P22217 · TRX1_YEAST
- ProteinThioredoxin-1
- GeneTRX1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids103 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Participates as a hydrogen donor in redox reactions through the reversible oxidation of its active center dithiol to a disulfide, accompanied by the transfer of 2 electrons and 2 protons. It is involved in many cellular processes, including deoxyribonucleotide synthesis, repair of oxidatively damaged proteins, protein folding, sulfur metabolism, and redox homeostasis. Thioredoxin-dependent enzymes include phosphoadenosine-phosphosulfate reductase MET16, alkyl-hydroperoxide reductase DOT5, thioredoxin peroxidases TSA1 and TSA2, alkyl hydroperoxide reductase AHP1, and peroxiredoxin HYR1. Thioredoxin is also involved in protection against reducing stress. As part of the LMA1 complex, it is involved in the facilitation of vesicle fusion such as homotypic vacuole and ER-derived COPII vesicle fusion with the Golgi. This activity does not require the redox mechanism.
Miscellaneous
Present with 8579 molecules/cell in log phase SD medium.
Yeast has two cytoplasmic thioredoxins, TRX1 and TRX2, and one mitochondrial, TRX3.
Features
Showing features for site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 24 | Deprotonates C-terminal active site Cys | ||||
Sequence: D | ||||||
Active site | 30 | Nucleophile | ||||
Sequence: C | ||||||
Site | 31 | Contributes to redox potential value | ||||
Sequence: G | ||||||
Site | 32 | Contributes to redox potential value | ||||
Sequence: P | ||||||
Active site | 33 | Nucleophile | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | fungal-type vacuole | |
Cellular Component | Golgi membrane | |
Cellular Component | membrane fusion priming complex | |
Cellular Component | mitochondrial intermembrane space | |
Cellular Component | mitochondrion | |
Cellular Component | nucleus | |
Molecular Function | disulfide oxidoreductase activity | |
Molecular Function | protein-disulfide reductase activity | |
Biological Process | cell redox homeostasis | |
Biological Process | deoxyribonucleotide biosynthetic process | |
Biological Process | endoplasmic reticulum to Golgi vesicle-mediated transport | |
Biological Process | protein transport | |
Biological Process | retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum | |
Biological Process | vacuole fusion, non-autophagic | |
Biological Process | vacuole inheritance |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameThioredoxin-1
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP22217
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Golgi apparatus membrane ; Peripheral membrane protein
Keywords
- Cellular component
PTM/Processing
Features
Showing features for initiator methionine, chain, disulfide bond, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000120044 | 2-103 | Thioredoxin-1 | |||
Sequence: VTQFKTASEFDSAIAQDKLVVVDFYATWCGPCKMIAPMIEKFSEQYPQADFYKLDVDELGDVAQKNEVSAMPTLLLFKNGKEVAKVVGANPAAIKQAIAANA | ||||||
Disulfide bond | 30↔33 | Redox-active | ||||
Sequence: CGPC | ||||||
Cross-link | 54 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 66 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 96 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K |
Post-translational modification
Reversible disulfide bond formation between Cys-30 and Cys-33, reverted by thioredoxin reductase TRR1 using NADPH as hydrogen donor.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Monomer. Part of the heterodimeric LMA1 complex together with the proteinase inhibitor PBI2. Most of the thioredoxin of yeast is in this complex rather than the well-studied monomer. LMA1 binds to the ATPase SEC18.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P22217 | TRX2 P22803 | 3 | EBI-19607, EBI-19598 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-103 | Thioredoxin | ||||
Sequence: VTQFKTASEFDSAIAQDKLVVVDFYATWCGPCKMIAPMIEKFSEQYPQADFYKLDVDELGDVAQKNEVSAMPTLLLFKNGKEVAKVVGANPAAIKQAIAANA |
Sequence similarities
Belongs to the thioredoxin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length103
- Mass (Da)11,235
- Last updated2007-01-23 v3
- Checksum87A19FBBBDB20CF5
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M59169 EMBL· GenBank· DDBJ | AAA35171.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M62647 EMBL· GenBank· DDBJ | AAA35177.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z73215 EMBL· GenBank· DDBJ | CAA97572.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY558203 EMBL· GenBank· DDBJ | AAS56529.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006945 EMBL· GenBank· DDBJ | DAA09361.1 EMBL· GenBank· DDBJ | Genomic DNA |