InterPro domain: IPR019133

Mitofilin (also known as MICOS complex subunit MIC60) is a component of the MICOS complex which controls mitochondrial cristae morphology, maintenance of junctions, inner membrane architecture, and formation of contact sites to the outer membrane [ 1 , 2 ]. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex [ 3 ]. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence (residues 1-43) rich in positive-charged and hydroxylated residues and a membrane anchor domain (residues 47-66). In addition, it has three centrally located coiled coil domains (residues 200-240, 280-310 and 400-420) [ 4 ].

1. MINOS1 is a conserved component of mitofilin complexes and required for mitochondrial function and cristae organization. Mol. Biol. Cell 23, 247-57
2. Detailed analysis of the human mitochondrial contact site complex indicate a hierarchy of subunits. PLoS ONE 10, e0120213
3. Molecular characterization of mitofilin (HMP), a mitochondria-associated protein with predicted coiled coil and intermembrane space targeting domains. J. Cell. Sci. 109 ( Pt 9), 2253-64
4. The mitochondrial inner membrane protein mitofilin controls cristae morphology. Mol. Biol. Cell 16, 1543-54