YCL043C

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Systematic name YCL043C
Gene name PDI1
Aliases MFP1, TRG1
Feature type ORF, Verified
Coordinates Chr III:50221..48653
Primary SGDID S000000548


Description of YCL043C: Protein disulfide isomerase; multifunctional protein of ER lumen, essential for formation of disulfide bonds in secretory and cell-surface proteins, unscrambles non-native disulfide bonds; key regulator of Ero1p; forms complex with Mnl1p that has exomannosidase activity, processing unfolded protein-bound Man8GlcNAc2 oligosaccharides to Man7GlcNAc2, promoting degradation in unfolded protein response; PDI1 has a paralog, EUG1, that arose from the whole genome duplication[1][2][3][4][5][6][7]




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References

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  1. Byrne KP and Wolfe KH (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61 SGD PMID 16169922
  2. Farquhar R, et al. (1991) Protein disulfide isomerase is essential for viability in Saccharomyces cerevisiae. Gene 108(1):81-9 SGD PMID 1761235
  3. Gauss R, et al. (2011) A complex of pdi1p and the mannosidase htm1p initiates clearance of unfolded glycoproteins from the endoplasmic reticulum. Mol Cell 42(6):782-93 SGD PMID 21700223
  4. Kim S, et al. (2012) Balanced Ero1 activation and inactivation establishes ER redox homeostasis. J Cell Biol 196(6):713-25 SGD PMID 22412017
  5. Laboissiere MC, et al. (1995) The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds. J Biol Chem 270(47):28006-9 SGD PMID 7499282
  6. Noiva R and Lennarz WJ (1992) Protein disulfide isomerase. A multifunctional protein resident in the lumen of the endoplasmic reticulum. J Biol Chem 267(6):3553-6 SGD PMID 1740407
  7. Sevier CS, et al. (2001) A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation. Nat Cell Biol 3(10):874-82 SGD PMID 11584268

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