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P02767 (TTHY_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transthyretin
Alternative name(s):
Prealbumin
TBPA
Gene names
Name:Ttr
Synonyms:Tt
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length147 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain. Ref.9

Subunit structure

Homotetramer. Dimer of dimers. In the homotetramer, subunits assemble around a central channel that can accommodate two ligand molecules. Interacts with RBP4. Ref.7 Ref.10 Ref.11

Subcellular location

Secreted Ref.7 Ref.9.

Tissue specificity

Detected in serum and cerebrospinal fluid (at protein level). Highly expressed in the choroid plexus. Detected at lower levels in the liver. Ref.3 Ref.7 Ref.9

Miscellaneous

This protein binds retinol-binding protein at levels similar to, and the thyroid hormones at levels much higher than, the human protein.

Tetramer dissociation and partial unfolding leads to the formation of aggregates and amyloid fibrils. Small molecules that occupy at least one of the thyroid hormone binding sites stabilize the tetramer, and thereby stabilize the native state and protect against misfolding and the formation of amyloid fibrils By similarity.

Sequence similarities

Belongs to the transthyretin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.7
Chain21 – 147127Transthyretin
PRO_0000035764

Regions

Region135 – 1395Thyroid hormone binding

Sites

Binding site351Thyroid hormone
Binding site741Thyroid hormone

Amino acid modifications

Modified residue6214-carboxyglutamate By similarity
Glycosylation1181N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict551K → R in AAA41801. Ref.1

Secondary structure

...................... 147
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02767 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 67F00D09BCF195BA

FASTA14715,720
        10         20         30         40         50         60 
MASLRLFLLC LAGLIFASEA GPGGAGESKC PLMVKVLDAV RGSPAVDVAV KVFKKTADGS 

        70         80         90        100        110        120 
WEPFASGKTA ESGELHGLTT DEKFTEGVYR VELDTKSYWK ALGISPFHEY AEVVFTANDS 

       130        140 
GHRHYTIAAL LSPYSYSTTA VVSNPQN 

« Hide

References

« Hide 'large scale' references
[1]"The primary structure of rabbit and rat prealbumin and a comparison with the tertiary structure of human prealbumin."
Sundelin J., Melhus H., Das S., Eriksson U., Lind P., Traegaardh L., Peterson P.A., Rask L.
J. Biol. Chem. 260:6481-6487(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Rat transthyretin (prealbumin). Molecular cloning, nucleotide sequence, and gene expression in liver and brain."
Dickson P.W., Howlett G.J., Schreiber G.
J. Biol. Chem. 260:8214-8219(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Cloning and nucleotide sequencing of transthyretin (prealbumin) cDNA from rat choroid plexus and liver."
Duan W., Cole T., Schreiber G.
Nucleic Acids Res. 17:3979-3979(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[4]"Cloning and identification of differential display genes after short interval successive partial hepatectomy in rat liver regeneration."
Lee Y., Xu C., Zhang Y.
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.
[6]"Structure and expression of the rat transthyretin (prealbumin) gene."
Fung W.-P., Thomas T., Dickson P.W., Aldred A.R., Milland J., Dziadek M., Power B., Hudson P.J., Schreiber G.
J. Biol. Chem. 263:480-488(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23 AND 113-147.
Strain: Buffalo.
Tissue: Liver.
[7]"Rat plasma prealbumin. Isolation and partial characterization."
Navab M., Mallia A.K., Kanda Y., Goodman D.S.
J. Biol. Chem. 252:5100-5106(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-35 AND 38-50, SUBUNIT, INTERACTION WITH RBP4, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Serum.
[8]Lubec G., Afjehi-Sadat L., Lubec S.
Submitted (SEP-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 56-90; 101-123 AND 124-147, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain and Spinal cord.
[9]"Thyroxine transport from blood to brain via transthyretin synthesis in choroid plexus."
Schreiber G., Aldred A.R., Jaworowski A., Nilsson C., Achen M.G., Segal M.B.
Am. J. Physiol. 258:R338-R345(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[10]"Crystal structure of rat transthyretin at 2.5-A resolution: first report on a unique tetrameric structure."
Wojtczak A.
Acta Biochim. Pol. 44:505-517(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), SUBUNIT.
[11]"Complex of rat transthyretin with tetraiodothyroacetic acid refined at 2.1 and 1.8 A resolution."
Muziol T., Cody V., Luft J.R., Pangborn W., Wojtczak A.
Acta Biochim. Pol. 48:877-884(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 21-147 IN COMPLEX WITH TETRAIODOTHYROACETIC ACID, INTERACTION WITH RETINOL-BINDING PROTEIN, SUBUNIT.
[12]"High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy."
Jaroniec C.P., MacPhee C.E., Bajaj V.S., McMahon M.T., Dobson C.M., Griffin R.G.
Proc. Natl. Acad. Sci. U.S.A. 101:711-716(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 125-135 OF FIBRILLAR FORM.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K03252 mRNA. Translation: AAA41801.1.
K03251 Genomic DNA. Translation: AAA41802.1.
X14876 mRNA. Translation: CAA33017.1.
AF479660 mRNA. Translation: AAL78377.1.
BC086946 mRNA. Translation: AAH86946.1.
M18685 Genomic DNA. Translation: AAA40708.1.
M20246 Genomic DNA. Translation: AAA40709.1.
PIRVBRT. A92542.
RefSeqNP_036813.2. NM_012681.2.
XP_006254519.1. XM_006254457.1.
UniGeneRn.1404.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GKEX-ray2.50A/B/C/D28-147[»]
1IE4X-ray2.50A/B/C/D21-147[»]
1KGIX-ray1.80A/B/C/D21-147[»]
1KGJX-ray2.30A/B/C/D21-147[»]
1RVSNMR-A125-135[»]
2M5Kelectron microscopy12.70A/B/C/D/E/F/G/H125-135[»]
2M5Melectron microscopy12.20A/B/C/D/E/F/G/H/I/J/K/L125-135[»]
3ZPKNMR-A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P125-135[»]
ProteinModelPortalP02767.
SMRP02767. Positions 25-147.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP02767. 2 interactions.
MINTMINT-4585805.
STRING10116.ENSRNOP00000022113.

Chemistry

ChEMBLCHEMBL2151.
DrugBankDB00451. Levothyroxine.

Protein family/group databases

TCDB9.B.35.1.1. the putative thyronine-transporting transthyretin (transthyretin) family.

Proteomic databases

PaxDbP02767.
PRIDEP02767.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000022113; ENSRNOP00000022113; ENSRNOG00000016275.
GeneID24856.
KEGGrno:24856.

Organism-specific databases

CTD7276.
RGD3916. Ttr.

Phylogenomic databases

eggNOGCOG2351.
GeneTreeENSGT00390000005321.
HOGENOMHOG000251776.
HOVERGENHBG000285.
InParanoidP02767.
OMATKSYWKA.
OrthoDBEOG7S4X7V.
PhylomeDBP02767.
TreeFamTF300210.

Gene expression databases

GenevestigatorP02767.

Family and domain databases

Gene3D2.60.40.180. 1 hit.
InterProIPR023418. Thyroxine_BS.
IPR000895. Transthyretin/HIU_hydrolase.
IPR023416. Transthyretin/HIU_hydrolase_SF.
IPR023419. Transthyretin_CS.
[Graphical view]
PfamPF00576. Transthyretin. 1 hit.
[Graphical view]
PRINTSPR00189. TRNSTHYRETIN.
SMARTSM00095. TR_THY. 1 hit.
[Graphical view]
SUPFAMSSF49472. SSF49472. 1 hit.
PROSITEPS00768. TRANSTHYRETIN_1. 1 hit.
PS00769. TRANSTHYRETIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP02767.
NextBio604658.
PROP02767.

Entry information

Entry nameTTHY_RAT
AccessionPrimary (citable) accession number: P02767
Secondary accession number(s): Q547K9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 16, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references