Glutaredoxin 2 (GLRX2)

The predicted GLRX2A and GLRX2B proteins contain 164 and 165 amino acids, respectively, and both have molecular masses of approximately 18.1 kD. Each protein has a conserved active site, a glutathione-binding domain, a hydrophobic surface area, and a putative nuclear translocation signal. GLRX2A and GLRX2B differ in their N-terminal sequences, with GLRX2B lacking an N-terminal mitochondrial translocation signal found in GLRX2A. The GLRX2 proteins share 34% sequence identity with GLRX1 and about 70% sequence similarity with the rat and mouse sequences.A transcript of about 8 kb was also found in all tissues. Western blot analysis of fractionated human leukemic cells determined that GLRX2 localizes as a 16- to 18-kD protein in the nuclear and mitochondrial fractions, but not in cytoplasmic fractions.