TTHY_CHICK
ID TTHY_CHICK Reviewed; 150 AA.
AC P27731;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Transthyretin;
DE AltName: Full=Prealbumin;
DE AltName: Full=TBPA;
DE Flags: Precursor;
GN Name=TTR;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-40, FUNCTION,
RP SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE SPECIFICITY.
RC STRAIN=White leghorn; TISSUE=Liver;
RX PubMed=1833190; DOI=10.1111/j.1432-1033.1991.tb16232.x;
RA Duan W., Achen M.G., Richardson S.J., Lawrence M.C., Wettenhall R.E.H.,
RA Jaworowski A., Schreiber G.;
RT "Isolation, characterization, cDNA cloning and gene expression of an avian
RT transthyretin. Implications for the evolution of structure and function of
RT transthyretin in vertebrates.";
RL Eur. J. Biochem. 200:679-687(1991).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=1799976; DOI=10.1016/0305-0491(91)90383-o;
RA Southwell B.R., Duan W., Tu G.F., Schreiber G.;
RT "Ontogenesis of transthyretin gene expression in chicken choroid plexus and
RT liver.";
RL Comp. Biochem. Physiol. 100B:329-338(1991).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), SUBUNIT, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=8612621; DOI=10.1111/j.1432-1033.1996.00491.x;
RA Sunde M., Richardson S.J., Chang L., Pettersson T.M., Schreiber G.,
RA Blake C.C.F.;
RT "The crystal structure of transthyretin from chicken.";
RL Eur. J. Biochem. 236:491-499(1996).
CC -!- FUNCTION: Thyroid hormone-binding protein. Probably transports
CC thyroxine from the bloodstream to the brain.
CC {ECO:0000269|PubMed:1833190}.
CC -!- SUBUNIT: Homotetramer. Dimer of dimers. In the homotetramer, subunits
CC assemble around a central channel that can accommodate two ligand
CC molecules. {ECO:0000269|PubMed:1833190, ECO:0000269|PubMed:8612621}.
CC -!- INTERACTION:
CC P27731; P41263: RBP4; NbExp=4; IntAct=EBI-6622511, EBI-6622456;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1833190,
CC ECO:0000269|PubMed:8612621}.
CC -!- TISSUE SPECIFICITY: Detected in serum (at protein level). Detected in
CC liver and choroid plexus. {ECO:0000269|PubMed:1799976,
CC ECO:0000269|PubMed:1833190, ECO:0000269|PubMed:8612621}.
CC -!- SIMILARITY: Belongs to the transthyretin family. {ECO:0000305}.
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DR EMBL; X60471; CAA43000.1; -; mRNA.
DR PIR; S17827; S17827.
DR RefSeq; NP_990666.1; NM_205335.3.
DR PDB; 1TFP; X-ray; 2.90 A; A/B=21-150.
DR PDBsum; 1TFP; -.
DR AlphaFoldDB; P27731; -.
DR SMR; P27731; -.
DR IntAct; P27731; 1.
DR STRING; 9031.ENSGALP00000024388; -.
DR PaxDb; P27731; -.
DR GeneID; 396277; -.
DR KEGG; gga:396277; -.
DR CTD; 7276; -.
DR VEuPathDB; HostDB:geneid_396277; -.
DR eggNOG; KOG3006; Eukaryota.
DR HOGENOM; CLU_115536_2_0_1; -.
DR InParanoid; P27731; -.
DR PhylomeDB; P27731; -.
DR TreeFam; TF300210; -.
DR EvolutionaryTrace; P27731; -.
DR PRO; PR:P27731; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:AgBase.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0032991; C:protein-containing complex; IDA:AgBase.
DR GO; GO:0060417; C:yolk; IDA:AgBase.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0042562; F:hormone binding; ISA:AgBase.
DR GO; GO:0019904; F:protein domain specific binding; IPI:AgBase.
DR GO; GO:0046982; F:protein heterodimerization activity; ISA:AgBase.
DR GO; GO:0036094; F:small molecule binding; IPI:AgBase.
DR GO; GO:0070324; F:thyroid hormone binding; IDA:AgBase.
DR GO; GO:0001555; P:oocyte growth; IEP:AgBase.
DR GO; GO:0051262; P:protein tetramerization; IDA:AgBase.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:AgBase.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IBA:GO_Central.
DR GO; GO:0009615; P:response to virus; IDA:AgBase.
DR GO; GO:0042572; P:retinol metabolic process; ISA:AgBase.
DR GO; GO:0070327; P:thyroid hormone transport; TAS:AgBase.
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 3D-structure; Direct protein sequencing; Hormone; Reference proteome;
KW Secreted; Signal; Thyroid hormone; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:1833190"
FT CHAIN 21..150
FT /note="Transthyretin"
FT /id="PRO_0000035768"
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 STRAND 35..41
FT /evidence="ECO:0007829|PDB:1TFP"
FT TURN 42..45
FT /evidence="ECO:0007829|PDB:1TFP"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:1TFP"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:1TFP"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:1TFP"
FT STRAND 89..97
FT /evidence="ECO:0007829|PDB:1TFP"
FT TURN 99..106
FT /evidence="ECO:0007829|PDB:1TFP"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:1TFP"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:1TFP"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:1TFP"
FT STRAND 136..145
FT /evidence="ECO:0007829|PDB:1TFP"
SQ SEQUENCE 150 AA; 16309 MW; 1F82A776A9996360 CRC64;
MAFHSTLLVF LAGLVFLSEA APLVSHGSVD SKCPLMVKVL DAVRGSPAAN VAVKVFKKAA
DGTWQDFATG KTTEFGEIHE LTTEEQFVEG VYRVEFDTSS YWKGLGLSPF HEYADVVFTA
NDSGHRHYTI AALLSPFSYS TTAVVSDPQE
