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P07309 (TTHY_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Gene names
Name:Ttr
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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.

Subunit structure

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

Subcellular location

Secreted.

Tissue specificity

Detected in plasma (at protein level). Detected in liver.

Miscellaneous

The mouse protein shows increased stability and much reduced propensity to form amyloid fibrils, compared to the human protein.

Sequence similarities

Belongs to the transthyretin family.

Ontologies

Keywords
   Biological processTransport
   Cellular componentSecreted
   DomainSignal
   Molecular functionHormone
Thyroid hormone
   PTMGamma-carboxyglutamic acid
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processretinol metabolic process

Inferred from electronic annotation. Source: Ensembl

transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular space

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionhormone binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020
Chain21 – 147127Transthyretin
PRO_0000035760

Regions

Region135 – 1395Thyroid hormone binding By similarity

Sites

Binding site351Thyroid hormone By similarity
Binding site741Thyroid hormone By similarity

Amino acid modifications

Modified residue6214-carboxyglutamate By similarity
Glycosylation1181N-linked (GlcNAc...) Ref.6

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P07309 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: 9803CCC3024BA911

FASTA14715,776
        10         20         30         40         50         60 
MASLRLFLLC LAGLVFVSEA GPAGAGESKC PLMVKVLDAV RGSPAVDVAV KVFKKTSEGS 

        70         80         90        100        110        120 
WEPFASGKTA ESGELHGLTT DEKFVEGVYR VELDTKSYWK TLGISPFHEF ADVVFTANDS 

       130        140 
GHRHYTIAAL LSPYSYSTTA VVSNPQN 

« Hide

References

« Hide 'large scale' references
[1]"Structural comparisons between mouse and human prealbumin."
Wakasugi S., Maeda S., Shimada K., Nakashima H., Migita S.
J. Biochem. 98:1707-1714(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], THYROID HORMONE-BINDING SITES LYS-35 AND GLU-74.
Tissue: Liver.
[2]"Structure and expression of the mouse prealbumin gene."
Wakasugi S., Maeda S., Shimada K.
J. Biochem. 100:49-58(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[3]Kita H., Kawamoto S., Okubo K., Matsubara K.
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: C57BL/6.
Tissue: Choroid plexus.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Kidney.
[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].
Strain: FVB/N.
Tissue: Salivary gland.
[6]"Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides."
Bernhard O.K., Kapp E.A., Simpson R.J.
J. Proteome Res. 6:987-995(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-118.
Strain: C57BL/6.
Tissue: Plasma.
[7]"Human-murine transthyretin heterotetramers are kinetically stable and non-amyloidogenic. A lesson in the generation of transgenic models of diseases involving oligomeric proteins."
Reixach N., Foss T.R., Santelli E., Pascual J., Kelly J.W., Buxbaum J.N.
J. Biol. Chem. 283:2098-2107(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 21-147, INCREASED STABILITY OF THE MOUSE PROTEIN, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03351 mRNA. Translation: CAA27057.1.
D00073 Genomic DNA. Translation: BAA00050.1.
D89076 mRNA. Translation: BAA13757.1.
AK018701 mRNA. Translation: BAB31352.1.
BC024702 mRNA. Translation: AAH24702.1.
PIRVBMS. A24132.
RefSeqNP_038725.1. NM_013697.5.
UniGeneMm.2108.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QPFX-ray2.05A/B/C/D/E/F/G/H21-147[»]
ProteinModelPortalP07309.
SMRP07309. Positions 31-144.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-29726N.
IntActP07309. 2 interactions.
MINTMINT-1855774.

PTM databases

PhosphoSiteP07309.

2D gel databases

UCD-2DPAGEP07309.

Proteomic databases

PaxDbP07309.
PRIDEP07309.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000075312; ENSMUSP00000074783; ENSMUSG00000061808.
GeneID22139.
KEGGmmu:22139.
UCSCuc008eet.2. mouse.

Organism-specific databases

CTD7276.
MGIMGI:98865. Ttr.

Phylogenomic databases

eggNOGCOG2351.
HOGENOMHOG000251776.
HOVERGENHBG000285.
InParanoidP07309.
OMATKSYWKA.
OrthoDBEOG7S4X7V.
PhylomeDBP07309.
TreeFamTF300210.

Gene expression databases

ArrayExpressP07309.
BgeeP07309.
CleanExMM_TTR.
GenevestigatorP07309.

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

ChiTaRSTTR. mouse.
EvolutionaryTraceP07309.
NextBio302028.
PROP07309.
SOURCESearch...

Entry information

Entry nameTTHY_MOUSE
AccessionPrimary (citable) accession number: P07309
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: April 16, 2014
This is version 121 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot