Abstract
The cDNA of a thrombospondin homologue in Drosophila melanogaster (DTSP) has been sequenced, and structural features of the translated protein analyzed. Thrombospondin proteins had previously been identified only in vertebrates, including human and mouse. Comparison with the genomic sequence revealed that the DTSP gene is divided into 13 exons; The translation initiation site is in exon 2. The transcription start site was analyzed using a PCR procedure, and the longest transcripts were found to initiate about 300 bp 5' of the predicted start site. The open reading frame of the DTSP cDNA encodes a protein that has 1060 amino acid residues. The polypeptide is composed of domains or repeats characteristic of the TSP3/TSP4/COMP subfamily of thrombospondin proteins: Amino-terminal domain, four Type II repeats, seven Type III repeats, carboxyl-terminal domain. The protein is highly acidic, particularly in the region of Type III repeats, with an Asp + Glu content of 15.8%. A signal peptide was detected at the N-terminus, which indicates that DTSP, like other TSPs, functions as an extracellular protein. Ten Asn residues were identified as potential glycosylation sites. Alignment of the amino acid sequences of the Drosophila TSP with human TSP1-TSP4 and COMP demonstrated a high degree of homology between the four Type II repeats, seven Type III repeats, and C-terminal domain.
