Unlike its human ortholog, murine perilipin is composed of 517 amino acids in the primary structure of which several regions can be identified. Three moderately hydrophobic sequences (H1, H2, H3) of 18 rem (243-260 aa), 23 rem (320-332 aa) and 16 rem (349-364 aa) can be identified in the centre of the protein, as well as an acidic region of 28 residues where both glutamic and aspartic acids add up to 19 of them. Five sequences 18 residues long that could form amphipathic β-pleated sheets—according to a prediction made through LOCATE program—are found between aa 111 and 182.  Serines occupying positions 81, 222, 276, 433, 492 and 517 act as phosphorylation sites -numbered from 1 to 6- for PKA, as well as several other threonines and serines which add up to 27 phosphorylation sites.