Synaptotagmin XIV (SYT14)

Syt14 formed oligomers independent of Ca(2+). Oligomerization was mainly mediated by fatty-acylated cysteines between the transmembrane domain and spacer domain. The C2 domains of Syt14 bound liposomes made up of phosphatidylcholine and phosphatidylserine.

The deduced 555-amino acid mouse and human SYT14 proteins contain conserved N-terminal extracellular cysteines, followed by a transmembrane domain and C-terminal C-type tandem C2 domains. Database analysis identified a SYT14 homolog in Drosophila, but not in nematode, plant, or yeast. RT-PCR detected highest Syt14 expression in mouse heart and testis, with moderate expression in kidney. In mouse embryos, expression was weak on day 7 and strong on days 11, 15, and 17.