Signal peptide
Signal Peptide
A Signal peptide (or signal sequence, leader sequence, leader peptide) is a short (3-60 amino acids long) peptide chain that directs the post-translational transport of a protein.
Function[edit | edit source]
Signal peptides are used to direct the protein to certain locations within the cell. They are usually found at the N-terminus of the protein sequence and are cleaved off by a signal peptidase after the protein is transported.
Structure[edit | edit source]
The structure of a signal peptide varies between different proteins, but they generally contain three regions: a positively charged n-region, a hydrophobic h-region, and a polar c-region.
Signal Recognition Particle[edit | edit source]
The Signal Recognition Particle (SRP) is a protein-RNA complex that recognizes and targets specific proteins to the endoplasmic reticulum in eukaryotes and the plasma membrane in prokaryotes.
Secretory Proteins[edit | edit source]
Secretory proteins are synthesized on ribosomes bound to the ER. They have signal peptides that direct them into the ER lumen, where they are folded and modified.
See Also[edit | edit source]
References[edit | edit source]
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Contributors: Prab R. Tumpati, MD