Faculty Collaboration Database

Cloning and sequence analysis of the cation-independent mannose 6-phosphate receptor. J Biol Chem 1988 Feb 15;263(5):2563-70

Date

02/15/1988

Pubmed ID

2963004

Scopus ID

2-s2.0-0023840372 (requires institutional sign-in at Scopus site)   180 Citations

Abstract

We have isolated and sequenced cDNA clones encoding the entire sequence of the bovine cation-independent mannose 6-phosphate receptor. The deduced 2499-amino acid precursor has a calculated molecular mass of 275 kDa. Analysis of the sequence indicates that the protein has a 44-residue amino-terminal signal sequence, a 2269-residue extracytoplasmic region, a single 23-residue transmembrane region, and a 163-residue carboxyl-terminal cytoplasmic region. The extra-cytoplasmic region consists of 15 contiguous repeating domains, one of which contains a 43-residue insertion that is similar to the type II repeat of fibronectin. The 15 domains have an average size of 147 amino acids and a distinctive pattern of 8 cysteine residues. Alignment of the 15 domains and the extracytoplasmic domain of the cation-dependent mannose 6-phosphate receptor shows that all have sequence similarities and suggests that all are homologous.

Author List

Lobel P, Dahms NM, 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
Cattle
Cloning, Molecular
DNA
Molecular Sequence Data
Receptor, IGF Type 2