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7  structures 36  species 3  interactions 50  sequences 2  architectures

Family: Colipase (PF01114)

Summary: Colipase, N-terminal domain

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Colipase Edit Wikipedia article

Colipase, pancreatic
Pancreatic lipase–colipase complex with inhibitor 1LPB.png
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 OMIM120105 MGI88421 HomoloGene1383 GeneCards: CLPS Gene
Orthologs
Species Human Mouse
Entrez 1208 109791
Ensembl ENSG00000137392 ENSMUSG00000024225
UniProt P04118 Q9CQC2
RefSeq (mRNA) NM_001252597 NM_025469
RefSeq (protein) NP_001239526 NP_079745
Location (UCSC) Chr 6:
35.76 – 35.77 Mb
Chr 17:
28.56 – 28.56 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]
Identifiers
Symbol Colipase
Pfam PF01114
InterPro IPR001981
PROSITE PDOC00111
SCOP 1lpb
SUPERFAMILY 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
Identifiers
Symbol Colipase_C
Pfam PF02740
InterPro IPR017914
PROSITE PDOC00111
SCOP 1lpb
SUPERFAMILY 1lpb

See also

References

  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. doi:10.1016/s1388-1981(99)00149-3. 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 incorporates text from the public domain Pfam and InterPro IPR001981


This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Colipase, N-terminal domain Provide feedback

SCOP reports duplication of common fold with Colipase C-terminal domain.

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR017913

This entry represents the N-terminal domain of colipase proteins. Colipase [PUBMED:1567900, PUBMED:3147715] is a small protein cofactor needed by pancreatic lipase for efficient dietary lipid hydrolyisis. It also binds to the bile-salt covered triacylglycerol interface, thus allowing the enzyme to anchor itself to the water-lipid interface. 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 as active conformation and considerably increasing the overall hydrophobic binding site. Structural studies of the complex and of colipase alone have revealed the functionality of its architecture [PUBMED:9240923, PUBMED:10570245].

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 [PUBMED:10570245].

Gene Ontology

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Domain organisation

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Alignments

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

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(9)
Full
(50)
Representative proteomes NCBI
(47)
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(3)
RP35
(3)
RP55
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RP75
(28)
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  Seed
(9)
Full
(50)
Representative proteomes NCBI
(47)
Meta
(0)
RP15
(3)
RP35
(3)
RP55
(7)
RP75
(28)
Alignment:
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  Seed
(9)
Full
(50)
Representative proteomes NCBI
(47)
Meta
(0)
RP15
(3)
RP35
(3)
RP55
(7)
RP75
(28)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

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Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Prosite
Previous IDs: none
Type: Domain
Author: Finn RD, Bateman A, Griffiths-Jones SR
Number in seed: 9
Number in full: 50
Average length of the domain: 39.20 aa
Average identity of full alignment: 63 %
Average coverage of the sequence by the domain: 37.13 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 19.4 19.4
Trusted cut-off 19.6 24.9
Noise cut-off 19.1 17.1
Model length: 40
Family (HMM) version: 13
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Species distribution

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Interactions

There are 3 interactions for this family. More...

Colipase_C Lipase PLAT

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Colipase domain has been found. There are 7 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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