Colipase

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Colipase N-terminal domain
	Structure of the pancreatic lipase-colipase complex inhibited by a C11 alkyl phosphonate.
Identifiers
Symbol	Colipase
Pfam	PF01114
InterPro	IPR001981
PROSITE	PDOC00111
SCOP	1lpb
SUPERFAMILY	1lpb
CDD	cd00039
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Colipase, pancreatic
Colipase, pancreatic
	250px Cartoon diagram of pig colipase (blue) in complex with human pancreatic lipase and a small molecule inhibitor. From PDB: 1LPB.
Identifiers
Symbol	CLPS
External IDs	OMIM: 120105 MGI: 88421 HomoloGene: 1383 GeneCards: CLPS Gene
Gene ontology
Molecular function	• enzyme activator activity;
Cellular component	• extracellular region; • extracellular exosome;
Biological process	• retinoid metabolic process; • lipid metabolic process; • phototransduction, visible light; • post-embryonic development; • lipid catabolic process; • response to food; • positive regulation of catalytic activity; • lipid digestion; • small molecule metabolic process;
	Sources: Amigo / QuickGO
Orthologs
Species	Human
Entrez	1208
Ensembl	ENSG00000137392
UniProt	P04118
RefSeq (mRNA)	NM_001252597
RefSeq (protein)	NP_001239526
Location (UCSC)	Chr 6:; 35.79 – 35.8 Mb
PubMed search	[1]
	v; t; e;

Colipase is a protein co-enzyme required for optimal enzyme activity of pancreatic lipase. It is secreted by the pancreas in an inactive form, procolipase, which is activated in the intestinal lumen by trypsin. Its function is to prevent the inhibitory effect of bile salts on the lipase-catalyzed intraduodenal hydrolysis of dietary long-chain triglycerides.

In humans, the colipase protein is encoded by the CLPS gene.^[1]

Protein domain

Colipase is also a family of evolutionarily related proteins.

Colipase is a small protein cofactor needed by pancreatic lipase for efficient dietary lipid hydrolyisis. 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 an active conformation and considerably increasing the hydrophobicity binding site. Structural studies of the complex and of colipase alone have revealed the functionality of its architecture.^[2]^[3]

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.^[3]