Endoplasmic reticulum P5A-ATPase (ATP13A1)

Endoplasmic reticulum P5A-ATPase (ATP13A1) is an evolutionarily conserved P-type ATPase enzyme localized in the endoplasmic reticulum (ER) membrane[2][1][3][6]. It functions as a protein dislocase, removing mislocalized mitochondrial tail-anchored proteins and substrates with misoriented N-terminal transmembrane domains from the ER, thus maintaining proteome quality and correct protein topogenesis[1][2][6][4]. ATP13A1 also contributes to cellular manganese ion homeostasis by mediating manganese transport into the ER, affecting various manganese-dependent processes[3][5]. Dysfunction or absence of ATP13A1 impairs protein folding, increases ER stress, disrupts manganese homeostasis, and may predispose to neurodegenerative diseases[5][6][3]. It is part of the P5A subfamily of P-type ATPases and is not currently known to be the direct target of any approved therapeutics or drugs.

Other names

ATP13AKIAA1825FLJ31858CGI-152endoplasmic reticulum transmembrane helix translocasemanganese-transporting ATPase 13A1probable cation-transporting ATPase 13A1

ATP-driven transport (of cations, especially manganese) and protein dislocation/removal based on substrate recognition; maintains protein and ion homeostasis in the ER