When the protein is translated from messenger RNA, it is created from N-terminus to C-terminus. The amino end of an amino acid (on a charged tRNA) during the elongation stage of translation, attaches to the carboxyl end of the growing or nascent chain. Since the start codon of the genetic code codes for the amino acid methionine, most protein sequences start with a methionine (more specifically: the modified version N-formylmethionine, fMet). However, some proteins are modified posttranslationally, for example by cleavage from a protein precursor, and therefore may have different amino acids at their N-terminus.
The N-terminal signal peptide is recognized by the signal recognition particle (SRP) and results in the targeting of the protein to the secretory pathway. In eukaryotic cells, these proteins are synthesized at the rough endoplasmic reticulum. In prokaryotic cells, the proteins are exported across the cell membrane. In chloroplasts, signal peptides target proteins to the thylakoids.
The N-terminal mitochondrial targeting peptide (mtTP) allows for the protein to be imported into the mitochondrion.
The N-terminal chloroplast targeting peptide (cpTP) allows for the protein to be imported into the chloroplast.
The N-terminus can be modified by the addition of a myristoyl anchor. Proteins that are modified this way contain a consensus motif at their N-terminus as a modification signal.
The N-terminus can also be modified by the addition of a fatty acid anchor to form N-acylated proteins. The most common form of such modification is the addition of a palmitoyl group.