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P02767

- TTHY_RAT

UniProt

P02767 - TTHY_RAT

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Protein

Transthyretin

Gene
Ttr, Tt
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei35 – 351Thyroid hormone
Binding sitei74 – 741Thyroid hormone

GO - Molecular functioni

  1. hormone binding Source: RGD
  2. protein heterodimerization activity Source: RGD

GO - Biological processi

  1. retinol metabolic process Source: RGD
  2. thyroid hormone metabolic process Source: RGD
  3. transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hormone, Thyroid hormone

Keywords - Biological processi

Transport

Enzyme and pathway databases

ReactomeiREACT_198744. Retinoid cycle disease events.
REACT_198756. Non-integrin membrane-ECM interactions.
REACT_199015. Retinoid metabolism and transport.
REACT_199225. Amyloids.
REACT_209105. The canonical retinoid cycle in rods (twilight vision).

Protein family/group databases

TCDBi9.B.35.1.1. the putative thyronine-transporting transthyretin (transthyretin) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Transthyretin
Alternative name(s):
Prealbumin
TBPA
Gene namesi
Name:Ttr
Synonyms:Tt
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 18

Organism-specific databases

RGDi3916. Ttr.

Subcellular locationi

Secreted 2 Publications

GO - Cellular componenti

  1. extracellular space Source: RGD
  2. protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20201 PublicationAdd
BLAST
Chaini21 – 147127TransthyretinPRO_0000035764Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei62 – 6214-carboxyglutamate By similarity
Glycosylationi118 – 1181N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Gamma-carboxyglutamic acid, Glycoprotein

Proteomic databases

PaxDbiP02767.
PRIDEiP02767.

Expressioni

Tissue specificityi

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

Gene expression databases

GenevestigatoriP02767.

Interactioni

Subunit structurei

Homotetramer. Dimer of dimers. In the homotetramer, subunits assemble around a central channel that can accommodate two ligand molecules. Interacts with RBP4.3 Publications

Protein-protein interaction databases

IntActiP02767. 2 interactions.
MINTiMINT-4585805.
STRINGi10116.ENSRNOP00000022113.

Structurei

Secondary structure

1
147
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi31 – 388
Turni39 – 424
Beta strandi49 – 557
Beta strandi61 – 688
Beta strandi73 – 753
Turni81 – 833
Beta strandi86 – 938
Helixi95 – 1017
Beta strandi107 – 11812
Beta strandi124 – 1329
Beta strandi135 – 1439

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP02767.
SMRiP02767. Positions 25-147.

Miscellaneous databases

EvolutionaryTraceiP02767.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni135 – 1395Thyroid hormone binding

Sequence similaritiesi

Belongs to the transthyretin family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2351.
GeneTreeiENSGT00390000005321.
HOGENOMiHOG000251776.
HOVERGENiHBG000285.
InParanoidiP02767.
OMAiRRYTIAA.
OrthoDBiEOG7S4X7V.
PhylomeDBiP02767.
TreeFamiTF300210.

Family and domain databases

Gene3Di2.60.40.180. 1 hit.
InterProiIPR023418. Thyroxine_BS.
IPR000895. Transthyretin/HIU_hydrolase.
IPR023416. Transthyretin/HIU_hydrolase_SF.
IPR023419. Transthyretin_CS.
[Graphical view]
PfamiPF00576. Transthyretin. 1 hit.
[Graphical view]
PRINTSiPR00189. TRNSTHYRETIN.
SMARTiSM00095. TR_THY. 1 hit.
[Graphical view]
SUPFAMiSSF49472. SSF49472. 1 hit.
PROSITEiPS00768. TRANSTHYRETIN_1. 1 hit.
PS00769. TRANSTHYRETIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P02767-1 [UniParc]FASTAAdd to Basket

« Hide

MASLRLFLLC LAGLIFASEA GPGGAGESKC PLMVKVLDAV RGSPAVDVAV    50
KVFKKTADGS WEPFASGKTA ESGELHGLTT DEKFTEGVYR VELDTKSYWK 100
ALGISPFHEY AEVVFTANDS GHRHYTIAAL LSPYSYSTTA VVSNPQN 147
Length:147
Mass (Da):15,720
Last modified:July 21, 1986 - v1
Checksum:i67F00D09BCF195BA
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551K → R in AAA41801. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiA92542. VBRT.
RefSeqiNP_036813.2. NM_012681.2.
XP_006254519.1. XM_006254457.1.
UniGeneiRn.1404.

Genome annotation databases

EnsembliENSRNOT00000022113; ENSRNOP00000022113; ENSRNOG00000016275.
GeneIDi24856.
KEGGirno:24856.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi A92542. VBRT.
RefSeqi NP_036813.2. NM_012681.2.
XP_006254519.1. XM_006254457.1.
UniGenei Rn.1404.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GKE X-ray 2.50 A/B/C/D 28-147 [» ]
1IE4 X-ray 2.50 A/B/C/D 21-147 [» ]
1KGI X-ray 1.80 A/B/C/D 21-147 [» ]
1KGJ X-ray 2.30 A/B/C/D 21-147 [» ]
1RVS NMR - A 125-135 [» ]
2M5K electron microscopy 12.70 A/B/C/D/E/F/G/H 125-135 [» ]
2M5M electron microscopy 12.20 A/B/C/D/E/F/G/H/I/J/K/L 125-135 [» ]
3ZPK NMR - A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P 125-135 [» ]
ProteinModelPortali P02767.
SMRi P02767. Positions 25-147.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P02767. 2 interactions.
MINTi MINT-4585805.
STRINGi 10116.ENSRNOP00000022113.

Chemistry

ChEMBLi CHEMBL2151.
DrugBanki DB00451. Levothyroxine.

Protein family/group databases

TCDBi 9.B.35.1.1. the putative thyronine-transporting transthyretin (transthyretin) family.

Proteomic databases

PaxDbi P02767.
PRIDEi P02767.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000022113 ; ENSRNOP00000022113 ; ENSRNOG00000016275 .
GeneIDi 24856.
KEGGi rno:24856.

Organism-specific databases

CTDi 7276.
RGDi 3916. Ttr.

Phylogenomic databases

eggNOGi COG2351.
GeneTreei ENSGT00390000005321.
HOGENOMi HOG000251776.
HOVERGENi HBG000285.
InParanoidi P02767.
OMAi RRYTIAA.
OrthoDBi EOG7S4X7V.
PhylomeDBi P02767.
TreeFami TF300210.

Enzyme and pathway databases

Reactomei REACT_198744. Retinoid cycle disease events.
REACT_198756. Non-integrin membrane-ECM interactions.
REACT_199015. Retinoid metabolism and transport.
REACT_199225. Amyloids.
REACT_209105. The canonical retinoid cycle in rods (twilight vision).

Miscellaneous databases

EvolutionaryTracei P02767.
NextBioi 604658.
PROi P02767.

Gene expression databases

Genevestigatori P02767.

Family and domain databases

Gene3Di 2.60.40.180. 1 hit.
InterProi IPR023418. Thyroxine_BS.
IPR000895. Transthyretin/HIU_hydrolase.
IPR023416. Transthyretin/HIU_hydrolase_SF.
IPR023419. Transthyretin_CS.
[Graphical view ]
Pfami PF00576. Transthyretin. 1 hit.
[Graphical view ]
PRINTSi PR00189. TRNSTHYRETIN.
SMARTi SM00095. TR_THY. 1 hit.
[Graphical view ]
SUPFAMi SSF49472. SSF49472. 1 hit.
PROSITEi PS00768. TRANSTHYRETIN_1. 1 hit.
PS00769. TRANSTHYRETIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiTTHY_RAT
AccessioniPrimary (citable) accession number: P02767
Secondary accession number(s): Q547K9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: September 3, 2014
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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