POR1
Domain
Consists mainly of membrane-spanning sided beta-sheets. 19 strands distributed along the entire VDAC protein, have the potential to adopt transmembrane beta pleated sheet structures, which rolled together may form a 'beta-barrel' type structure, possessing pore dimensions.
Function
Non-selective voltage-gated ion channel that mediates the transport of anions and cations through the mitochondrion outer membrane (PubMed:9435273). The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV (PubMed:9435273). The open state has a weak anion selectivity whereas the closed state is cation-selective (PubMed:9435273). Is the major permeability factor of the mitochondrial outer membrane (PubMed:9435273).
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.
Sequence Similarities
Belongs to the eukaryotic mitochondrial porin family.
Cellular localization
- Mitochondrion outer membrane
Alternative names
OMP2, VDAC1, YNL055C, N2441, YNL2441C, POR1, Non-selective voltage-gated ion channel 1, Outer mitochondrial membrane protein porin 1, Voltage-dependent anion-selective channel protein 1, VDAC-1