Colipase

Colipase, abbreviated CLPS, 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.

CLPS
Identifiers
AliasesCLPS, entrez:1208, colipase
External IDsOMIM: 120105 MGI: 88421 HomoloGene: 1383 GeneCards: CLPS
Orthologs
SpeciesHumanMouse
Entrez

1208

109791

Ensembl

ENSG00000137392

ENSMUSG00000024225

UniProt

P04118

Q9CQC2

RefSeq (mRNA)

NM_001832
NM_001252597
NM_001252598

NM_025469
NM_001317065

RefSeq (protein)

NP_001239526
NP_001239527
NP_001823

NP_001303994
NP_079745

Location (UCSC)Chr 6: 35.79 – 35.8 MbChr 17: 28.78 – 28.78 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

In humans, the colipase protein is encoded by the CLPS gene.[5]

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 hydrolysis. 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 of its binding site. Structural studies of the complex and of colipase alone have revealed the functionality of its architecture.[6][7]

Colipase is a small protein (12K) 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.[7]

Colipase N-terminal domain
Structure of the pancreatic lipase-colipase complex inhibited by a C11 alkyl phosphonate.[8]
Identifiers
SymbolColipase
PfamPF01114
InterProIPR001981
PROSITEPDOC00111
SCOP21lpb / SCOPe / SUPFAM
CDDcd00039
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1eth, 1lpa, 1lpb, 1n8s, 1pcn, 1pco
Colipase C-terminal domain
solution structure of porcine pancreatic procolipase as determined from 1h homonuclear two-and three-dimensional nmr
Identifiers
SymbolColipase_C
PfamPF02740
InterProIPR017914
PROSITEPDOC00111
SCOP21lpb / SCOPe / SUPFAM
CDDcd00039
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

See also

References

  1. GRCh38: Ensembl release 89: ENSG00000137392 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000024225 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. 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.
  6. 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.
  7. 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. doi:10.1016/s1388-1981(99)00149-3. PMID 10570245.
  8. 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

This article incorporates text from the public domain Pfam and InterPro: IPR001981


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