Synaptotagmin XIV Like Protein (SYT14L)

SYTDEP contains 3 N-glycosylation sites, an O-glycosylation site, a number of potential serine, threonine, and tyrosine phosphorylation sites, 3 N-terminal cysteine residues that might be fatty-acylated, and a single C2B domain. The N-terminal 24 amino acids of SYTDEP showed no significant homology with any known protein domain.

Sequence analysis suggested that, like SYT14, SYTDEP is a calcium-independent C2 protein. RT-PCR analysis showed that SYTDEP was highly expressed in mature peripheral blood neutrophils and became upregulated during neutrophil differentiation of HL-60 cells that did not express SYT14. GOS-3 cells expressed both SYTDEP and SYT14. Western blot analysis of neutrophils detected a 27-kD protein, suggesting posttranslational modification.