YCL043C - Revision history

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@@ Line 18: / Line 18: @@
 |}
 <br>
-'''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; key regulator of Ero1p activity; 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<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
+'''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
   {{SGDpaper|S000066106}} PMID 11584268</ref>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''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<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='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
+'''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; key regulator of Ero1p activity; 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<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
   {{SGDpaper|S000066106}} PMID 11584268</ref>
 <br>

@@ Line 4: / Line 4: @@
 {|{{Prettytable}} align = 'right' width = '200px'
 |-
-|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000548 YCL043C]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000548 YCL043C]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''PDI1 ''

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''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<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='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
+'''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<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='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
   {{SGDpaper|S000066106}} PMID 11584268</ref>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''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<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='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='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='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
+'''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<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='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
-  {{SGDpaper|S000069894}} PMID 1740407</ref>
+  {{SGDpaper|S000066106}} PMID 11584268</ref>
 <br>
 <br>

@@ Line 4: / Line 4: @@
 {|{{Prettytable}} align = 'right' width = '200px'
 |-
-|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YCL043C YCL043C]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000548 YCL043C]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''PDI1 ''
@@ Line 14: / Line 14: @@
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 |nowrap| Chr III:50221..48653
 |}
 <br>
-'''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
+'''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<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
   {{SGDpaper|S000047853}} PMID 1761235</ref>
 <br>
@@ Line 37: / Line 39: @@
 J Biol Chem 278(5):3265-74</ref>
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		+	Specifically higher expression in carbon limited chemostat cultures versus carbon excess.
		+	<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.
		+	J Biol Chem 278(5):3265-74</ref>
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