Gene

vha-5

Species
Caenorhabditis elegans
Symbol
vha-5
Name
Vacuolar H ATPase 5
Synonyms
  • CELE_F35H10.4
  • F35H10.4
Biotype
protein coding gene
Automated Description
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.
Cross References
Additional Information
Literature

Orthology

Gene tree
PANTHER:PTHR11629
Links to orthology data in JBrowse by filter level: Stringent,  Moderate,  No filter,  Best and Best Reverse

Paralogy

Function - GO Annotations

Pathways

No data available

Phenotypes

Primary Sources
Other Sources
None

Disease Associations

Cases where the expected disease association was NOT found
Cell color indicative of annotation volume

Transgenic Alleles

Models

Sequence Feature Viewer

Genome location
Assembly version
WBcel235
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8.3040M8.3045M8.3050M8.3055M8.3060M8.3065M8.3070M

Sequence Details

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Expression

Primary Sources
Other Sources
Cell color indicative of annotation volume; red slash indicates species lacks structure or developmental stage.

Molecular Interactions

Genetic Interactions