We isolated and sequenced cDNA clones corresponding to two storage proteins (HcSP-1 and HcSP-2) from fall webworm, Hyphantria cunea. The cDNAs for HcSP-1 (2,337 bp) and HcSP-2 (2,572 bp) code for 753 and 747 residue proteins with predicted molecular masses of 88.3 and 88.5 kDa, respectively. The calculated isoelectric points are pI = 8.4 (HcSP-1) and 7.6 (HcSP-2). Multiple alignment analysis of the amino acid sequence revealed that HcSP-1 is most similar to SL-1 from S. litura (73.8% identity) and other methionine-rich hexamers, whereas HcSP-2 is most similar to the SL-2 a subunit from S. litura (74.8% identity) and other moderately methionine-rich hexamers. The two storage proteins from H. cunea shared only 38.4% identity with one another. According to both phylogenetic analyses and the criteria of amino acid composition, HcSP-1 belongs to the subfamily of Met-rich storage proteins (6% methionine, 10% aromatic amino acid), and HcSP-2 belongs to the subfamily of moderately methionine-rich storage proteins (3.2% methionine, 12.9% aromatic amino acid). Topical application of the JH analog, methoprene, after head ligation of larvae, suppressed transcription of the SP genes, indicating hormonal effects at the transcriptional level. The HcSP-1 transcript was detected by Northern blot analysis in Malpighian tubule, testis, and ovary, in addition to fat body where it was most abundant. The nucleotide sequences reported in this paper have been submitted to the Genbank/EMBL Data Bank with accession number U60988 (HcSP-1) and AF157013 (HcSP-2).