GLRX3
Domain
The thioredoxin domain lacks the two redox-active cysteines. This strongly suggests that it lacks thioredoxin activity.
Function
Together with BOLA2, acts as a cytosolic iron-sulfur (Fe-S) cluster assembly factor that facilitates [2Fe-2S] cluster insertion into a subset of cytosolic proteins (PubMed:26613676, PubMed:27519415). Acts as a critical negative regulator of cardiac hypertrophy and a positive inotropic regulator (By similarity). Required for hemoglobin maturation (PubMed:23615448). Does not possess any thyoredoxin activity since it lacks the conserved motif that is essential for catalytic activity.
Tissue Specificity
Expressed in heart, spleen, testis and, to a lower extent, in thymus and peripheral blood leukocytes. Weakly expressed in lung, placenta, colon and small intestine.
Cellular localization
- Cytoplasm
- Cytosol
- Cytoplasm
- Cell cortex
- Cytoplasm
- Myofibril
- Sarcomere
- Z line
- Under the plasma membrane (By similarity). After PMA stimulation, GLRX3 and PRKCQ/PKC-theta translocate to a more extended submembrane area (By similarity). In the Z line, found associated with CSRP3 (By similarity).
Alternative names
PICOT, TXNL2, HUSSY-22, GLRX3, Glutaredoxin-3, PKC-interacting cousin of thioredoxin, PKC-theta-interacting protein, Thioredoxin-like protein 2, PKCq-interacting protein