VAPA
VAMP-Associated Protein A ( or Vesicle-Associated Membrane Protein-Associated Protein A) is a protein that in humans is encoded by the VAPA gene. Together with VAPB and VAPC it forms the VAP protein family. They are integral endoplasmic reticulum membrane proteins of the type II and are ubiquitous among eukaryotes. VAPA is ubiquitously expressed in human tissues and is thought to be involved in membrane trafficking by interaction with SNAREs, in regulation of lipid transport and metabolism, and in the Unfolded Protein Response (UPR). Protein structure The protein is divided in three different domains. First, an N-terminal beta-sheet with an immunoglobulin-like fold that shares homology with the Nematode major sperm protein (MSP). Secondly, a central coiled-coil domain. Then finally a C-terminal transmembrane domain (TMD) which is usually present in proteins of the t-SNARE superfamily and has been found in other proteins associated with vesicular transport. VAPA can form homo-dimers and also hetero dimers with VAPB by interactions through their (TMD). Intracellular Localisation Because of its ubiquitous expression, the intracellular localisation and function of VAPA may vary between cell types. It is however mainly located in the ER, Golgi apparatus and the Vesicular Tubular Compartment or ER-Golgi Intermediate Compartment, an organelle of