Outer mitochondrial translocase required to remove mislocalized tail-anchored transmembrane proteins on mitochondria (By similarity). Specifically recognizes and binds tail-anchored transmembrane proteins: acts as a dislocase that mediates the ATP-dependent extraction of mistargeted tail-anchored transmembrane proteins from the mitochondrion outer membrane (By similarity). Also plays a critical role in regulating the surface expression of AMPA receptors (AMPAR), thereby regulating synaptic plasticity and learning and memory (PubMed:21496646). Required for NMDA-stimulated AMPAR internalization and inhibition of GRIA1 and GRIA2 recycling back to the plasma membrane; these activities are ATPase-dependent (PubMed:21496646). [protein]-with a C-terminal TM segment(out) + ATP + H2O = [protein]-with a C-terminal TM segment(in) + ADP + H(+) + phosphate Interacts with GRIA2 and GRIP1 in an ATP-dependent manner (PubMed:21496646). ATAD1-catalyzed ATP hydrolysis disrupts not only its binding to GRIA2 and GRIP1, but also interaction between GRIP1 and GRIA2, leading to AMPAR complex disassembly (PubMed:21496646). Widely expressed with the highest expression in the brain and testis. In the brain, relatively high expression in hippocampal CA1 pyramidal cells (at protein level). About 80% of the mutant mice die of a seizure-like syndrome between postnatal days 19 and 25; the remaining 20% survive up to 8 weeks of age. No gross abnormalities in tissues analyzed, including heart, lung, spleen, kidney, thymus, liver, intestine, testis, eyes, and muscle. In the CA1 region of the hippocampus, no substantial difference in the dendritic complexity or in the number or size of dendritic spines and normal density of synapses in mutant animals compared to wild-type. Belongs to the AAA ATPase family. MSP1 subfamily.