PRY1 cDNA ORF clone, Saccharomyces cerevisiae S288C

Life with 6000 genes.
Goffeau A, Barrell BG, Bussey H, Davis RW, Dujon B, Feldmann H, Galibert F, Hoheisel JD, Jacq C, Johnston M, Louis EJ, Mewes HW, Murakami Y, Philippsen P, Tettelin H, Oliver SG
Science (New York, N.Y.)274(5287)546, 563-7(1996 Oct)

Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.
Galibert F, Alexandraki D, Baur A, Boles E, Chalwatzis N, Chuat JC, Coster F, Cziepluch C, De Haan M, Domdey H, Durand P, Entian KD, Gatius M, Goffeau A, Grivell LA, Hennemann A, Herbert CJ, Heumann K, Hilger F, Hollenberg CP, Huang ME, Jacq C, Jauniaux JC, Katsoulou C, Karpfinger-Hartl L
The EMBO journal15(9)2031-49(1996 May)

These results indicate that some CAP family members, such as Pry1, can bind different lipids, particularly sterols and fatty acids, at distinct binding sites, suggesting that the CAP domain may serve as a stable, secreted protein domain that can accommodate multiple ligand-binding sites.
Title: The pathogen-related yeast protein Pry1, a member of the CAP protein superfamily, is a fatty acid-binding protein.

the caveolin-binding motif of Pry1 is crucial for selective lipid binding and that lipid binding may occur through displacement of the loop containing this motif
Title: The caveolin-binding motif of the pathogen-related yeast protein Pry1, a member of the CAP protein superfamily, is required for in vivo export of cholesteryl acetate.