Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Combined Automated Annotation using Multiple IEA Methods
Annotation inferences using phylogenetic trees
FFAT motif phosphorylation controls formation and lipid transfer function of inter-organelle contacts.
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Human VAPA is anchored in the ER by a C-terminal transmembrane domain with its MSP domain in the cytosol, and the crystal structure of the VAPA MSP domain with a phospho-FFAT peptide identifies the binding-pocket residues.
"VAP‐A, VAP‐B, and MOSPD2 are anchored in the ER membrane by a carboxyl‐terminal transmembrane domain with their MSP domain projecting into the cytosol."
VAP-33 localizes to both an intracellular vesicle population and with occludin at the tight junction.
UniProtKB A0A3Q2H1L9: horse VAPA sequence and domain features
UniProtKB Q9P0L0: human VAPA reviewed record
VAPA human–horse sequence comparison
VAPA horse A0A3Q2H1L9: isoform correspondence and FFAT pocket (re-review)