domain:Consists mainly of a membrane-spanning beta-barrel formed by 19 beta-strands. The helical N-terminus folds back into the pore opening and plays a role in voltage-gated channel activity.,function:Forms a channel through the mitochondrial outer membrane and also the plasma membrane. The channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules; in the plasma membrane it is involved in cell volume regulation and apoptosis. It adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective. May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis.,similarity:Belongs to the eukaryotic mitochondrial porin family.,subunit:Interacts with hexokinases (By similarity). Interacts with BCL2L1. Interacts with influenza A virus PB1-F2 protein.,tissue specificity:Heart, liver and skeletal muscle.,
Mitochondrion outer membrane ; Multi-pass membrane protein . Cell membrane ; Multi-pass membrane protein . Membrane raft ; Multi-pass membrane protein .
Expressed in erythrocytes (at protein level) (PubMed:27641616). Expressed in heart, liver and skeletal muscle (PubMed:8420959).