BNIP3L

This gene encodes a protein that belongs to the pro-apoptotic subfamily within the Bcl-2 family of proteins. The encoded protein binds to Bcl-2 and possesses the BH3 domain. The protein directly targets mitochondria and causes apoptotic changes, including loss of membrane potential and the release of cytochrome c.

BCL2 interacting protein 3 like

Induces apoptosis. Interacts with viral and cellular anti-apoptosis proteins. Can overcome the suppressors BCL-2 and BCL-XL, although high levels of BCL-XL expression will inhibit apoptosis. Inhibits apoptosis induced by BNIP3. Involved in mitochondrial quality control via its interaction with SPATA18/MIEAP: in response to mitochondrial damage, participates in mitochondrial protein catabolic process (also named MALM) leading to the degradation of damaged proteins inside mitochondria. The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix. May function as a tumor suppressor.

Cellular response to hypoxia Source: MGI
Defense response to virus Source: UniProtKB
Mitochondrial outer membrane permeabilization Source: GO_Central
Mitochondrial protein catabolic process Source: UniProtKB
Negative regulation of apoptotic process Source: UniProtKB
Negative regulation of cell death Source: MGI
Negative regulation of mitochondrial membrane potential Source: Ensembl
Positive regulation of apoptotic process Source: UniProtKB
Positive regulation of macroautophagy Source: MGI
Regulation of apoptotic process Source: Reactome
Regulation of autophagy of mitochondrion Source: Ensembl
Regulation of programmed cell death Source: GO_Central
Regulation of protein targeting to mitochondrion Source: Ensembl
Viral process Source: UniProtKB-KW

Mitochondrion outer membrane; Endoplasmic reticulum; Nucleus envelope; Membrane. Colocalizes with SPATA18 at the mitochondrion outer membrane.

Helical: 188-208 aa

Undergoes progressive proteolysis to an 11 kDa C-terminal fragment, which is blocked by the proteasome inhibitor lactacystin.