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
07/17/1987Pubmed ID
2954652DOI
10.1016/0092-8674(87)90214-5Scopus ID
2-s2.0-0023658301 (requires institutional sign-in at Scopus site) 112 CitationsAbstract
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 SAuthor
Nancy M. Dahms PhD Professor in the Biochemistry department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Amino Acid SequenceAnimals
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