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Literature summary for 1.16.3.1 extracted from
- Core glycan in the yeast multicopper ferroxidase, Fet3p: a case study of N-linked glycosylation, protein maturation, and stability (2010), Protein Sci., 19, 1739-1750.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of FLAG-tagged wild-type and mutants N113A and N194A | Saccharomyces cerevisiae |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | truncation of the C-terminal transmembrane domain leading to a soluble enzyme form, sFet3p, that is secreted from the cell, structure comparison with the wild-type enzyme, overview. The apparent trafficking defect observed with alanine substitution at some asparagines in sFet3p is not observed in the full-length, membrane-tethered protein | Saccharomyces cerevisiae |
| N113A | site-directed mutagenesis of a potential N-glycosylation site. The mutant shows Fe uptake and turnover altered kinetics, but steady-state localization in the plasma membrane like the wild-type enzyme | Saccharomyces cerevisiae |
| N194A | site-directed mutagenesis of a potential N-glycosylation site. The mutant shows Fe uptake and turnover altered kinetics | Saccharomyces cerevisiae |
| N198A | site-directed mutagenesis of a potential N-glycosylation site. The mutant shows Fe uptake and turnover altered kinetics | Saccharomyces cerevisiae |
| N244A | site-directed mutagenesis of a potential N-glycosylation site | Saccharomyces cerevisiae |
| N265A | site-directed mutagenesis of a potential N-glycosylation site | Saccharomyces cerevisiae |
| N27A | site-directed mutagenesis of a potential N-glycosylation site | Saccharomyces cerevisiae |
| N292A | site-directed mutagenesis of a potential N-glycosylation site | Saccharomyces cerevisiae |
| N300A | site-directed mutagenesis of a potential N-glycosylation site | Saccharomyces cerevisiae |
| N359A | site-directed mutagenesis of a potential N-glycosylation site | Saccharomyces cerevisiae |
| N381A | site-directed mutagenesis of a potential N-glycosylation site | Saccharomyces cerevisiae |
| N74A | site-directed mutagenesis of a potential N-glycosylation site | Saccharomyces cerevisiae |
| N77A | site-directed mutagenesis of a potential N-glycosylation site. The mutant shows Fe uptake and turnover altered kinetics, but steady-state localization in the plasma membrane like the wild-type enzyme | Saccharomyces cerevisiae |
| N88A | site-directed mutagenesis of a potential N-glycosylation site | Saccharomyces cerevisiae |
| T307A | site-directed mutagenesis of a potential O-glycosylation site | Saccharomyces cerevisiae |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | core glycosylation suppresses Fet3p nascent chain aggregation during synthesis into the endoplasmic reticulum | Saccharomyces cerevisiae |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| plasma membrane | Fet3p has 11 crystallographically mapped N-linked core glycan units. Assembly of four of these units is specifically required for localization of Fet3p to the plasma membrane. Fet3 protein lacking any one of these glycan units is found in an intracellular high-molecular mass species, overview | Saccharomyces cerevisiae | 5886 | - |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | glycosylation occurs at N-linked Asn residues 27, 74, 88, 198, 244, 265, 292, 300, or 381, or at the putative O-linked T307 in native soluble sFet3p. Fet3p has 11 crystallographically mapped N-linked core glycan units. Assembly of four of these units is specifically required for localization of Fet3p to the plasma membrane. Core glycosylation suppresses Fet3p nascent chain aggregation during synthesis into the endoplasmic reticulum | Saccharomyces cerevisiae |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant FLAG-tagged wild-type and mutants N113A and N194A, treatment with EndoH glycosidase | Saccharomyces cerevisiae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| fet3p | - |
Saccharomyces cerevisiae |
| multicopper ferroxidase | - |
Saccharomyces cerevisiae |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
thermal denaturation analysis for wild-type and mutant sFet3 proteins, transition temperatures of 52-74°C, overview | Saccharomyces cerevisiae |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | core glycosylation suppresses Fet3p nascent chain aggregation during synthesis into the endoplasmic reticulum. Fet3 protein lacking any one of the glycan units is found in an intracellular high-molecular mass species. But the missing carbohydrate is not required for native structure and biologic activity | Saccharomyces cerevisiae |
| physiological function | native function includes the interaction with the iron permease, Ftr1p, and wild-type high-affinity iron uptake activity. The four essential sequons are found within relatively nonpolar regions located in surface recesses and are strongly conserved among fungal Fet3 proteins | Saccharomyces cerevisiae |
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