46 kd mannose 6-phosphate receptor: Cloning, expression, and homology to the 215 kd mannose 6-phosphate receptor

Nancy M. Dahms, Peter Lobel, James Breitmeyer, John M. Chirgwin, Stuart Kornfeld

Research output: Contribution to journalArticle

95 Scopus citations


We have isolated cDNA clones encoding the entire sequence of the bovine 46 kd cation-dependent mannose 6-phosphate (CD Man-6-P) receptor. Translation of CD Man-6-P receptor mRNA in Xenopus laevis oocytes results in a protein that binds specifically to phosphomannan-Sepharose, thus demonstrating that our cDNA clones encode a functional receptor. The deduced 279 amino acid sequence reveals a single polypeptide chain that contains a putative signal sequence and a transmembrane domain. Trypsin digestion of microsomal membranes containing the receptor and the location of the five potential N-linked glycosylation sites indicate that the receptor is a transmembrane protein with an extracytoplasmic amino terminus. This extracytoplasmic domain is homologous to the approximately 145 amino acid long repeating domains present in the 215 kd cation-independent Man-6-P receptor.

Original languageEnglish (US)
Pages (from-to)181-192
Number of pages12
Issue number2
StatePublished - Jul 17 1987


ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this