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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1984 Dec;81(23):7338–7342. doi: 10.1073/pnas.81.23.7338

Rat liver asialoglycoprotein receptor lacks a cleavable NH2-terminal signal sequence.

E C Holland, J O Leung, K Drickamer
PMCID: PMC392141  PMID: 6095287

Abstract

Two cDNA clones encoding the predominant form of the asialoglycoprotein receptor from rat liver (the major rat hepatic lectin; RHL-1) were identified by screening a rat liver cDNA library with a mixed oligonucleotide probe 35 nucleotides long. One clone was a nearly full-length copy of the mRNA for RHL-1, while the other was shortened at both ends. The sequences of these clones demonstrate that this transmembrane receptor is not synthesized with an NH2-terminal signal sequence. The only proteolytic processing occurring in the biosynthesis of RHL-1 is the removal of the NH2-terminal initiator methionine residue. Insertion of RHL-1 into the membrane is postulated to occur by the recognition of the internal transmembrane region as a signal sequence.

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Selected References

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