MOAP1
Domain
The protein is evolutionarily related to retrotransposon Gag proteins: it contains the capsid (CA)subdomain of gag.
The BH3-like domain is required for association with BAX and for mediating apoptosis (PubMed:11060313). The three BH domains (BH1, BH2, and BH3) of BAX are all required for mediating protein-protein interaction (PubMed:11060313).
The LIR motif (LC3-interacting region) is required for the interaction with the ATG8 family proteins MAP1LC3A, MAP1LC3B and MAP1LC3C.
Function
Retrotransposon-derived protein that forms virion-like capsids (By similarity). Acts as an effector of BAX during apoptosis: enriched at outer mitochondria membrane and associates with BAX upon induction of apoptosis, facilitating BAX-dependent mitochondrial outer membrane permeabilization and apoptosis (PubMed:11060313, PubMed:16199525). Required for death receptor-dependent apoptosis (PubMed:11060313). When associated with RASSF1, promotes BAX conformational change and translocation to mitochondrial membranes in response to TNF and TNFSF10 stimulation (PubMed:15949439). Also promotes autophagy: promotes phagophore closure via association with ATG8 proteins (PubMed:33783314). Acts as an inhibitor of the NFE2L2/NRF2 pathway via interaction with SQSTM1: interaction promotes dissociation of SQSTM1 inclusion bodies that sequester KEAP1, relieving inactivation of the BCR(KEAP1) complex (PubMed:33393215).
Post-translational modifications
Ubiquitinated and degraded during mitotic exit by APC/C-Cdh1, this modification is inhibited by TRIM39.
Sequence Similarities
Belongs to the PNMA family.
Tissue Specificity
Widely expressed, with high levels in heart and brain.
Cellular localization
- Cytoplasm
- Cytosol
- Mitochondrion outer membrane
- Extracellular vesicle membrane
- Forms virion-like extracellular vesicles that are released from cells.
Alternative names
PNMA4, MOAP1, Modulator of apoptosis 1, MAP-1, MAP1, Paraneoplastic antigen Ma4