TTHY_BOVIN
ID TTHY_BOVIN Reviewed; 147 AA.
AC O46375; Q3SZ91;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Transthyretin;
DE AltName: Full=Prealbumin;
DE Flags: Precursor;
GN Name=TTR;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Irikura D., Kanaoka Y., Urade Y.;
RT "Cloning of bovine homolog of transthyretin.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Kidney;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH RBP4.
RX PubMed=2598638; DOI=10.1016/0305-0491(89)90014-x;
RA Berni R., Lamberti V.;
RT "Dissociation of the bovine serum retinol-binding protein-transthyretin
RT complex and purification of the two interacting proteins.";
RL Comp. Biochem. Physiol. 94B:79-83(1989).
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. {ECO:0000269|PubMed:2598638}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2598638}.
CC -!- TISSUE SPECIFICITY: Detected in serum (at protein level).
CC {ECO:0000269|PubMed:2598638}.
CC -!- SIMILARITY: Belongs to the transthyretin family. {ECO:0000305}.
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DR EMBL; AB009591; BAA23983.1; -; mRNA.
DR EMBL; BC103035; AAI03036.1; -; mRNA.
DR RefSeq; NP_776392.1; NM_173967.3.
DR AlphaFoldDB; O46375; -.
DR SMR; O46375; -.
DR STRING; 9913.ENSBTAP00000014585; -.
DR PaxDb; O46375; -.
DR PeptideAtlas; O46375; -.
DR PRIDE; O46375; -.
DR Ensembl; ENSBTAT00000014585; ENSBTAP00000014585; ENSBTAG00000010991.
DR GeneID; 280948; -.
DR KEGG; bta:280948; -.
DR CTD; 7276; -.
DR VEuPathDB; HostDB:ENSBTAG00000010991; -.
DR VGNC; VGNC:36499; TTR.
DR eggNOG; KOG3006; Eukaryota.
DR GeneTree; ENSGT00940000153229; -.
DR HOGENOM; CLU_115536_2_0_1; -.
DR InParanoid; O46375; -.
DR OMA; TWEPFAT; -.
DR OrthoDB; 1453185at2759; -.
DR TreeFam; TF300210; -.
DR Proteomes; UP000009136; Chromosome 24.
DR Bgee; ENSBTAG00000010991; Expressed in liver and 94 other tissues.
DR ExpressionAtlas; O46375; baseline and differential.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0070324; F:thyroid hormone binding; IBA:GO_Central.
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 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 Gamma-carboxyglutamic acid; Glycoprotein; Hormone; Phosphoprotein;
KW Reference proteome; Secreted; Signal; Thyroid hormone; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..147
FT /note="Transthyretin"
FT /id="PRO_0000035753"
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 62
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P02766"
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"
SQ SEQUENCE 147 AA; 15727 MW; 54C8CA7EC04478B7 CRC64;
MASFRLFLLC LAGLVFVSEA GSVGAGEPKC PLMVKVLDAV RGSPAANVGV KVFKKAADET
WEPFASGKTS ESGELHGLTT EDKFVEGLYK VELDTKSYWK SLGISPFHEF AEVVFTANDS
GPRHYTIAAL LSPYSYSTTA LVSSPKA