The ArsA Arsenite Transporter, ATP-Binding, Homolog 1 is a human recombinant protein that plays a crucial role in cellular processes, particularly in the context of arsenic resistance and protein targeting within cells. This protein is encoded by the ASNA1 gene, which is the human homolog of the bacterial arsA gene .
The ASNA1 gene is located on chromosome 19p13.13 and encodes a protein consisting of 332 amino acids . The protein has an N-terminal ATP-binding cassette (ABC) domain and a C-terminal domain of unknown function . The gene is ubiquitously expressed in various tissues, indicating its fundamental role in cellular physiology .
The ArsA protein functions as an ATPase that is involved in the transport of arsenite, a toxic metalloid, out of cells. This activity is crucial for cellular resistance to arsenicals . In bacteria, the ArsA ATPase is part of a multisubunit oxyanion pump responsible for resistance to arsenicals and antimonials .
In humans, the ArsA protein is also a central component of the transmembrane domain (TMD) recognition complex (TRC), specifically known as TRC40 . This complex is involved in the post-translational delivery of tail-anchored (TA) proteins from the cytosol to the endoplasmic reticulum (ER) . The ArsA protein recognizes and selectively binds the TMD of TA proteins in the cytosol and delivers them to the ER for insertion .
The ability of ArsA to transport arsenite and its role in the TRC40 complex highlight its importance in both detoxification processes and protein targeting within cells . The ATPase activity of ArsA is regulated by ATP binding and hydrolysis, which drives the homodimer towards the closed dimer state, facilitating the recognition of newly synthesized TA membrane proteins .