Difference between revisions of "YAL058W"
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| − | '''Description of YAL058W:''' Calnexin; integral membrane ER chaperone involved in folding and quality control of glycoproteins; chaperone activity is inhibited by Mpd1p, with which Cne1p interacts; 24% identical to mammalian calnexin; Ca+ binding not yet shown in yeast<ref name='S000082272'>Kimura T, et al. (2005) Interactions among Yeast Protein-Disulfide Isomerase Proteins and Endoplasmic Reticulum Chaperone Proteins Influence Their Activities. J Biol Chem 280(36):31438-41 {{SGDpaper|S000082272}} PMID 16002399</ref><ref name='S000076690'>Xu X, et al. (2004) P-domain and lectin site are involved in the chaperone function of Saccharomyces cerevisiae calnexin homologue. FEBS Lett 570(1-3):155-60 {{SGDpaper|S000076690}} PMID 15251457</ref><ref name='S000076464'>Xu X, et al. (2004) Expression and characterization of Saccharomyces cerevisiae Cne1p, a calnexin homologue. J Biochem | + | '''Description of YAL058W:''' Calnexin; integral membrane ER chaperone involved in folding and quality control of glycoproteins; chaperone activity is inhibited by Mpd1p, with which Cne1p interacts; 24% identical to mammalian calnexin; Ca+ binding not yet shown in yeast<ref name='S000082272'>Kimura T, et al. (2005) Interactions among Yeast Protein-Disulfide Isomerase Proteins and Endoplasmic Reticulum Chaperone Proteins Influence Their Activities. J Biol Chem 280(36):31438-41 {{SGDpaper|S000082272}} PMID 16002399</ref><ref name='S000076690'>Xu X, et al. (2004) P-domain and lectin site are involved in the chaperone function of Saccharomyces cerevisiae calnexin homologue. FEBS Lett 570(1-3):155-60 {{SGDpaper|S000076690}} PMID 15251457</ref><ref name='S000076464'>Xu X, et al. (2004) Expression and characterization of Saccharomyces cerevisiae Cne1p, a calnexin homologue. J Biochem 135(5):615-8 {{SGDpaper|S000076464}} PMID 15173200</ref><ref name='S000039200'>Parlati F, et al. (1995) Saccharomyces cerevisiae CNE1 encodes an endoplasmic reticulum (ER) membrane protein with sequence similarity to calnexin and calreticulin and functions as a constituent of the ER quality control apparatus. J Biol Chem 270(1):244-53 |
{{SGDpaper|S000039200}} PMID 7814381</ref> | {{SGDpaper|S000039200}} PMID 7814381</ref> | ||
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Revision as of 14:05, 22 December 2007
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| Systematic name | YAL058W |
| Gene name | CNE1 |
| Aliases | FUN48 |
| Feature type | ORF, Verified |
| Coordinates | Chr I:37465..38973 |
| Primary SGDID | S000000054 |
Description of YAL058W: Calnexin; integral membrane ER chaperone involved in folding and quality control of glycoproteins; chaperone activity is inhibited by Mpd1p, with which Cne1p interacts; 24% identical to mammalian calnexin; Ca+ binding not yet shown in yeast[1][2][3][4]
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References
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- Jump up ↑ Kimura T, et al. (2005) Interactions among Yeast Protein-Disulfide Isomerase Proteins and Endoplasmic Reticulum Chaperone Proteins Influence Their Activities. J Biol Chem 280(36):31438-41 SGD PMID 16002399
- Jump up ↑ Xu X, et al. (2004) P-domain and lectin site are involved in the chaperone function of Saccharomyces cerevisiae calnexin homologue. FEBS Lett 570(1-3):155-60 SGD PMID 15251457
- Jump up ↑ Xu X, et al. (2004) Expression and characterization of Saccharomyces cerevisiae Cne1p, a calnexin homologue. J Biochem 135(5):615-8 SGD PMID 15173200
- Jump up ↑ Parlati F, et al. (1995) Saccharomyces cerevisiae CNE1 encodes an endoplasmic reticulum (ER) membrane protein with sequence similarity to calnexin and calreticulin and functions as a constituent of the ER quality control apparatus. J Biol Chem 270(1):244-53 SGD PMID 7814381
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