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Literature summary for 3.2.1.106 extracted from

  • Saint-Jore-Dupas, C.; Nebenfuehr, A.; Boulaflous, A.; Follet-Gueye, M.L.; Plasson, C.; Hawes, C.; Driouich, A.; Faye, L.; Gomord, V.
    Plant N-glycan processing enzymes employ different targeting mechanisms for their spatial arrangement along the secretory pathway (2006), Plant Cell, 18, 3182-3200.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.2.1.106

Cloned(Commentary)

Cloned (Comment) Organism
full-length Arabidopsis GCSI fused to GFP, stable expression in tobacco BY-2 cells Arabidopsis thaliana

Protein Variants

Protein Variants Comment Organism
additional information removal of the first 11 amino acids of the GCSI cytoplasmic tail results in relocalization from the endoplasmic reticulum to the Golgi apparatus Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum with cytoplasmic tail, which is crucial for endoplasmic reticulum retention, thus there is a targeting mechanism relying on protein-protein interaction Arabidopsis thaliana 5783
-
membrane endoplasmic reticulum resident membrane protein, the 18-amino acid long transmembrane domain of GCSI is not sufficient to target this glycosidase in the endoplasmic reticulum membrane Arabidopsis thaliana 16020
-

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
-
-

Synonyms

Synonyms Comment Organism
GCSI
-
 Arabidopsis thaliana
glucosidase I
-
 Arabidopsis thaliana