Drosophila homolog of the murine Int-1 protooncogene

• Published in: Proceedings of the National Academy of Sciences - PNAS 1988-05, Vol.85 (9), p.3034-3038
• Main Authors: Uzvolgyi, E, Kiss, I, Pitt, A, Arsenian, S, Ingvarsson, S, Udvardy, A, Hamada, M, Klein, G, Sumegi, J
• Format: Article
• Language: English
• Subjects: ADN; Amino Acid Sequence; Amino acids; Animals; ARN; Bacteriophages; Base Sequence; Biological and medical sciences; Chromosome Mapping; CLONE; CLONES; Cloning, Molecular; Complementary DNA; DNA; DNA probes; DROSOPHILA; DROSOPHILA MELANOGASTER; Drosophila melanogaster - genetics; Drosophilidae; Embryos; Fundamental and applied biological sciences. Psychology; GENE; GENES; Genes. Genome; Genomics; Mice; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; Nucleic Acid Hybridization; NUCLEOTIDE; NUCLEOTIDES; NUCLEOTIDOS; Proto-Oncogenes; RNA; RNA, Messenger - analysis
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.85.9.3034

We have isolated phage clones from Drosophila melanogaster genomic and cDNA libraries containing a sequence homologous to the murine Int-1 protooncogene. The Drosophila gene is represented by a single locus at position 28A1-2 on chromosome 2. The gene is expressed as a 2.9-kilobase-long polyadenylylated mRNA in embryo, larval, and pupal stages. It is hardly detectable in adult flies. The longest open reading frame of the cDNA clone corresponds to a protein 469 amino acids long. Alignment of the predicted amino acid sequences shows that the Drosophila protein is 86 amino acids longer than its murine counterpart. In spite of the difference in length, the two proteins are highly conserved with an overall sequence homology of 54%. Both Drosophila and murine Int-1 proteins begin with a hydrophobic leader sequence and contain cysteine residues and sites for glycosylation (four in the murine protein and one in the Drosophila protein) in conserved positions, suggesting that they play important functional roles.