Glycosylphosphatidylinositol anchor attachment 1 protein (GPAA1)

Glycosylphosphatidylinositol anchor attachment 1 protein (GPAA1) is a core subunit of the GPI transamidase complex, which catalyzes the covalent attachment of a glycosylphosphatidylinositol (GPI) lipid anchor to specific proteins during post-translational modification in the endoplasmic reticulum. This process is essential for anchoring many proteins to the cell surface and is broadly required for normal cellular function. GPAA1 is a metallo-peptide-synthetase of the M28 family, likely binding a zinc ion, and helps form the structural and enzymatic core of the transamidase complex together with partners such as PIG-K and PIG-T[1][2][4]. The GPAA1 gene is ubiquitously expressed in human tissues, and mutations are linked to GPI biosynthesis defects causing congenital and neuromuscular disorders[4]. GPAA1 interacts closely with other GPI transamidase subunits, facilitating the transfer and covalent attachment of the GPI-anchor to the ω-site of substrate proteins[1][2][3][4]. There are no current therapeutic drugs or inhibitors directly targeting GPAA1 for clinical use, but its essential role in GPI-anchor biosynthesis makes it a potential target for future drug discovery, especially for infectious diseases involving GPI-anchored proteins[1].

Other names

GPI-anchor transamidase component GPAA1GPI anchor attachment protein 1GAA1hGAA1GPAA1P anchor attachment protein 1 homologGPI transamidase subunitGPIBD15glycophosphatidylinositol anchor attachment 1 protein