Predicted to enable ATPase binding activity. Involved in several processes, including collagen and cuticulin-based cuticle development; exosomal secretion; and multicellular organismal-level water homeostasis. Located in apical plasma membrane; cell body membrane; and cytoplasmic vesicle. Part of vacuolar proton-transporting V-type ATPase complex. Is expressed in several structures, including excretory cell; hypodermis; neuronal sheath cell; rectum; and vulva. Human ortholog(s) of this gene implicated in autosomal recessive cutis laxa type IIA; autosomal recessive osteopetrosis 1; developmental and epileptic encephalopathy 104; renal tubular acidosis; and wrinkly skin syndrome. Orthologous to several human genes including ATP6V0A1 (ATPase H+ transporting V0 subunit a1); ATP6V0A2 (ATPase H+ transporting V0 subunit a2); and ATP6V0A4 (ATPase H+ transporting V0 subunit a4).
WB Description
vha-5 encodes an ortholog of subunit a of the membrane-bound (V0) domainof vacuolar proton-translocating ATPase (V-ATPase); VHA-5 is orthologousto human ATP6N1A (OMIM:192130), ATP6V0A2, ATP6V0A4 (OMIM:605239, mutatedin distal renal tubular acidosis), and TCIRG1 (OMIM:604592, mutated inosteopetrosis); VHA-5 is expressed broadly in embryos (in dot- orcup-like perinuclear compartments in each cell), and in thepostembryonic pharynx, excretory cell, and epidermal syncytium; VHA-5 isrequired for survival past the L2 larval stage; VHA-5 is required forosmoregulation, since vha-5(mc38) die as fluid-filled L1 larvae; VHA-5is also required for apical secretion of the hedgehog-like proteinsWRT-2 and -8, and this requirement is genetically separable fromV-ATPase activity (i.e., WRT secretion may require only the V0 domain,acting separately from the V1 domain); VHA-5 is required for alaeformation, like the V0 subunits VHA-1 and VHA-4, but not like the V1subunits VHA-8 or VHA-13; in S. cerevisiae, different V0 a-subunits(Stv1p and Vph1p) direct the assembly of V-ATPases to differentmembranes and organelles, suggesting that the profusion of such subunitsin C. elegans (VHA-5, VHA-6, VHA-7, and six UNC-32 isoforms) may have asimilar function; VHA-5 is predicted to capture protons from V-ATPasetransmembrane rotor components and export the protons across themembrane.