Voltage-dependent anion channel
| Eukaryotic porin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
Crystal Structure of the Human Voltage-Dependent Anion Channel. The arrows denote the antiparallel beta sheets that form the characteristic beta-barrel | |||||||||
| Identifiers | |||||||||
| Symbol | Porin_3 | ||||||||
| Pfam | PF01459 | ||||||||
| InterPro | IPR001925 | ||||||||
| PROSITE | PDOC00483 | ||||||||
| TCDB | 1.B.8 | ||||||||
| OPM superfamily | 189 | ||||||||
| OPM protein | 3emn | ||||||||
| CDD | cd07306 | ||||||||
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Voltage-dependent anion channels, or mitochondrial porins, are a class of porin ion channel located on the outer mitochondrial membrane. There is debate as to whether or not this channel is expressed in the cell surface membrane.
This major protein of the outer mitochondrial membrane of eukaryotes forms a voltage-dependent anion-selective channel (VDAC) that behaves as a general diffusion pore for small hydrophilic molecules. The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30–40 mV. VDAC facilitates the exchange of ions and molecules between mitochondria and cytosol and is regulated by the interactions with other proteins and small molecules.