Cartoon diagram of pig colipase (blue) in complex with human pancreatic lipase and a small molecule inhibitor. From PDB 1LPB.
Symbol CLPS
External IDs OMIM120105 MGI88421 HomoloGene1383 GeneCards: CLPS Gene
Species Human Mouse
Entrez 1208 109791
Ensembl ENSG00000137392 ENSMUSG00000024225
UniProt P04118 Q9CQC2
RefSeq (mRNA) NM_001832 NM_025469
RefSeq (protein) NP_001823 NP_079745
Location (UCSC) Chr 6:
35.87 – 35.87 Mb
Chr 17:
28.7 – 28.7 Mb
PubMed search [1] [2]

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]

Colipase N-terminal domain
PDB 1lpb EBI.jpg
Structure of the pancreatic lipase-colipase complex inhibited by a C11 alkyl phosphonate.[4]
Symbol Colipase
Pfam PF01114
InterPro IPR001981
SCOP 1lpb
Colipase C-terminal domain
PDB 1pcn EBI.jpg
solution structure of porcine pancreatic procolipase as determined from 1h homonuclear two-and three-dimensional nmr
Symbol Colipase_C
Pfam PF02740
InterPro IPR017914
SCOP 1lpb

See also


  1. ^ Davis RC, Xia YR, Mohandas T, Schotz MC, Lusis AJ (May 1991). "Assignment of the human pancreatic colipase gene to chromosome 6p21.1 to pter". Genomics 10 (1): 262–5. doi:10.1016/0888-7543(91)90509-D. PMID 2045105. 
  2. ^ Lowe ME (1997). "Structure and function of pancreatic lipase and colipase". Annu. Rev. Nutr. 17: 141–158. doi:10.1146/annurev.nutr.17.1.141. PMID 9240923. 
  3. ^ a b Verger R, van Tilbeurgh H, Cambillau C, Bezzine S, Carriere F (1999). "Colipase: structure and interaction with pancreatic lipase". Biochim. Biophys. Acta 1441 (2-3): 173–184. PMID 10570245. 
  4. ^ Egloff MP, Marguet F, Buono G, Verger R, Cambillau C, van Tilbeurgh H (March 1995). "The 2.46 A resolution structure of the pancreatic lipase-colipase complex inhibited by a C11 alkyl phosphonate". Biochemistry 34 (9): 2751–62. doi:10.1021/bi00009a003. PMID 7893686. 

Further reading

External links

This article includes text from the public domain Pfam and InterPro IPR001981