Molecular characterization of the CAN1 locus in Saccharomyces cerevisiae. A transmembrane protein without N-terminal hydrophobic signal sequence.
The complete DNA sequence of the CAN1 locus of the yeast Saccharomyces cerevisiae is presented. The predicted primary translation product consists of 590 amino acids. From the hydropathic profile of the amino acid sequence (as calculated by the algorithm of Kyte and Doolittle (Kyte, J., and Doolittle, R. F. (1982) J. Mol. Biol. 157, 105-132)), one can divide the protein into two distinct regions. The 93-amino acid long N-terminal domain is extremely hydrophilic and does not exhibit any cleavable signal sequence. The rest of the protein (from amino acids 94 to 590) shows features typical for an integral membrane protein. The proposal for the N terminus of the primary translation product is based on results obtained by S1 mapping, insertion mutagenesis, and gene fusion experiments.
D000595:Amino Acid Sequence; D026905:Amino Acid Transport Systems; D001120:Arginine / Q000378:metabolism; D001483:Base Sequence; D002874:Chromosome Mapping; D005800:Genes, Fungal; D026901:Membrane Transport Proteins / Q000032:analysis / Q000096:biosynthesis / Q000235:genetics*; D009693:Nucleic Acid Hybridization; D011401:Promoter Regions, Genetic; D012441:Saccharomyces cerevisiae / Q000235:genetics*; D014158:Transcription, Genetic
D026905:Amino Acid Transport Systems; D026901:Membrane Transport Proteins; D001120:Arginine