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Literature summary for 3.1.4.12 extracted from

  • Jenkins, R.W.; Idkowiak-Baldys, J.; Simbari, F.; Canals, D.; Roddy, P.; Riner, C.D.; Clarke, C.J.; Hannun, Y.A.
    A novel mechanism of lysosomal acid sphingomyelinase maturation: requirement for carboxyl-terminal proteolytic processing (2011), J. Biol. Chem., 286, 3777-3788.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of V5-tagged unprocessed aSMase in MCF-7 and HEK-293 cells Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
desipramine inhibits the processed lysosomal L-SMase Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular secreted aSMase, S-SMase Homo sapiens
-
-
lysosome lysosomal aSMase, L-SMase Homo sapiens 5764
-

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ aSMase is processed from a 75-kDa, Zn2+-activated proenzyme to a mature 65 kDa, Zn2+-independent L-SMase Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification aSMase is processed from a 75-kDa, Zn2+-activated proenzyme to a mature 65 kDa, Zn2+-independent L-SMase, C-terminal proteolytic processing Homo sapiens

Synonyms

Synonyms Comment Organism
acid sphingomyelinase
-
Homo sapiens
aSMase
-
Homo sapiens

General Information

General Information Comment Organism
additional information aSMase exists in two forms: a Zn2+-independent lysosomal aSMase, L-SMase, and a Zn2+-dependent secreted aSMase, S-SMase, that arise from alternative trafficking of a single protein precursor. Mechanism of aSMase maturation involving C-terminal proteolytic processing within, or in close proximity to, endolysosomes, overview Homo sapiens