FKBP8
Function
Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis. Involved in the inhibition of viral infection by influenza A viruses (IAV) (PubMed:28169297).
Post-translational modifications
Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30.
Tissue Specificity
Widely expressed. Highest levels seen in the brain. Highly abundant in the retina.
Cellular localization
- Mitochondrion
- Mitochondrion membrane
- Single-pass membrane protein
- Cytoplasmic side
- Isoform 1
- Mitochondrion membrane
- Single-pass membrane protein
- Cytoplasmic side
- Isoform 3
- Mitochondrion membrane
- Single-pass membrane protein
- Cytoplasmic side
Alternative names
FKBP38, FKBP8, Peptidyl-prolyl cis-trans isomerase FKBP8, PPIase FKBP8, 38 kDa FK506-binding protein, FK506-binding protein 8, FKBPR38, Rotamase, 38 kDa FKBP, FKBP-38, hFKBP38, FKBP-8