Voltage-dependent anion-selective channel protein 2
Domain
Consists mainly of a membrane-spanning beta-barrel formed by 19 beta-strands.
Function
Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules (PubMed:38065946). The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV (By similarity). The open state has a weak anion selectivity whereas the closed state is cation-selective (By similarity). Binds various lipids, including the sphingolipid ceramide, the phospholipid phosphatidylcholine, and the sterols cholesterol and oxysterol (PubMed:31015432). Binding of ceramide promotes the mitochondrial outer membrane permeabilization (MOMP) apoptotic pathway (PubMed:31015432).
Catalyzes the scrambling of phospholipids across the outer mitochondrial membrane; the mechanism is unrelated to channel activity and is capable of translocating both anionic and zwitterionic phospholipids.
Post-translational modifications
Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30.
Sequence Similarities
Belongs to the eukaryotic mitochondrial porin family.
Tissue Specificity
Expressed in erythrocytes (at protein level) (PubMed:27641616). Expressed in all tissues examined (PubMed:8420959).
Cellular localization
- Mitochondrion outer membrane
- Membrane
- May localize to non-mitochondrial membranes.
Alternative names
Voltage-dependent anion-selective channel protein 2, VDAC-2, hVDAC2, Outer mitochondrial membrane protein porin 2, VDAC2