Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase.
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Eug1p is a soluble ER protein induced by ER protein accumulation; overexpression can support growth without Pdi1p but only partially restores a vacuolar glycoprotein-folding phenotype.
"The product of the EUG1 gene of Saccharomyces cerevisiae is a soluble endoplasmic reticulum protein with homology to both the mammalian protein disulfide isomerase (PDI) and the yeast PDI homolog encoded by the essential PDI1 gene."
Mutation of yeast Eug1p CXXS active sites to CXXC results in a dramatic increase in protein disulphide isomerase activity.
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Native CXXS Eug1p has very little oxidative-refolding or isomerase-only activity, whereas CXXC mutants approach genuine PDI activity.
"The wild-type protein showed very little activity, not only in oxidative refolding but also in assays where only isomerase activity was required."
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The authors conclude that general disulfide isomerization is not Eug1p's main in-vivo function.
"These results lead us to propose that general disulphide isomerization is not the main function of Eug1p in vivo."
Functional differences in yeast protein disulfide isomerases.
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Eug1p is not functionally interchangeable with Pdi1p: EUG1 suppression of pdi1 deletion requires endogenous CXXC-containing homologues, and PDI family mutant combinations impair CPY folding.
"This shows that the homologues are not functionally interchangeable."
Subcellular localization of the yeast proteome.
Interactions among yeast protein-disulfide isomerase proteins and endoplasmic reticulum chaperone proteins influence their activities.
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Eug1p has 2.16% of Pdi1p oxidative-refolding activity in the reported assay.
"Mpd1p, Mpd2, and Eug1p exhibit activities of 13.8, 16.0, and 2.16%, respectively, compared with Pdi1p"
One library to make them all: streamlining the creation of yeast libraries via a SWAp-Tag strategy.
An inter-species protein-protein interaction network across vast evolutionary distance.
Falcon deep research report for EUG1
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The synthesis interprets Eug1p as a specialized component of a cooperative ER redox-folding network rather than a standalone replacement for Pdi1p.
"Eug1p supplies a specialized component of a cooperative redox network."