Difference between revisions of "YCL043C"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YCL043C 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 ''
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|nowrap| Chr III:50221..48653
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000000548
 
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'''Description of {{PAGENAME}}:''' 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<ref name='S000069894'>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 {{SGDpaper|S000069894}} PMID 1740407</ref><ref name='S000066106'>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 {{SGDpaper|S000066106}} PMID 11584268</ref><ref name='S000052206'>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 {{SGDpaper|S000052206}} PMID 7499282</ref><ref name='S000047853'>Farquhar R, et al. (1991) Protein disulfide isomerase is essential for viability in Saccharomyces cerevisiae. Gene 108(1):81-9
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'''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<ref name='S000113653'>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 {{SGDpaper|S000113653}} PMID 16169922</ref><ref name='S000047853'>Farquhar R, et al. (1991) Protein disulfide isomerase is essential for viability in Saccharomyces cerevisiae. Gene 108(1):81-9 {{SGDpaper|S000047853}} PMID 1761235</ref><ref name='S000145917'>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 {{SGDpaper|S000145917}} PMID 21700223</ref><ref name='S000150261'>Kim S, et al. (2012) Balanced Ero1 activation and inactivation establishes ER redox homeostasis. J Cell Biol 196(6):713-25 {{SGDpaper|S000150261}} PMID 22412017</ref><ref name='S000052206'>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 {{SGDpaper|S000052206}} PMID 7499282</ref><ref name='S000069894'>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 {{SGDpaper|S000069894}} PMID 1740407</ref><ref name='S000066106'>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
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==Community Commentary==
 
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Specifically higher expression in carbon limited chemostat cultures versus carbon excess.
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<ref>Boer VM, et al. (2003) The genome-wide transcriptional responses of Saccharomyces cerevisiae grown on glucose in aerobic chemostat cultures limited for carbon, nitrogen, phosphorus, or sulfur.
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J Biol Chem 278(5):3265-74</ref>
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==References==
 
==References==
 
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Latest revision as of 13:05, 16 August 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 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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