signal peptide

However, they lack a signal peptide that would allow them to do so.

This is the result expected if the signal peptide were necessary for secretion.

Signaling peptides include members of the following protein families.

The free signal peptides are then digested by specific proteases.

Another member of this pathway is the signal peptide peptidase.

Fam158a does not have any predicted signal peptides or transmembrane regions.

The putative signal peptide is indicated by a dashed line starting at Met1.

Thus, a favored and a minor cleavage site seem to exist for the signal peptide.

The production of multiple signalling peptides from one precursor is a common feature found in animals.

Also, this protein is predicted to be non-myristoylated and does not contain a signal peptide.

This signal peptide is removed by proteolysis after their transport through a membrane.

Some secretory proteins do not have classical signal peptide sequences.

Like other proteins that contain a signal peptide, their name is prefixed by pre.

The signal peptide is cleaved off in the endoplasmic reticulum.

It stays membrane-bound as long as there is no signal peptide.

More specifically, the N-terminal domain functions as a signal peptide which helps export.

Its signal peptide is at the N-terminus but is not cleaved off.

One possible N-glycosylation site was predicted, but a signal peptide was not detected.

The signal peptide on the N-terminus acts as a temporary tether to hold it in place.

Before the hormone is released from the cell, the signal peptide and other amino acids are removed.

In the entire nucleotide sequence, only 40 amino acids make up the signal peptide.

Any eukaryotic signal peptide sequence usually works fine.

The first exon codes for a signal peptide.

The presence of these signal peptides can be used to predict the secretome of a cell.

All members of this family have either a signal peptide or a transmembrane region, indicating an extracellular location (Figure 3).