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Literature summary for 3.2.1.108 extracted from

  • Diekmann, L.; Behrendt, M.; Amiri, M.; Naim, H.Y.
    Structural determinants for transport of lactase phlorizin-hydrolase in the early secretory pathway as a multi-domain membrane glycoprotein (2017), Biochim. Biophys. Acta, 1861, 3119-3128 .
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information the enzyme without domain II (LPHDELTA2) is normally transported along the secretory pathway, but does not dimerize nor is enzymatically active Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum
-
Homo sapiens 5783
-
membrane
-
Homo sapiens 16020
-

Organism

Organism UniProt Comment Textmining
Homo sapiens P09848
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein the polypeptide stretch in domain II between L735-R868 harbors a unique N-glycosylation site that is responsible for lactase phlorizin-hydrolase retention in the endoplasmic reticulum via association with calnexin and facilitates proper folding of domains I and III before ER exit of lactase phlorizin-hydrolase. A similar N-glycosylation site in domain IV shows comparable effects on the trafficking of lactase phlorizin-hydrolase-derived molecules Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
intestinal epithelium
-
Homo sapiens
-

Synonyms

Synonyms Comment Organism
lactase phlorizin-hydrolase
-
Homo sapiens