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Beschreibung

Vesicle-associated membrane protein-associated protein A (UniProt Q9P0L0, also known as 33 kDa VAMP-associated protein, hVAP-33, VAMP-A, VAMP-associated protein A, VAP-33, VAP-A) is encoded by the VAPA (also known as VAP33) gene (Gene ID 9218) in human. VAMP-associated proteins (VAPs) are type IV membrane proteins that are well conserved among species. There exist three human VAPs encoded by two genes, with VAPA encoding VAP-A and VAPB encoding VAP-B and VAP-C. VAPs generally localize at the endoplasmic reticulum (ER), although they are also reported to localize at other subcellular organelles in some species and cell types. VAP-A contains a major sperm protein (MSP) domain at the N-terminal, followed by a coiled-coil domain, and a transmembrane (TM) domain. VAPs were shown to have important roles in non-vesicular lipid transport, lipid metabolism, the regulation of ER structure, and the unfolded protein response through MSP domain-mediated interaction with FFAT motifs. Oxysterol-binding protein (OSBP) is a cytosolic receptor of cholesterol and oxysterols. OSBP is recruited to the ER by binding to the MSP domain of VAP-A, a process essential for the stimulation of sphingomyelin synthesis by 25-hydroxycholesterol.