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Protein

Transthyretin

Gene

Ttr

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei35Thyroid hormone1
Binding sitei74Thyroid hormone1

GO - Molecular functioni

  • hormone binding Source: RGD
  • protein heterodimerization activity Source: RGD
  • thyroid hormone binding Source: GO_Central

GO - Biological processi

  • retinol metabolic process Source: RGD
  • thyroid hormone metabolic process Source: RGD
  • thyroid hormone transport Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hormone, Thyroid hormone

Keywords - Biological processi

Transport

Enzyme and pathway databases

ReactomeiR-RNO-2453902. The canonical retinoid cycle in rods (twilight vision).
R-RNO-3000171. Non-integrin membrane-ECM interactions.
R-RNO-6798695. Neutrophil degranulation.
R-RNO-975634. Retinoid metabolism and transport.

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
Proteomesi
  • UP000002494 Componenti: Chromosome 18

Organism-specific databases

RGDi3916. Ttr.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: Ensembl
  • extracellular space Source: RGD
  • protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2151.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 201 PublicationAdd BLAST20
ChainiPRO_000003576421 – 147TransthyretinAdd BLAST127

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei624-carboxyglutamateBy similarity1
Modified residuei72PhosphoserineCombined sources1
Glycosylationi118N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Gamma-carboxyglutamic acid, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP02767.
PRIDEiP02767.

PTM databases

iPTMnetiP02767.
PhosphoSitePlusiP02767.

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

BgeeiENSRNOG00000016275.
GenevisibleiP02767. RN.

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

GO - Molecular functioni

  • protein heterodimerization activity Source: RGD

Protein-protein interaction databases

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

Structurei

Secondary structure

1147
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi31 – 38Combined sources8
Turni39 – 42Combined sources4
Beta strandi49 – 55Combined sources7
Beta strandi61 – 68Combined sources8
Beta strandi73 – 75Combined sources3
Turni81 – 83Combined sources3
Beta strandi86 – 93Combined sources8
Helixi95 – 101Combined sources7
Beta strandi107 – 118Combined sources12
Beta strandi124 – 132Combined sources9
Beta strandi135 – 143Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02767.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni135 – 139Thyroid hormone binding5

Sequence similaritiesi

Belongs to the transthyretin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3006. Eukaryota.
COG2351. LUCA.
GeneTreeiENSGT00390000005321.
HOGENOMiHOG000251776.
HOVERGENiHBG000285.
InParanoidiP02767.
KOiK20731.
OMAiKTSEFGE.
OrthoDBiEOG091G0VSV.
PhylomeDBiP02767.
TreeFamiTF300210.

Family and domain databases

Gene3Di2.60.40.180. 1 hit.
InterProiIPR023418. Thyroxine_BS.
IPR030178. Transthyretin.
IPR000895. Transthyretin/HIU_hydrolase.
IPR023416. Transthyretin/HIU_hydrolase_SF.
IPR023419. Transthyretin_CS.
[Graphical view]
PANTHERiPTHR10395:SF12. PTHR10395:SF12. 1 hit.
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

        10         20         30         40         50
MASLRLFLLC LAGLIFASEA GPGGAGESKC PLMVKVLDAV RGSPAVDVAV
60 70 80 90 100
KVFKKTADGS WEPFASGKTA ESGELHGLTT DEKFTEGVYR VELDTKSYWK
110 120 130 140
ALGISPFHEY AEVVFTANDS GHRHYTIAAL LSPYSYSTTA VVSNPQN
Length:147
Mass (Da):15,720
Last modified:July 21, 1986 - v1
Checksum:i67F00D09BCF195BA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti55K → R in AAA41801 (PubMed:3922975).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry databases

ChEMBLiCHEMBL2151.

Protein family/group databases

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

PTM databases

iPTMnetiP02767.
PhosphoSitePlusiP02767.

Proteomic databases

PaxDbiP02767.
PRIDEiP02767.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7276.
RGDi3916. Ttr.

Phylogenomic databases

eggNOGiKOG3006. Eukaryota.
COG2351. LUCA.
GeneTreeiENSGT00390000005321.
HOGENOMiHOG000251776.
HOVERGENiHBG000285.
InParanoidiP02767.
KOiK20731.
OMAiKTSEFGE.
OrthoDBiEOG091G0VSV.
PhylomeDBiP02767.
TreeFamiTF300210.

Enzyme and pathway databases

ReactomeiR-RNO-2453902. The canonical retinoid cycle in rods (twilight vision).
R-RNO-3000171. Non-integrin membrane-ECM interactions.
R-RNO-6798695. Neutrophil degranulation.
R-RNO-975634. Retinoid metabolism and transport.

Miscellaneous databases

EvolutionaryTraceiP02767.
PROiP02767.

Gene expression databases

BgeeiENSRNOG00000016275.
GenevisibleiP02767. RN.

Family and domain databases

Gene3Di2.60.40.180. 1 hit.
InterProiIPR023418. Thyroxine_BS.
IPR030178. Transthyretin.
IPR000895. Transthyretin/HIU_hydrolase.
IPR023416. Transthyretin/HIU_hydrolase_SF.
IPR023419. Transthyretin_CS.
[Graphical view]
PANTHERiPTHR10395:SF12. PTHR10395:SF12. 1 hit.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 150 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.