Q8VWG7 · TDX_ARATH
- ProteinTPR repeat-containing thioredoxin TDX
- GeneTDX
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids380 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 304 | Nucleophile | ||||
Sequence: C | ||||||
Site | 305 | Contributes to redox potential value | ||||
Sequence: G | ||||||
Site | 306 | Contributes to redox potential value | ||||
Sequence: P | ||||||
Active site | 307 | Nucleophile | ||||
Sequence: C |
GO annotations
all annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | histone deacetylase complex | |
Molecular Function | Hsp70 protein binding | |
Molecular Function | identical protein binding | |
Molecular Function | oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor | |
Molecular Function | protein dimerization activity | |
Biological Process | heat acclimation | |
Biological Process | protein complex oligomerization | |
Biological Process | protein folding |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameTPR repeat-containing thioredoxin TDX
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ8VWG7
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Disruption phenotype
High sensitivity to heat shock.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 304 | Loss of disulfide reductase activity. | ||||
Sequence: C → S | ||||||
Mutagenesis | 307 | Loss of disulfide reductase activity. | ||||
Sequence: C → S |
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.
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylvaline | ||||
Sequence: V | ||||||
Chain | PRO_0000394548 | 2-380 | TPR repeat-containing thioredoxin TDX | |||
Sequence: VDAIQVAELRRFVEQLKLNPSILHDPSLVFFKEYLRSLGAQVPKIEKTERDYEDKAETKPSFSPKHDDDDDDIMESDVELDNSDVVEPDNEPPQPMGDPTAEVTDENRDDAQSEKSKAMEAISDGRFDEAIEHLTKAVMLNPTSAILYATRASVFLKVKKPNAAIRDANVALQFNSDSAKGYKSRGMAKAMLGQWEEAAADLHVASKLDYDEEIGTMLKKVEPNAKRIEEHRRKYQRLRKEKELQRAERERRKQQEAQEREAQAALNDGEVISIHSTSELEAKTKAAKKASRLLILYFTATWCGPCRYMSPLYSNLATQHSRVVFLKVDIDKANDVAASWNISSVPTFCFIRDGKEVDKVVGADKGSLEQKIAQHSSSK | ||||||
Disulfide bond | 304↔307 | Redox-active | ||||
Sequence: CGPC |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Oligomerization under high temperature.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8VWG7 | TDX Q8VWG7 | 5 | EBI-15764744, EBI-15764744 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, repeat, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 49-70 | Basic and acidic residues | ||||
Sequence: TERDYEDKAETKPSFSPKHDDD | ||||||
Region | 49-115 | Disordered | ||||
Sequence: TERDYEDKAETKPSFSPKHDDDDDDIMESDVELDNSDVVEPDNEPPQPMGDPTAEVTDENRDDAQSE | ||||||
Compositional bias | 71-87 | Acidic residues | ||||
Sequence: DDDIMESDVELDNSDVV | ||||||
Repeat | 112-145 | TPR 1 | ||||
Sequence: AQSEKSKAMEAISDGRFDEAIEHLTKAVMLNPTS | ||||||
Repeat | 147-179 | TPR 2 | ||||
Sequence: ILYATRASVFLKVKKPNAAIRDANVALQFNSDS | ||||||
Repeat | 181-213 | TPR 3 | ||||
Sequence: KGYKSRGMAKAMLGQWEEAAADLHVASKLDYDE | ||||||
Compositional bias | 240-260 | Basic and acidic residues | ||||
Sequence: RKEKELQRAERERRKQQEAQE | ||||||
Region | 240-265 | Disordered | ||||
Sequence: RKEKELQRAERERRKQQEAQEREAQA | ||||||
Domain | 252-378 | Thioredoxin | ||||
Sequence: RRKQQEAQEREAQAALNDGEVISIHSTSELEAKTKAAKKASRLLILYFTATWCGPCRYMSPLYSNLATQHSRVVFLKVDIDKANDVAASWNISSVPTFCFIRDGKEVDKVVGADKGSLEQKIAQHSS |
Sequence similarities
Belongs to the thioredoxin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
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.
- Name1
- Length380
- Mass (Da)42,846
- Last updated2002-03-01 v1
- ChecksumC0181F1D74CD3AA4
Q8VWG7-2
- Name2
- Differences from canonical
- 50-56: Missing
Sequence caution
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 49-70 | Basic and acidic residues | ||||
Sequence: TERDYEDKAETKPSFSPKHDDD | ||||||
Alternative sequence | VSP_039289 | 50-56 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 71-87 | Acidic residues | ||||
Sequence: DDDIMESDVELDNSDVV | ||||||
Compositional bias | 240-260 | Basic and acidic residues | ||||
Sequence: RKEKELQRAERERRKQQEAQE | ||||||
Sequence conflict | 324 | in Ref. 5; AAM60989 | ||||
Sequence: V → F |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |