Isolation and identification of partial cDNA clones for endoplasmin, the major glycoprotein of mammalian endoplasmic reticulum.
The amino acid sequences of peptides isolated from murine endoplasmin showed significant homology (approximately 50%) with sequences in the heat-shock proteins 90 and 83 of yeast and Drosophila, respectively, indicating that they are related proteins. Mixed oligonucleotide probes, deduced from the peptide sequences, were used to isolate cDNAs from a murine liver cDNA library. DNA sequencing confirmed the presence of a coding sequence for one of the endoplasmin peptides, formally establishing the authenticity of the cDNA. The identity of the murine and hamster endoplasmin sequences suggests a level of sequence conservation associated with proteins that perform a structural role in cells.
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA; D004721:Endoplasmic Reticulum / Q000032:analysis*; D006023:Glycoproteins / Q000302:isolation & purification*; D008562:Membrane Glycoproteins; D008565:Membrane Proteins / Q000302:isolation & purification*; D051379:Mice
D006023:Glycoproteins; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; C053387:endoplasmin; D004247:DNA