: Precursor;
OS Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX NCBI_TaxID=8400;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Tadpole liver;
RX PubMed=9760166; DOI=10.1046/j.1432-1327.1998.2560287.x;
RA Yamauchi K., Takeuchi H.-A., Overall M., Dziadek M., Munro S.L.A.,
RA Schreiber G.;
RT "Structural characteristics of bullfrog (Rana catesbeiana) transthyretin
RT and its cDNA. Comparison of its pattern of expression during metamorphosis
RT with that of lipocalin.";
RL Eur. J. Biochem. 256:287-296(1998).
RN [2]
RP PROTEIN SEQUENCE OF 25-43, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Tadpole;
RX PubMed=8477670; DOI=10.1210/endo.132.5.8477670;
RA Yamauchi K., Kasahara T., Hayashi H., Horiuchi R.;
RT "Purification and characterization of a 3,5,3'-L-triiodothyronine-specific
RT binding protein from bullfrog tadpole plasma: a homolog of mammalian
RT transthyretin.";
RL Endocrinology 132:2254-2261(1993).
RN [3]
RP FUNCTION, INHIBITION OF TRIIODOTHYRONINE-BINDING, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=11017780; DOI=10.1006/gcen.2000.7528;
RA Yamauchi K., Prapunpoj P., Richardson S.J.;
RT "Effect of diethylstilbestrol on thyroid hormone binding to amphibian
RT transthyretins.";
RL Gen. Comp. Endocrinol. 119:329-339(2000).
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:11017780, ECO:0000269|PubMed:8477670}.
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:8477670}.
CC -!- TISSUE SPECIFICITY: Detected in plasma (at protein level). Expressed
CC during metamorphosis in tadpole liver but not in tadpole brain, nor
CC adult liver. {ECO:0000269|PubMed:11017780, ECO:0000269|PubMed:8477670,
CC ECO:0000269|PubMed:9760166}.
CC -!- DEVELOPMENTAL STAGE: Expressed in tadpoles from premetamorphic stage X,
CC increasing until the end of prometamorphic stage (stage XX). Expression
CC then declines during metamorphic climax stages (stages XXI-XXV),
CC becoming undetectable at stage XXV and in adults.
CC {ECO:0000269|PubMed:11017780, ECO:0000269|PubMed:8477670,
CC ECO:0000269|PubMed:9760166}.
CC -!- DOMAIN: The N-terminus strongly influences thyroid hormone-binding
CC properties. {ECO:0000250}.
CC -!- MISCELLANEOUS: A number of compounds can compete with and disrupt
CC triiodothyronine (T3)-binding. Binds the synthetic estrogen
CC diethylstilbestrol (DES) with the same affinity as T3.
CC -!- SIMILARITY: Belongs to the transthyretin family. {ECO:0000305}.
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DR EMBL; AB006134; BAA33456.1; -; mRNA.
DR AlphaFoldDB; P31779; -.
DR SMR; P31779; -.
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; IEP: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; Secreted; Signal; Thyroid hormone;
KW Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:8477670"
FT CHAIN 25..153
FT /note="Transthyretin"
FT /id="PRO_0000035771"
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"
FT CONFLICT 34
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 153 AA; 16973 MW; 2E6FB07D7C1A9E78 CRC64;
MAYYNTLALL TIFIFSGAFH RAQGTHGEAD SKCPLMVKVL DAVRGIPAAK LPVKVFKQNE
DKSWDLISSG TTSSDGEIHN LATEEQFVEG IYKLEFATKR FWSKLGLTPF HEYVDVVFTA
NDAGHRHYTT AVLLTPYSFS TTAVVSDVKE AHV
