title: Sequence and N-terminal processing of the transmembrane protein E1 of the coronavirus transmissible gastroenteritis virus.
abstract: Sequencing of part of a clone from a transmissible gastroenteritis virus genome cDNA library led to the identification of the gene encoding the E1 matrix protein. The amino acid sequence of the primary translation product predicts a polypeptide of 262 residues which shares many features with the previously characterized murine hepatitis virus and infectious bronchitis virus E1 proteins. However, N-terminal amino acid sequencing revealed that a putative signal peptide of 17 residues was absent in the virion-associated polypeptide. The predicted mol. wt. of the mature unglycosylated product, 27,800, is in agreement with the experimental Mr value.
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D003062:Codon; D003332:Coronaviridae / Q000032:analysis*; D005814:Genes, Viral; D008970:Molecular Weight; D014176:Protein Biosynthesis; D021382:Protein Sorting Signals / Q000032:analysis; D005760:Transmissible gastroenteritis virus / Q000032:analysis* / Q000235:genetics; D014763:Viral Matrix Proteins; D014764:Viral Proteins / Q000032:analysis* / Q000235:genetics
chemical_list: D003062:Codon; D021382:Protein Sorting Signals; D014763:Viral Matrix Proteins; D014764:Viral Proteins