A signal peptide sometimes also called signal sequence, targeting signal, localization signal, localization sequence, transit peptide or leader peptide. It is a short, generally 5-30 amino acids long, peptide present at the N-terminus of most newly synthesized proteins. These proteins include those that reside either secreted from the cell, inside certain organelles (Golgi or endoplasmic reticulum), or inserted into most cellular membranes. Although the majority of type I membrane-bound proteins have signal peptides, most type II and multi-spanning membrane-bound proteins are targeted to these secretary pathways via their first transmembrane domain, which biochemically resembles a signal sequence after it is cleaved. Now, bioinformaticians at Creative Proteomics are proud to tell you we are open to help you with Signal Peptide Prediction Service!
The core of the signal peptide includes a long section of hydrophobic amino acids (about 5-16 residues long) that has a tendency to form a single alpha-helix (also referred to as the "h-region"). In addition, lots of signal peptides begin with a short positively charged section of amino acids, which may contribute to form proper topology of the polypeptide during translocation. Because of its close location to the N-terminal it is referred to as the "n-region". At the terminal of the signal peptide, there is generally a stretch of amino acids that is detected and cleaved by signal peptidase and therefore called cleavage site.
Methods used in signal peptide prediction service provided by Creative Proteomics, include:
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