Immunogen sequence: IQDYLQQLTGA RTVPRVFIGK DCIGGCSDLV S
Highest antigen sequence identity to the following orthologs - mouse 97%, rat 97%.
GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 (GLRX) and GRX2, which are members of this subfamily. Also included in this subfamily are the N-terminal GRX domains of proteins similar to human thioredoxin reductase 1 and 3.
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Protein Aliases: Glrx; Glrx1; Glutaredoxin; glutaredoxin (thioltransferase); Glutaredoxin-1; Glutaredoxin1; Grx 1; Grx1; MGC117; thioltransferase; Thioltransferase-1; TTase-1
Gene Aliases: GLRX; GRX; GRX1
UniProt ID: (Human) P35754
Entrez Gene ID: (Human) 2745
Molecular Function: oxidoreductase