The domain within your query sequence starts at position 22 and ends at position 102; the E-value for the Colipase-like domain shown below is 1.3e-17.
HSENSPPKKANGDKCVHHTQCSSDCCLIDLERSGAFCTPKSRIGMGCLPQTKGSLNIMCP CRSGLNCHSKDPTCPRRCQMI
Colipase-like |
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| PFAM accession number: | PF15083 |
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| Interpro abstract (IPR001981): | Colipase [ (PUBMED:1567900) (PUBMED: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 [ (PUBMED:9240923) (PUBMED: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 [ (PUBMED:10570245) ]. |
| GO process: | lipid catabolic process (GO:0016042), digestion (GO:0007586) |
| GO component: | extracellular region (GO:0005576) |
| GO function: | enzyme activator activity (GO:0008047) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry Colipase-like