Cloning and sequence analysis of the cation-independent mannose 6-phosphate receptor.
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.
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002352:Carrier Proteins / Q000235:genetics*; D002417:Cattle; D003001:Cloning, Molecular; D004247:DNA / Q000032:analysis; D008969:Molecular Sequence Data; D017527:Receptor, IGF Type 2
D002352:Carrier Proteins; D017527:Receptor, IGF Type 2; D004247:DNA