O89049
uniprot
O89049
canonical
amino_acid_sequence
MNDSKDAPKSYDFDLIIIGGGSGGLAAAKEAAKFDKKVMVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKLEDTVKHDWEKMTESVQNHIGSLNWGYRVALREKKVVYENAYGKFIGPHKIMATNNKGKEKVYSAERFLIATGERPRYLGIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDMANKIGEHMEEHGIKFIRQFVPTKIEQIEAGTPGRLKVTAKSTNSEETIEDEFNTVLLAVGRDSCTRTIGLETVGVKINEKTGKIPVTDEEQTNVPYIYAIGDILEGKLELTPVAIQAGRLLAQRLYGGSTVKCDYDNVPTTVFTPLEYGCCGLSEEKAVEKFGEENIEVYHSFFWPLEWTVPSRDNNKCYAKVICNLKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKQQLDSTIGIHPVCAEIFTTLSVTKRSGGDILQSGCUG
uniprot
proteins
ec_number
1.11.1.2
uniprot
proteins
ec_number
1.8.1.9
uniprot
proteins
function
FUNCTION: Reduces disulfide protein thioredoxin (Trx) to its dithiol-containing form. Homodimeric flavoprotein involved in the regulation of cellular redox reactions, growth and differentiation. A selenocysteine residue at the C-terminal active site is essential for catalysis (PubMed:10849437). Also has reductase activity on hydrogen peroxide (H2O2) (PubMed:10849437). {ECO:0000269|PubMed:10849437}.
uniprot
proteins
mass_dalton
54671
uniprot
proteins
mutagenesis
MUTAGEN 498; /note="U->S: Loss of activity."; /evidence="ECO:0000269|PubMed:10849437"; MUTAGEN 498; /note="Missing: Loss of activity."; /evidence="ECO:0000269|PubMed:10849437
uniprot
proteins
post_translational_modification
PTM: ISGylated. {ECO:0000250|UniProtKB:Q16881}.
uniprot
proteins
protein_family
Class-I pyridine nucleotide-disulfide oxidoreductase family
uniprot
proteins
pubmed
10333487
uniprot
proteins
pubmed
10849437
uniprot
proteins
pubmed
11481439
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
9535831
uniprot
proteins
sequence_length
499
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16881}.
uniprot
proteins