A thrombospondin homologue in Drosophila melanogaster

cDNA and protein structure

Research output: Contribution to journalArticle

14 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)177-184
Number of pages8
JournalGene
Volume269
Issue number1-2
DOIs
StatePublished - May 16 2001

Fingerprint

Thrombospondins
Drosophila Proteins
Complementary DNA
Proteins
Terminal Repeat Sequences
Exons
Transcription Initiation Site
Protein Sorting Signals
Drosophila melanogaster
Glycosylation
Open Reading Frames
Drosophila
Vertebrates
Amino Acid Sequence
Amino Acids
Polymerase Chain Reaction
Peptides
Genes

Keywords

  • Exon/intron organization
  • Nucleotide sequence
  • Open reading frame
  • Polypeptide domains
  • Transcription start site
  • TSP3/TSP4/COMP subfamily

Cite this

A thrombospondin homologue in Drosophila melanogaster : cDNA and protein structure. / Adolph, Kenneth W.

In: Gene, Vol. 269, No. 1-2, 16.05.2001, p. 177-184.

Research output: Contribution to journalArticle

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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.",
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