PLB1 is a membrane-associated phospholipase which exhibits a calcium-independent broad substrate specificity including phospholipase A2/lysophospholipase activity. It shows preferential hydrolysis at the sn-2 position of diacylphospholipids and diacyglycerol, whereas it shows no positional specificity toward triacylglycerol. It also exhibits esterase activity toward p-nitrophenyl. It may act on the brush border membrane to facilitate the absorption of digested lipids.
Function:
Membrane-associated phospholipase. Exhibits a calcium-independent broad substrate specificity including phospholipase A2/lysophospholipase activity. Preferential hydrolysis at the sn-2 position of diacylphospholipids and diacyglycerol, whereas it shows no positional specificity toward triacylglycerol. Exhibits also esterase activity toward p-nitrophenyl. May act on the brush border membrane to facilitate the absorption of digested lipids (By similarity).
Subcellular Location:
Apical cell membrane; Single-pass type I membrane protein. Note: Present in the intestinal brush border membranes.
Tissue Specificity:
Expressed in the epidermis (at protein level).
Post-translational modifications:
Undergoes proteolytic cleavage in the ileum.
Similarity:
Belongs to the 'GDSL' lipolytic enzyme family. Phospholipase B1 subfamily.
SWISS:
Q6P1J6
Gene ID:
151056
Database links:
Entrez Gene: 151056 Human
Omim: 610179 Human
SwissProt: Q6P1J6 Human
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