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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
Pancreatic lipase–colipase complex with inhibitor 1LPB.png
Identifiers
AliasesCLPS, entrez:1208, colipase
External IDsOMIM: 120105 MGI: 88421 HomoloGene: 1383 GeneCards: CLPS
Gene location (Human)
Chromosome 6 (human)
Chr.Chromosome 6 (human)[1]
Chromosome 6 (human)
Genomic location for CLPS
Genomic location for CLPS
Band6p21.31Start35,794,982 bp[1]
End35,797,344 bp[1]
RNA expression pattern
PBB GE PNPLA6 203718 at tn.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
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: 28.56 – 28.56 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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

Protein domainEdit

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
SCOPe1lpb / SUPFAM
CDDcd00039
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
SCOPe1lpb / SUPFAM
CDDcd00039

See alsoEdit

ReferencesEdit

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000137392 - Ensembl, May 2017
  2. ^ a b c 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. ^ 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. 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 readingEdit

External linksEdit

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