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

doi:10.1016/0092-8674(87)90214-5

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

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Abstract

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 language	English
Pages (from-to)	181-192
Number of pages	12
Journal	Cell
Volume	50
Issue number	2
DOIs	https://doi.org/10.1016/0092-8674(87)90214-5
State	Published - Jul 17 1987

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Dahms, N. M., Lobel, P., Breitmeyer, J., Chirgwin, J. M., & Kornfeld, S. (1987). 46 kd mannose 6-phosphate receptor: Cloning, expression, and homology to the 215 kd mannose 6-phosphate receptor. Cell, 50(2), 181-192. https://doi.org/10.1016/0092-8674(87)90214-5

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abstract = "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.",

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