Human MOAP1 gene contains three exons and the encoding sequence of 1056 bases is in the exon 3.

MOAP1 is a 351 amino-acid long protein.

No reported pseudogenes.

MOAP1 is a short-lived protein with a half-life of 25 minutes. It is degraded by the ubiquitin-proteosome system (Fu et al., 2007).

MOAP-1 is a 351 amino-acid long protein with a molecular mass of 39.5 kDa. Isoelectric point (pI) of MOAP-1 is 4.939 at pH 7.0. MOAP-1 contains a BH3 (Bcl-2 homology 3) like domain required for homodimerization and interaction with Bcl-2 associated X (Bax) protein. Under normal condition, MOAP1 is held as an inactive conformation through intramolecular interactions. Interaction between RASSF1A (ras-association domain family 1, isoform A) and MOAP1 reduces the inhibitory intramolecular interaction of MOAP1 and allows MOAP1 through the BH3 like domain to bind Bax (Baksh et al., 2005).

MOAP1 is expressed in the adipose, adrenal, blood, brain, breast, colon and heart. MOAP1 is expressed in higher level in the heart and brain.

MOAP-1 protein localizes in the cytoplasm (Law, 2012) and also seen in the mitochondria (Tan et al., 2005).

MOAP1 is a BH3-like protein that acts as a pro-apoptotic molecule (Tan et al., 2001). When overexpressed, MOAP1 induces caspase-dependent apoptosis in mammalian cells (Tan et al., 2005). Studies showed that TNFα stimulation recruits RASSF1A and MOAP1 to death receptors complexes. This recruitment leads to the association of RASSF1A with MOAP1 and to the induction of a conformational change in MOAP1. This results in the opening of the BH3 domain to allow MOAP1 to interact with Bax. Bax is subsequently inserted into the mitochondrial membrane leading to apoptosis (Baksh et al., 2005; Foley et al., 2008).

Also highly conserved in rat (Rattus norvegicus) and mouse (Mus musculus), human MOAP1 protein shares 99% amino acids identity with that of chimpanzee (Pan troglodytes) (Law et al., 2012).

Gene mutations have not been described yet.