Table 1.
C-terminal sequences | Genes | Function | Location | Strength of ERSa |
---|---|---|---|---|
NFRDEL | SIL1 (Ref. 19) | Nucleotide exchange factor for the ER luminal chaperone Kar2p | ER | Medium |
DGEDEL | GPI17 (Ref. 21) | Subunit of the glycosylphosphatidylinositol transamidase complex that adds GPIs to newly synthesized proteins | ER membrane | Weak |
PYLDEL | QCR2 (Ref. 32) | Subunit 2 of ubiquinol cytochrome-c reductase | Mitochondrion inner membrane | Weak |
MLKDEL | SCJ1 (Ref. 20) | A homolog of bacterial chaperone DnaJ, cooperates with Kar2p to mediate maturation of proteins | ER lumen | Medium |
AIHDEL | PDI1 (Ref. 33) | Protein disulfide isomerase, essential for disulfide bond formation in secretory and cell-surface proteins | ER lumen | Strong |
GLHDEL | SED4 (Ref. 34) | Integral ER membrane protein that stimulates Sar1p GTPase activity | ER membrane; Golgi apparatus membrane | Medium |
AAHDEL | CPR5 (Ref. 35) | Peptidyl-prolyl cis-trans isomerase (cyclophilin) of the ER; catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues | ER lumen | Weak |
TVHDEL | EUG1 (Ref. 36) | Protein disulfide isomerase of the ER lumen | ER lumen | Medium |
VSHDEL | SEC20 (Ref. 37) | Membrane glycoprotein v-SNARE; involved in retrograde transport from the Golgi to ER | ER | Medium |
ILHDEL | LHS1 (Ref. 38) | Molecular chaperone of the ER lumen; involved in polypeptide translocation and folding | ER lumen | Strong |
SSHDEL | MPD2 (Ref. 39) | Member of the Pdi family; exhibits chaperone activity | ER | Weak |
PLHDEL | KRE5 (Ref. 40) | Protein required for β-1,6-glucan biosynthesis | ER lumen | Strong |
NKHDEL | MPD1 (Ref. 41) | Member of the Pdi family; interacts with and inhibits the chaperone activity of Cne1p | ER lumen | Weak |
IEHDEL | YOS9 (Ref. 42) | ER quality-control lectin; integral subunit of the HRD ligase; participates in efficient ER retention of misfolded proteins in ERAD | ER membrane | Strong |
FEHDEL | KAR2 (Ref. 43) | ATPase involved in protein import into the ER; acts as a chaperone to mediate ER protein folding and may help export soluble proteins | ER lumen | Strongb |
a The strength of the ERS was evaluated in our research.
b The high level of ER retention strength in FEHDEL was identified in both our and others' research (14).