All synucleins have in common a highly conserved alpha-helical lipid-binding motif with similarity to the class-A2 lipid-binding domains of the exchangeable apolipoproteins. Synuclein family members are not found outside vertebrates, although they have some conserved structural similarity with plant 'late-embryo-abundant' proteins.
^Polymeropoulos MH, Lavedan C, Leroy E, Ide SE, Dehejia A, Dutra A et al. (1997). "Mutation in the alpha-synuclein gene identified in families with Parkinson's disease.". Science276 (5321): 2045–7. doi:10.1126/science.276.5321.2045. PMID9197268.CS1 maint: Explicit use of et al. (link)
^Mezey E, Dehejia A, Harta G, Papp MI, Polymeropoulos MH, Brownstein MJ (1998). "Alpha synuclein in neurodegenerative disorders: murderer or accomplice?". Nat Med4 (7): 755–7. doi:10.1038/nm0798-755. PMID9662355.