ID   TTHY_MACFA              Reviewed;         147 AA.
AC   Q8HXW1; Q4R5L4;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 2.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Transthyretin;
DE   AltName: Full=Prealbumin;
DE   Flags: Precursor;
GN   Name=TTR; ORFNames=QccE-10711, QccE-14396;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RA   Kusuda J., Osada N., Hida M., Sugano S., Hashimoto K.;
RT   "Isolation and characterization of cDNA for macaque neurological disease
RT   genes.";
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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:0000250}.
CC   -!- SIMILARITY: Belongs to the transthyretin family. {ECO:0000305}.
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DR   EMBL; AB083330; BAC20609.1; -; mRNA.
DR   EMBL; AB169529; BAE01611.1; -; mRNA.
DR   RefSeq; NP_001270522.1; NM_001283593.1.
DR   AlphaFoldDB; Q8HXW1; -.
DR   SMR; Q8HXW1; -.
DR   STRING; 9541.XP_005587024.1; -.
DR   GeneID; 101864775; -.
DR   CTD; 7276; -.
DR   VEuPathDB; HostDB:ENSMFAG00000039111; -.
DR   eggNOG; KOG3006; Eukaryota.
DR   OMA; TWEPFAT; -.
DR   OrthoDB; 1453185at2759; -.
DR   Proteomes; UP000233100; Chromosome 18.
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   2: Evidence at transcript level;
KW   Glycoprotein; Hormone; Phosphoprotein; Reference proteome; Secreted;
KW   Signal; Thyroid hormone; Transport.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..147
FT                   /note="Transthyretin"
FT                   /id="PRO_0000035757"
FT   BINDING         35
FT                   /ligand="L-thyroxine"
FT                   /ligand_id="ChEBI:CHEBI:58448"
FT                   /evidence="ECO:0000250"
FT   BINDING         74
FT                   /ligand="L-thyroxine"
FT                   /ligand_id="ChEBI:CHEBI:58448"
FT                   /evidence="ECO:0000250"
FT   BINDING         135..139
FT                   /ligand="L-thyroxine"
FT                   /ligand_id="ChEBI:CHEBI:58448"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         72
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02767"
FT   CARBOHYD        118
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        129
FT                   /note="A -> R (in Ref. 1; BAC20609)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   147 AA;  15831 MW;  B6C2D66355FE0D77 CRC64;
     MASHRLLLLC LAGLVFVSEA GPTGVDESKC PLMVKVLDAV RGSPAVNVAV NVFKKAADET
     WAPFASGKTS ESGELHGLTT EEEFVEGIYK VEIDTKSYWK SLGISPFHEH AEVVFTANDS
     GPRHYTIAAL LSPYSYSTTA VVTNPKE