TTHY_PIG
ID TTHY_PIG Reviewed; 150 AA.
AC P50390; Q2IA93;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Transthyretin;
DE AltName: Full=Prealbumin;
DE Flags: Precursor;
GN Name=TTR;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, SUBUNIT, AND INTERACTION WITH RBP4.
RC STRAIN=Large white; TISSUE=Choroid plexus;
RX PubMed=7601162; DOI=10.1111/j.1432-1033.1995.tb20645.x;
RA Duan W., Richardson S.J., Koehrle J., Chang L., Southwell B.R., Harms P.J.,
RA Brack C.M., Pettersson T.M., Schreiber G.;
RT "Binding of thyroxine to pig transthyretin, its cDNA structure, and other
RT properties.";
RL Eur. J. Biochem. 230:977-986(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Jacobsen M., Horn P., Bendixen C.;
RT "Genetic variation and expression profile of porcine transthyretin gene.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-150.
RC TISSUE=Liver;
RX PubMed=8930078; DOI=10.1111/j.1365-2052.1996.tb00977.x;
RA Archibald A.L., Couperwhite S., Jiang Z.H.;
RT "The porcine TTR locus maps to chromosome 6q.";
RL Anim. Genet. 27:351-353(1996).
CC -!- FUNCTION: Thyroid hormone-binding protein. Probably transports
CC thyroxine from the bloodstream to the brain.
CC {ECO:0000269|PubMed:7601162}.
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:7601162}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7601162}.
CC -!- TISSUE SPECIFICITY: Detected in plasma and cerebrospinal fluid (at
CC protein level). Highly expressed in the choroid plexus. Detected in
CC liver. {ECO:0000269|PubMed:7601162}.
CC -!- SIMILARITY: Belongs to the transthyretin family. {ECO:0000305}.
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DR EMBL; X82258; CAA57713.1; -; mRNA.
DR EMBL; U16131; AAA79042.1; -; mRNA.
DR EMBL; DQ117974; AAZ94915.1; -; Genomic_DNA.
DR EMBL; DQ117971; AAZ94915.1; JOINED; Genomic_DNA.
DR EMBL; DQ117972; AAZ94915.1; JOINED; Genomic_DNA.
DR EMBL; DQ117973; AAZ94915.1; JOINED; Genomic_DNA.
DR EMBL; X87846; CAA61120.1; -; mRNA.
DR PIR; S65955; S65955.
DR RefSeq; NP_999377.1; NM_214212.1.
DR AlphaFoldDB; P50390; -.
DR SMR; P50390; -.
DR STRING; 9823.ENSSSCP00000022931; -.
DR PaxDb; P50390; -.
DR PeptideAtlas; P50390; -.
DR PRIDE; P50390; -.
DR Ensembl; ENSSSCT00060084543; ENSSSCP00060036610; ENSSSCG00060061967.
DR GeneID; 397419; -.
DR KEGG; ssc:397419; -.
DR CTD; 7276; -.
DR eggNOG; KOG3006; Eukaryota.
DR HOGENOM; CLU_115536_2_0_1; -.
DR InParanoid; P50390; -.
DR OMA; TWEPFAT; -.
DR OrthoDB; 1453185at2759; -.
DR TreeFam; TF300210; -.
DR Reactome; R-SSC-2453902; The canonical retinoid cycle in rods (twilight vision).
DR Reactome; R-SSC-6798695; Neutrophil degranulation.
DR Reactome; R-SSC-975634; Retinoid metabolism and transport.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; P50390; SS.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0036094; F:small molecule binding; IPI:AgBase.
DR GO; GO:0070324; F:thyroid hormone binding; IMP:AgBase.
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; Reference proteome;
KW Secreted; Signal; Thyroid hormone; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..150
FT /note="Transthyretin"
FT /id="PRO_0000035763"
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 CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 150 AA; 16081 MW; 0427FD5D3094CA07 CRC64;
MASYRLLLLC LAGLVFVSEA GPAGAGESKC PLMVKVLDAV RGSPAVNVGV KVFKKAADGT
WEPFALGKTS EFGELHGLTT DEKFVEGIYK VELDTKSYWK ALGISPFHEY AEVVFTANDS
GRRHYTIAAL LSPYSYSTTA LVSSPKEGAL
