Subunit of the integral membrane V0 complex of vacuolar ATPase. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system. In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation (By similarity).

(UniProt, Q9W4P5)

Eye color brown with whitish highlights. Paler than se, less purplish than pn. In cho2 2-amino-4-hydroxypterine absent; isoxanthopterin II present in excess (McKay, 1972, DIS 48: 62). Malpighian tubes of larvae and adults contain brown pigment like red. Larvae easily distinguished from wild type. Malpighian tube color autonomous in mosaic larvae [Falk, Orevi, and Menzel, 1973, Nature (London) New Biol. 246: 19-20]. Brown pigment of Malpighian tubes absent when cho is combined with v, cn, or st, mutations which prevent formation of brown eye pigment. Eye color of cho v is yellowish, but cho g cannot be distinguished from g. Separability, viability, and fertility excellent. RK1.