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Signal peptide
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==Function (translocation)== Signal peptides function to prompt a cell to [[Protein targeting#Protein translocation|translocate]] the protein, usually to the cellular membrane. In [[prokaryotes]], signal peptides direct the newly synthesized protein to the SecYEG protein-conducting channel, which is present in the [[plasma membrane]]. A homologous system exists in [[eukaryotes]], where the signal peptide directs the newly synthesized protein to the Sec61 channel, which shares structural and sequence homology with SecYEG, but is present in the endoplasmic reticulum.<ref>{{cite journal | vauthors = Rapoport TA | title = Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes | journal = Nature | volume = 450 | issue = 7170 | pages = 663β9 | date = November 2007 | pmid = 18046402 | doi = 10.1038/nature06384 | bibcode = 2007Natur.450..663R | s2cid = 2497138 }}</ref> Both the SecYEG and Sec61 channels are commonly referred to as the [[translocon]], and transit through this channel is known as translocation. While secreted proteins are threaded through the channel, transmembrane domains may diffuse across a lateral gate in the translocon to partition into the surrounding membrane.
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