Difference between revisions of "YCL043C"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000548 YCL043C]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000548 YCL043C]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''PDI1 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''PDI1 ''

Revision as of 07:45, 23 January 2012

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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 resident in the endoplasmic reticulum lumen, essential for the formation of disulfide bonds in secretory and cell-surface proteins, unscrambles non-native disulfide bonds; forms a complex with Mnl1p that has exomannosidase activity, processing unfolded protein-bound Man8GlcNAc2 oligosaccharides to Man7GlcNAc2 which promotes degradation in the unfolded protein response[1][2][3][4][5]




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References

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  1. Farquhar R, et al. (1991) Protein disulfide isomerase is essential for viability in Saccharomyces cerevisiae. Gene 108(1):81-9 SGD PMID 1761235
  2. 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
  3. 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
  4. 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
  5. 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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