O97508 · THIO_HORSE
- ProteinThioredoxin
- GeneTXN
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids105 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions (By similarity).
Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity (By similarity).
Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity (By similarity).
Features
Showing features for site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 26 | Deprotonates C-terminal active site Cys | ||||
Sequence: D | ||||||
Active site | 32 | Nucleophile | ||||
Sequence: C | ||||||
Site | 33 | Contributes to redox potential value | ||||
Sequence: G | ||||||
Site | 34 | Contributes to redox potential value | ||||
Sequence: P | ||||||
Active site | 35 | Nucleophile | ||||
Sequence: C |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | extracellular region | |
Cellular Component | nucleus | |
Molecular Function | protein-disulfide reductase activity | |
Biological Process | positive regulation of DNA binding | |
Biological Process | response to radiation |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameThioredoxin
- Short namesTrx
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Perissodactyla > Equidae > Equus
Accessions
- Primary accessionO97508
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: Translocates from the cytoplasm into the nucleus after phorbol 12-myristate 13-acetate induction (PMA). Predominantly in the cytoplasm in non irradiated cells. Radiation induces translocation of TRX from the cytoplasm to the nucleus. Secreted by a leaderless secretory pathway.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000120004 | 1-105 | Thioredoxin | |||
Sequence: MVKQIESKSAFQEALNSAGEKLVVVDFSATWCGPCKMIKPFFHSLSEKYSNVVFLEVDVDDCQDVAAECEVKCMPTFQFFKKGQKVDEFSGANKEKLEATIKGLI | ||||||
Modified residue | 3 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 8 | N6-succinyllysine | ||||
Sequence: K | ||||||
Disulfide bond | 32↔35 | Redox-active | ||||
Sequence: CGPC | ||||||
Modified residue | 39 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 62 | S-nitrosocysteine | ||||
Sequence: C | ||||||
Modified residue | 69 | S-nitrosocysteine | ||||
Sequence: C | ||||||
Modified residue | 73 | S-nitrosocysteine; alternate | ||||
Sequence: C | ||||||
Disulfide bond | 73 | Interchain; alternate | ||||
Sequence: C | ||||||
Modified residue | 94 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 94 | N6-succinyllysine; alternate | ||||
Sequence: K |
Post-translational modification
In the fully reduced protein, both Cys-69 and Cys-73 are nitrosylated in response to nitric oxide (NO). When two disulfide bonds are present in the protein, only Cys-73 is nitrosylated. Cys-73 can serve as donor for nitrosylation of target proteins (By similarity).
Keywords
- PTM
Proteomic databases
Expression
Gene expression databases
Interaction
Subunit
Homodimer; disulfide-linked. Interacts with TXNIP through the redox-active site. Interacts with MAP3K5 and CASP3. Interacts with APEX1; the interaction stimulates the FOS/JUN AP-1 DNA-binding activity in a redox-dependent manner (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-103 | Thioredoxin | ||||
Sequence: VKQIESKSAFQEALNSAGEKLVVVDFSATWCGPCKMIKPFFHSLSEKYSNVVFLEVDVDDCQDVAAECEVKCMPTFQFFKKGQKVDEFSGANKEKLEATIKG |
Sequence similarities
Belongs to the thioredoxin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length105
- Mass (Da)11,737
- Last updated2007-01-23 v3
- Checksum04F9E35DAABFB5C4
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB022431 EMBL· GenBank· DDBJ | BAA37154.1 EMBL· GenBank· DDBJ | mRNA |