Colipase

CLPS
Identifiers
Aliases	CLPS, entrez:1208, colipase
External IDs	OMIM: 120105; MGI: 88421; HomoloGene: 1383; GeneCards: CLPS; OMA:CLPS - orthologs
Gene location (Human) Chr. Chromosome 6 (human) Band 6p21.31 Start 35,794,982 bp End 35,797,344 bp
Gene location (Mouse) Chr. Chromosome 17 (mouse) Band 17|17 A3.3 Start 28,777,123 bp End 28,779,740 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in body of pancreas islet of Langerhans testicle pancreatic epithelial cell beta cell right coronary artery ectocervix right uterine tube Descending thoracic aorta right lobe of liver Top expressed in stomach islet of Langerhans jejunum duodenum colon ileum esophagus morula quadriceps femoris muscle yolk sac More reference expression data BioGPS More reference expression data
Gene ontology Molecular function enzyme activator activity Cellular component extracellular region Biological process lipid catabolic process digestion positive regulation of catalytic activity lipid metabolism response to food response to bacterium retinoid metabolic process lipid digestion Sources:Amigo / QuickGO
Orthologs Species Human Mouse 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 Mb Chr 17: 28.78 – 28.78 Mb PubMed search
Wikidata
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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.

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

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.

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.

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 SCOP2 1lpb / SCOPe / SUPFAM CDD cd00039 Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary PDB 1eth​, 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
Symbol	Colipase_C
Pfam	PF02740
InterPro	IPR017914
PROSITE	PDOC00111
SCOP2	1lpb / SCOPe / SUPFAM
CDD	cd00039
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

See also

• Enterostatin

Further reading

• Weyrich P, Albet S, Lammers R, et al. (2009). "Genetic variability of procolipase associates with altered insulin secretion in non-diabetic Caucasians". Exp. Clin. Endocrinol. Diabetes. 117 (2): 83–7. doi:10.1055/s-2008-1078733. PMID 18726866.
• Crandall WV, Lowe ME (2001). "Colipase residues Glu64 and Arg65 are essential for normal lipase-mediated fat digestion in the presence of bile salt micelles". J. Biol. Chem. 276 (16): 12505–12. doi:10.1074/jbc.M009986200. PMID 11278590.
• Miled N, Canaan S, Dupuis L, et al. (2000). "Digestive lipases: from three-dimensional structure to physiology". Biochimie. 82 (11): 973–86. doi:10.1016/S0300-9084(00)01179-2. PMID 11099794.
• van Tilbeurgh H, Egloff MP, Martinez C, et al. (1993). "Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography". Nature. 362 (6423): 814–20. doi:10.1038/362814a0. PMID 8479519.
• Wermter AK, Scherag A, Holter K, et al. (2009). "Procolipase gene: no association with early-onset obesity or fat intake". Obes Facts. 2 (1): 40–4. doi:10.1159/000196379. PMC 6444705. PMID 20054203.
• Lindner I, Helwig U, Rubin D, et al. (2005). "Putative association between a new polymorphism in exon 3 (Arg109Cys) of the pancreatic colipase gene and type 2 diabetes mellitus in two independent Caucasian study populations". Mol Nutr Food Res. 49 (10): 972–6. doi:10.1002/mnfr.200500087. PMID 16189801.
• Sims HF, Lowe ME (1992). "The human colipase gene: isolation, chromosomal location, and tissue-specific expression". Biochemistry. 31 (31): 7120–5. doi:10.1021/bi00146a013. PMID 1643046.
• Lowe ME, Rosenblum JL, McEwen P, Strauss AW (1990). "Cloning and characterization of the human colipase cDNA". Biochemistry. 29 (3): 823–8. doi:10.1021/bi00455a032. PMID 2337598.
• van Tilbeurgh H, Bezzine S, Cambillau C, et al. (1999). "Colipase: structure and interaction with pancreatic lipase". Biochim. Biophys. Acta. 1441 (2–3): 173–84. doi:10.1016/s1388-1981(99)00149-3. PMID 10570245.
• D'Silva S, Xiao X, Lowe ME (2007). "A polymorphism in the gene encoding procolipase produces a colipase, Arg92Cys, with decreased function against long-chain triglycerides". J. Lipid Res. 48 (11): 2478–84. doi:10.1194/jlr.M700371-JLR200. PMC 3684974. PMID 17715423.{{cite journal}}: CS1 maint: unflagged free DOI (link)
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Sternby B, Engström A, Hellman U, et al. (1984). "The primary sequence of human pancreatic colipase". Biochim. Biophys. Acta. 784 (1): 75–80. doi:10.1016/0167-4838(84)90175-4. PMID 6691986.
• Sias B, Ferrato F, Grandval P, et al. (2004). "Human pancreatic lipase-related protein 2 is a galactolipase". Biochemistry. 43 (31): 10138–48. doi:10.1021/bi049818d. PMID 15287741.
• Lowe ME (1997). "Structure and function of pancreatic lipase and colipase". Annu. Rev. Nutr. 17: 141–58. doi:10.1146/annurev.nutr.17.1.141. PMID 9240923.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Sugar IP, Mizuno NK, Momsen MM, et al. (2003). "Regulation of lipases by lipid-lipid interactions: implications for lipid-mediated signaling in cells". Chem. Phys. Lipids. 122 (1–2): 53–64. doi:10.1016/S0009-3084(02)00178-0. PMID 12598038.
• van Tilbeurgh H, Sarda L, Verger R, Cambillau C (1992). "Structure of the pancreatic lipase-procolipase complex". Nature. 359 (6391): 159–62. doi:10.1038/359159a0. PMID 1522902.
• Davis RC, Xia YR, Mohandas T, et al. (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.

External links

• Colipases at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
• PDBe-KB provides an overview of all the structure information available in the PDB for Pig Colipase

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