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Cloning and sequence analysis of the cation-independent mannose 6-phosphate receptor.

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Lobel, P, Dahms, N M, Kornfeld, S·1988·Journal of Biological Chemistry

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.

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Metadata

Authors
Lobel, P., Dahms, N. M., & Kornfeld, S.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1988-02
Volume
263
Issue
5
Pages
2563-2570
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1498772725
Cited by
216
References
0
FWCI
10.37
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Cloning and sequence analysis of the cation-independent mannose 6-phosphate receptor. https://app.cochat.ai/papers/10.1016/s0021-9258(18)69244-0
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Lobel, P., Dahms, N. M., & Kornfeld, S. (1988). Cloning and sequence analysis of the cation-independent mannose 6-phosphate receptor. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)69244-0

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