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P02767

- TTHY_RAT

UniProt

P02767 - TTHY_RAT

Protein

Transthyretin

Gene

Ttr

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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

    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

    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-carboxyglutamateBy similarity
    Glycosylationi118 – 1181N-linked (GlcNAc...)Sequence Analysis

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02767.

    Family & Domainsi

    Region

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

    Sequence similaritiesi

    Belongs to the transthyretin family.Curated

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti55 – 551K → R in AAA41801. (PubMed:3922975)Curated

    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

    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: October 1, 2014
    This is version 132 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.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