VPS9ankyrin

VPS9ankyrin is a putative eukaryotic protein characterized by a Vps9 domain fused to ankyrin repeats. The Vps9 domain is commonly associated with guanine nucleotide exchange factor (GEF) activity toward Rab GTPases, particularly Rab5, and ankyrin repeats function as versatile protein–protein interaction motifs. The combination in VPS9ankyrin suggests a role in coordinating endocytic trafficking and the assembly of protein complexes on endosomal membranes.

Predicted function and interactions: Based on domain composition, VPS9ankyrin may act as a Rab5-family GEF or regulator, promoting activation of Rab5 on early endosomes, while ankyrin repeats could recruit adaptors, scaffolding partners, or cargo proteins. The protein may participate in endosome maturation, receptor trafficking, and membrane dynamics, with potential regulatory input from phosphorylation or interaction with cytoskeletal elements.

Genomic context and evolution: VPS9ankyrin has been identified in several vertebrate lineages and in other opisthokonts in sequence databases as a conserved, multi-domain protein. Orthologs show varying numbers of ankyrin repeats, consistent with modular evolution of the ankyrin motif. The precise number and arrangement of domains can differ among species.

Clinical and research status: There is limited direct experimental evidence describing VPS9ankyrin's function, and there are no well-established disease associations. The protein remains a subject for future studies to validate its expression, subcellular localization, and mechanistic role in vesicular trafficking.