Short sequence of amino acids that determines the eventual location of a protein in the cell. An example is the N-terminal sequence of 20 or so amino acids that directs nascent secretory and transmembrane proteins to the endoplasmic reticulum.

A leader peptide that is cleaved out after the synthesis of the polypeptide and before the protein assumes its correct tertiary structure.

A short sequence of mainly hydrophobic amino acids at the N-terminus of secreted proteins. This peptide is captured by a signal-recognition particle as it emerges from the ribosome, which allows the ribosome to be transported to the endoplasmic reticulum.

a cleavable signal sequence of amino acids present in the pre-protein form of a secretable protein

a peptide capable of penetrating through the cell membrane to allow the export of cellular proteins

a peptide sequence that direct

a short hydrophobic sequence at the amino terminus of eukaryotic proteins targeted for the endoplasmic reticulum and often for secretion

a specific N-terminal sequence region with structural and physicochemical properties that permits protein membrane anchoring, insertion and translocation, most likely mediated by recognition mechanisms

A short sequence at the N-terminus of some proteins that directs the protein across a membrane.

A signal peptide is a short (3-60 amino acids long) peptide chain that directs the post-translational transport of a protein. Signal peptides may also be called targeting signals, signal sequences, transit peptides, or localization signals.