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. Author manuscript; available in PMC: 2012 Jun 1.
Published in final edited form as: Trends Endocrinol Metab. 2011 May 31;22(6):197–203. doi: 10.1016/j.tem.2011.03.008

Figure 2. Schematic diagram of the structural features of murine perilipin 5.

Figure 2

Structural domains that are shared by some of the perilipin family of proteins are depicted in shades of black and grey. The N terminus of perilipin 5 contains 100 amino acid (AA) sequences that are highly conserved between perilipin 1, 2, 3 but not 4 (PAT-1 domain, (black)). Overlapping with these sequences are stretches of amino acids containing 11-mer repeat sequences, a common feature for all perilipin proteins (PAT-2 domain, (medium grey)). The C-terminus of perilipin 5 contains a highly conserved sequence of 14 amino acids that folds into a hydrophobic cleft in perilipin 2, 3 and 4 but not in perilipin 1 (light grey). Unique to perilipin 5 are the ATGL and CGI-58 binding domain (blue) between 189 amino acids (AA) and 391 AA as well as a mitochondria-binding domain between 443 AA and 463 AA (yellow).