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Protein

Transthyretin

Gene

Ttr

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei35Thyroid hormone1
Binding sitei74Thyroid hormone1

GO - Molecular functioni

  • hormone activity Source: UniProtKB-KW
  • hormone binding Source: RGD
  • identical protein binding Source: Ensembl
  • protein heterodimerization activity Source: RGD
  • thyroid hormone binding Source: GO_Central

GO - Biological processi

  • retinol metabolic process Source: InterPro
  • thyroid hormone metabolic process Source: RGD
  • thyroid hormone transport Source: InterPro

Keywordsi

Molecular functionHormone, Thyroid hormone
Biological processTransport

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 18

Organism-specific databases

RGDi3916 Ttr

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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...) asparagineSequence 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

  • hormone activity Source: UniProtKB-KW
  • identical protein binding Source: Ensembl
  • protein heterodimerization activity Source: RGD

Protein-protein interaction databases

IntActiP02767, 2 interactors
MINTiP02767
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
OMAiHRHYTIA
OrthoDBiEOG091G0VSV
PhylomeDBiP02767
TreeFamiTF300210

Family and domain databases

Gene3Di2.60.40.180, 1 hit
InterProiView protein in InterPro
IPR023418 Thyroxine_BS
IPR030178 Transthyretin
IPR000895 Transthyretin/HIU_hydrolase
IPR023416 Transthyretin/HIU_hydrolase_d
IPR036817 Transthyretin/HIU_hydrolase_sf
IPR023419 Transthyretin_CS
PANTHERiPTHR10395 PTHR10395, 1 hit
PTHR10395:SF12 PTHR10395:SF12, 1 hit
PfamiView protein in Pfam
PF00576 Transthyretin, 1 hit
PRINTSiPR00189 TRNSTHYRETIN
SMARTiView protein in SMART
SM00095 TR_THY, 1 hit
SUPFAMiSSF49472 SSF49472, 1 hit
PROSITEiView protein in PROSITE
PS00768 TRANSTHYRETIN_1, 1 hit
PS00769 TRANSTHYRETIN_2, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiTTHY_RAT
AccessioniPrimary (citable) accession number: P02767
Secondary accession number(s): Q547K9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 23, 2018
This is version 160 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

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