Literature summary for 3.1.1.4 extracted from

Hiraoka, M.; Okamoto, K.; Ohguro, H.; Abe, A.
Role of N-glycosylation of human lysosomal phospholipase A2 for the formation of catalytically active enzyme (2013), J. Lipid Res., 54, 3098-3105.

Search for more literature for 3.1.1.4

Cloned(Commentary)

Cloned (Comment)	Organism
expression in COS-7 cell	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
N273	mutation in potential N-glycosylation site, reduction in catalytic activity, mutant is recovered in the soluble fraction	Homo sapiens
N289	mutation in potential N-glycosylation site, reduction in catalytic activity, mutant is recovered in the soluble fraction	Homo sapiens
N398	mutation in potential N-glycosylation site, reduction in catalytic activity, mutant is recovered in the soluble fraction	Homo sapiens
N99	mutation in potential N-glycosylation site, marked reduction in catalytic activity, mutant is mostly retained in the membrane fraction	Homo sapiens
N99/N273/N289/N398	mutation in all potential glycosylation sites, loss of catalyic activity	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
lysosome	-	Homo sapiens	5764	-

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q8NCC3	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	isoform LPLA2 contains four potential N-glycosylation sites. Single mutation at potential glycosylation sites N273, N289, or N398 partially reduces production of active enzyme. Single mutation at N99 and quadruple mutations at all four Asn sites results in a marked reduction of active LPLA2 and loss of active LPLA2, respectively	Homo sapiens

Synonyms

Synonyms	Comment	Organism
Lpla2	-	Homo sapiens
lysosomal phospholipase A2	-	Homo sapiens

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Release 2023.1 (January 2023)