Conserved Site

Colipase, conserved site (IPR017915)

Short name: Colipase_CS

Description

Colipase [PMID: 1567900, PMID: 3147715] is a small protein cofactor needed by pancreatic lipase for efficient dietary lipid hydrolyisis. It also binds to the bile-salt covered triacylglycerol interface, thus allowing the enzyme to anchor itself to the water-lipid interface. Efficient absorption of dietary fats is dependent on the action of pancreatic triglyceride lipase. Colipase binds to the C-terminal, non-catalytic domain of lipase, thereby stabilising as active conformation and considerably increasing the overall hydrophobic binding site. Structural studies of the complex and of colipase alone have revealed the functionality of its architecture [PMID: 9240923, PMID: 10570245].

Colipase is a small protein with five conserved disulphide bonds. Structural analogies have been recognised between a developmental protein (Dickkopf), the pancreatic lipase C-terminal domain, the N-terminal domains of lipoxygenases and the C-terminal domain of alpha-toxin. These non-catalytic domains in the latter enzymes are important for interaction with membrane. It has not been established if these domains are also involved in eventual protein cofactor binding as is the case for pancreatic lipase [PMID: 10570245].

This entry represents a conserved site within colipase enzymes, covering two of the cysteines involved in disulphide bond formation, as well as three tyrosine residues which seem to be involved in the interfacial binding.

GO terms

Biological Process

GO:0007586 digestion
GO:0016042 lipid catabolic process

Molecular Function

GO:0008047 enzyme activator activity

Cellular Component

GO:0005576 extracellular region

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns