Paralemmin (PALM)

Paralemmin is a member of the paralemmin protein family. PALM has a highly conserved coiled-coil N terminus that displays a periodicity of acidic, basic, hydrophobic, and glutamine residues, as well as 2 potential leucine zippers.

PALM has a central motif similar to a sequence found in lipid-anchored SNAREs that is involved in endoplasmic reticulum-Golgi transport. The C terminus of PALM contains a cluster of basic residues, which likely contribute to membrane association, putative palmitoylated cysteines, and a prenylation consensus motif. PALM also has phosphorylation motifs for several serine/threonine kinases. The 5-prime untranslated regions of the chicken, mouse, and human transcripts are GC rich.