P22217 |
UniProt ID : |
P22217 |
NCBI Taxonomy : |
559292 |
Protein names : |
Thioredoxin-1 |
Organism : |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) |
Taxonomy : |
Eukaryota |
Subcellular locations : | Cytoplasm;Golgi apparatus membrane;Mitochondrion intermembrane space;Nucleus; |
Length : |
103 |
Gene Ontology : | GO ID | Ontology | Definition | Evidence | GO:0005829 | Cellular Component | cytosol | IDA | GO:0000324 | Cellular Component | fungal-type vacuole | IPI | GO:0000139 | Cellular Component | Golgi membrane | IEA | GO:0005758 | Cellular Component | mitochondrial intermembrane space | IDA | GO:0005634 | Cellular Component | nucleus | IEA | GO:0015036 | Molecullar Function | disulfide oxidoreductase activity | IDA | GO:0009055 | Molecullar Function | electron carrier activity | IEA | GO:0015035 | Molecullar Function | protein disulfide oxidoreductase activity | IEA | GO:0045454 | Biological Process | cell redox homeostasis | TAS | GO:0034599 | Biological Process | cellular response to oxidative stress | ISS | GO:0009263 | Biological Process | deoxyribonucleotide biosynthetic process | IEA | GO:0006888 | Biological Process | ER to Golgi vesicle-mediated transport | IDA | GO:0006662 | Biological Process | glycerol ether metabolic process | IEA | GO:0080058 | Biological Process | protein deglutathionylation | IDA | GO:0015031 | Biological Process | protein transport | IEA | GO:0006890 | Biological Process | retrograde vesicle-mediated transport, Golgi to ER | IDA | GO:0042144 | Biological Process | vacuole fusion, non-autophagic | IDA | GO:0000011 | Biological Process | vacuole inheritance | IMP | |
SWISS-MODEL Repository : | P22217 |
Sequences : |
MVTQFKTASEFDSAIAQDKLVVVDFYATWCGPCKMIAPMIEKFSEQYPQADFYKLDVDELGDVAQKNEVSAMPTLLLFKNGKEVAKVVGANPAAIKQAIAANA |
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. |