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VapA

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For Research Use Only. Not For Clinical Use.


Background

vapA, or V-type proton ATPase catalytic subunit A, is a component of a V-type ATPase, a rotary proton pump. VapA contains ATP-binding sites and catalyzes the hydrolysis of ATP, providing the energy for pumping protons across membranes. V-type ATPases are crucial for maintaining organelle pH and various cellular processes.
Protein class

Metabolic proteins, Plasma proteins, Transporters

Predicted location

Membrane

Single cell type specificity

Low cell type specificity

Immune cell specificity

Low immune cell specificity

Cell line specificity

Low cell line specificity

Interaction

Homodimer, and heterodimer with VAPB (PubMed:11511104). Interacts with VAMP1, VAMP2, STX1A, BET1, SEC22C and with the C-terminal domain of OCLN (PubMed:11511104, PubMed:9657962, PubMed:10523508). Interacts with OSBPL1A (By similarity). Interacts (via MSP domain) with ZFYVE27; may retain ZFYVE27 in the endoplasmic reticulum and regulate its function in cell projections formation (PubMed:19289470, PubMed:21976701). Interacts with OSBP (PubMed:20178991). Interacts (via C-terminus) with RSAD2/viperin (via C-terminus) (PubMed:21957124). Interacts with IFITM3 (PubMed:23601107). Interacts with OSBPL3 (phosphorylated form) (PubMed:16143324, PubMed:25447204). Interacts with KIF5A in a ZFYVE27-dependent manner (PubMed:21976701). Interacts with STARD3 (via FFAT motif) (PubMed:24105263). Interacts with STARD3NL (via FFAT motif) (PubMed:24105263). Interacts with CERT1 (PubMed:16895911). Interacts with PLEKHA3 and SACM1L to form a ternary complex (PubMed:30659099). Interacts with VPS13A (via FFAT motif) (PubMed:30741634). (Microbial infection) Interacts with HCV protein NS5A and NS5B (PubMed:21957124).

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