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 Gen. Subj., 1861, 3119-3128 .

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Protein Variants

Protein Variants	Comment	Organism
additional information	removal of domain I (LPHDELTA1) results in a malfolded ER-localized protein. Enzyme without domain II (LPHDELTA2) is normally transported along the secretory pathway, but does not dimerize nor is enzymatically active. The lactase activity is not detectable in LPHDELTA1 and LPHDELTA2. Phlorizin hydrolase activity is only detectable in LPHDELTA2, albeit at substantially reduced levels of 4.3%	Homo sapiens

Localization

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

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P09848	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	membrane anchored type I glycoprotein	Homo sapiens

Source Tissue

Source Tissue	Comment	Organism	Textmining
intestinal epithelium	-	Homo sapiens	-

Synonyms

Synonyms	Comment	Organism
lactase-phlorizin hydrolase	-	Homo sapiens
LPH	-	Homo sapiens

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Release 2023.1 (January 2023)