Human perilipin-1 is composed by 522 amino acids, which add up to a molecular mass of 55.990 kDa. It presents an estimated number of 15 phosphorylation sites (residues 81, 85, 126, 130, 132, 137, 174, 299, 301, 382, 384, 408, 436, 497, 499 and 522) from which 3 -those in bold- have been suggested to be relevant for stimulated-lipolysis through PKA phosphorylation - they correspond respectively to PKA Phosphorylation sites 1, 5 and 6. A compositional bias of Glutamic acid can be found between residues 307 and 316.  Its secondary structure has been suggested to be conformed exclusively by partially hydrophobic α-helixes, as well as the respective coils and bends.
Whereas perilipin-1 is coded by a single gene, alternative mRNA splicing processes can lead to three protein isoforms (Perilipin A, B and C). Both Perilipin A and B present common N-terminal regions, differing in the C-terminal ones. Concretely, beginning from the N-terminal of Perilipin-1, a PAT domain—characteristic of its protein family—can be found, followed by an also characteristic repeated sequence of 13 residues which form amphipathic helixes with an active role in linking membranes and a 4-helix bundle before the C-terminal carbon. In Perilipin A, lipophile nature is conferred by the slightly hydrophobic amino acids concentrated in the central 25% of the sequence, region that anchors the protein to the core of the lipid droplet.