Q8VWG7 · TDX_ARATH

Function

function

Thiol-disulfide oxidoreductase that possesses insulin disulfide bonds reducing activity, disulfide reductase, foldase chaperone and holdase chaperone activities. Heat shock causes oligomerization and formation of high molecular weiht (HMW) complexes with concomitant functional switching from a disulfide reductase and foldase chaperone to a holdase chaperone. May interact with HSP70 proteins through the TPR repeats.

Features

Showing features for active site, site.

138050100150200250300350
TypeIDPosition(s)Description
Active site304Nucleophile
Site305Contributes to redox potential value
Site306Contributes to redox potential value
Active site307Nucleophile

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componenthistone deacetylase complex
Molecular FunctionHsp70 protein binding
Molecular Functionidentical protein binding
Molecular Functionoxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor
Molecular Functionprotein dimerization activity
Biological Processheat acclimation
Biological Processprotein complex oligomerization
Biological Processprotein folding

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    TPR repeat-containing thioredoxin TDX
  • Alternative names
    • HSP70-interacting protein 2 (AtHIP2)
    • Tetratricoredoxin (AtTDX)

Gene names

    • Name
      TDX
    • ORF names
      MEB5.10/MEB5.9
    • Ordered locus names
      At3g17880/At3g17870

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q8VWG7
  • Secondary accessions
    • Q7XJ63
    • Q8LG82
    • Q9LVI2
    • Q9LVI3

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Phenotypes & Variants

Disruption phenotype

High sensitivity to heat shock.

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis304Loss of disulfide reductase activity.
Mutagenesis307Loss of disulfide reductase activity.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 34 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain, disulfide bond.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylvaline
ChainPRO_00003945482-380TPR repeat-containing thioredoxin TDX
Disulfide bond304↔307Redox-active

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Oligomerization under high temperature.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q8VWG7TDX Q8VWG75EBI-15764744, EBI-15764744

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for compositional bias, region, repeat, domain.

TypeIDPosition(s)Description
Compositional bias49-70Basic and acidic residues
Region49-115Disordered
Compositional bias71-87Acidic residues
Repeat112-145TPR 1
Repeat147-179TPR 2
Repeat181-213TPR 3
Compositional bias240-260Basic and acidic residues
Region240-265Disordered
Domain252-378Thioredoxin

Sequence similarities

Belongs to the thioredoxin family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q8VWG7-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    380
  • Mass (Da)
    42,846
  • Last updated
    2002-03-01 v1
  • Checksum
    C0181F1D74CD3AA4
MVDAIQVAELRRFVEQLKLNPSILHDPSLVFFKEYLRSLGAQVPKIEKTERDYEDKAETKPSFSPKHDDDDDDIMESDVELDNSDVVEPDNEPPQPMGDPTAEVTDENRDDAQSEKSKAMEAISDGRFDEAIEHLTKAVMLNPTSAILYATRASVFLKVKKPNAAIRDANVALQFNSDSAKGYKSRGMAKAMLGQWEEAAADLHVASKLDYDEEIGTMLKKVEPNAKRIEEHRRKYQRLRKEKELQRAERERRKQQEAQEREAQAALNDGEVISIHSTSELEAKTKAAKKASRLLILYFTATWCGPCRYMSPLYSNLATQHSRVVFLKVDIDKANDVAASWNISSVPTFCFIRDGKEVDKVVGADKGSLEQKIAQHSSSK

Q8VWG7-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Sequence caution

The sequence BAB02710.1 differs from that shown. Reason: Erroneous gene model prediction Was originally thought to correspond to two different genes At3g17870 and At3g17880.
The sequence BAB02711.1 differs from that shown. Reason: Erroneous gene model prediction Was originally thought to correspond to two different genes At3g17870 and At3g17880.

Features

Showing features for compositional bias, alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Compositional bias49-70Basic and acidic residues
Alternative sequenceVSP_03928950-56in isoform 2
Compositional bias71-87Acidic residues
Compositional bias240-260Basic and acidic residues
Sequence conflict324in Ref. 5; AAM60989

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY064251
EMBL· GenBank· DDBJ
AAL54856.1
EMBL· GenBank· DDBJ
mRNA
AY064252
EMBL· GenBank· DDBJ
AAL54857.1
EMBL· GenBank· DDBJ
Genomic DNA
AB019230
EMBL· GenBank· DDBJ
BAB02710.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
AB019230
EMBL· GenBank· DDBJ
BAB02711.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
CP002686
EMBL· GenBank· DDBJ
AEE76019.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002686
EMBL· GenBank· DDBJ
AEE76020.1
EMBL· GenBank· DDBJ
Genomic DNA
AK175494
EMBL· GenBank· DDBJ
BAD43257.1
EMBL· GenBank· DDBJ
mRNA
AK227340
EMBL· GenBank· DDBJ
BAE99351.1
EMBL· GenBank· DDBJ
mRNA
AY084415
EMBL· GenBank· DDBJ
AAM60989.1
EMBL· GenBank· DDBJ
mRNA
BT009704
EMBL· GenBank· DDBJ
AAP88338.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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