Faculty Collaboration Database

46 kd mannose 6-phosphate receptor: cloning, expression, and homology to the 215 kd mannose 6-phosphate receptor. Cell 1987 Jul 17;50(2):181-92

Date

07/17/1987

Pubmed ID

2954652

DOI

10.1016/0092-8674(87)90214-5

Scopus ID

2-s2.0-0023658301 (requires institutional sign-in at Scopus site)   112 Citations

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.

Author List

Dahms NM, Lobel P, Breitmeyer J, Chirgwin JM, Kornfeld S

Author

Nancy M. Dahms PhD Professor in the Biochemistry department at Medical College of Wisconsin

MESH terms used to index this publication - Major topics in bold

Amino Acid Sequence
Animals
Base Sequence
Carrier Proteins
Cloning, Molecular
Female
Genes
Mannosephosphates
Molecular Weight
Oocytes
Peptide Fragments
Protein Biosynthesis
Receptor, IGF Type 2
Sequence Homology, Nucleic Acid
Transcription, Genetic
Trypsin
Xenopus laevis