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16  structures 255  species 3  interactions 1975  sequences 31  architectures

Family: Lipase (PF00151)

Summary: Lipase

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "Pancreatic lipase family". More...

Pancreatic lipase family Edit Wikipedia article

1lpa opm.gif
Complex of human pancreatic lipase with colipase
Identifiers
Symbol Lipase
Pfam PF00151
InterPro IPR013818
PROSITE PDOC00110
SCOP 1lpa
SUPERFAMILY 1lpa
OPM protein 1lpa

Triglyceride lipases (EC 3.1.1.3) are a family of lipolytic enzymes that hydrolyse ester linkages of triglycerides.[1] Lipases are widely distributed in animals, plants and prokaryotes.

At least three tissue-specific isozymes exist in higher vertebrates, pancreatic, hepatic and gastric/lingual. These lipases are closely related to each other and to lipoprotein lipase (EC 3.1.1.34), which hydrolyses triglycerides of chylomicrons and very low density lipoproteins (VLDL).[2]

The most conserved region in all these proteins is centred around a serine residue which has been shown[3] to participate, with an histidine and an aspartic acid residue, in a charge relay system. Such a region is also present in lipases of prokaryotic origin and in lecithin-cholesterol acyltransferase (EC 2.3.1.43) (LCAT),[4] which catalyzes fatty acid transfer between phosphatidylcholine and cholesterol.

Human proteins containing this domain[edit]

LIPC; LIPG; LIPH; LIPI; LPL; PLA1A; PNLIP; PNLIPRP1; PNLIPRP2; PNLIPRP3;

References[edit]

  1. ^ Chapus C, Rovery M, Sarda L, Verger R (1988). "Minireview on pancreatic lipase and colipase". Biochimie 70 (9): 1223–1234. doi:10.1016/0300-9084(88)90188-5. PMID 3147715. 
  2. ^ Persson B, Bengtsson-Olivecrona G, Enerback S, Olivecrona T, Jornvall H (1989). "Structural features of lipoprotein lipase. Lipase family relationships, binding interactions, non-equivalence of lipase cofactors, vitellogenin similarities and functional subdivision of lipoprotein lipase". Eur. J. Biochem. 179 (1): 39–45. doi:10.1111/j.1432-1033.1989.tb14518.x. PMID 2917565. 
  3. ^ Blow D (1990). "Enzymology. More of the catalytic triad". Nature 343 (6260): 694–695. doi:10.1038/343694a0. PMID 2304545. 
  4. ^ McLean J, Fielding C, Drayna D, Dieplinger H, Baer B, Kohr W, Henzel W, Lawn R (1986). "Cloning and expression of human lecithin-cholesterol acyltransferase cDNA". Proc. Natl. Acad. Sci. U.S.A. 83 (8): 2335–2339. doi:10.1073/pnas.83.8.2335. PMC 323291. PMID 3458198. 

Further reading[edit]

  • Roussel A, Yang Y, Ferrato F, Verger R, Cambillau C, Lowe M (November 1998). "Structure and activity of rat pancreatic lipase-related protein 2". J. Biol. Chem. 273 (48): 32121–8. PMID 9822688. 

This article incorporates text from the public domain Pfam and InterPro IPR013818


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.

Lipase Provide feedback

No Pfam abstract.

Literature references

  1. Roussel A, Yang Y, Ferrato F, Verger R, Cambillau C, Lowe M; , J Biol Chem 1998;273:32121-32128.: Structure and activity of rat pancreatic lipase-related protein 2. PUBMED:9822688 EPMC:9822688


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR013818

Triglyceride lipases (EC) are lipolytic enzymes that hydrolyse ester linkages of triglycerides [PUBMED:3147715]. Lipases are widely distributed in animals, plants and prokaryotes. At least three tissue-specific isozymes exist in higher vertebrates, pancreatic, hepatic and gastric/lingual. These lipases are closely related to each other and to lipoprotein lipase (EC), which hydrolyses triglycerides of chylomicrons and very low density lipoproteins (VLDL) [PUBMED:2917565]. The most conserved region in all these proteins is centred around a serine residue which has been shown [PUBMED:2304545] to participate, with an histidine and an aspartic acid residue, in a charge relay system. Such a region is also present in lipases of prokaryotic origin and in lecithin-cholesterol acyltransferase (EC) (LCAT) [PUBMED:3458198], which catalyzes fatty acid transfer between phosphatidylcholine and cholesterol.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...

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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.

  Seed
(16)
Full
(1975)
Representative proteomes NCBI
(2017)
Meta
(14)
RP15
(307)
RP35
(390)
RP55
(782)
RP75
(1058)
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Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(16)
Full
(1975)
Representative proteomes NCBI
(2017)
Meta
(14)
RP15
(307)
RP35
(390)
RP55
(782)
RP75
(1058)
Alignment:
Format:
Order:
Sequence:
Gaps:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(16)
Full
(1975)
Representative proteomes NCBI
(2017)
Meta
(14)
RP15
(307)
RP35
(390)
RP55
(782)
RP75
(1058)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

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.

Pfam alignments:

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

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.

Note: You can also download the data file for the tree.

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: lipase;
Type: Domain
Author: Sonnhammer ELL, Griffiths-Jones SR
Number in seed: 16
Number in full: 1975
Average length of the domain: 262.60 aa
Average identity of full alignment: 27 %
Average coverage of the sequence by the domain: 71.62 %

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 20.1 20.1
Trusted cut-off 20.1 20.1
Noise cut-off 20.0 20.0
Model length: 331
Family (HMM) version: 14
Download: download the raw HMM for this family

Species distribution

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Interactions

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

Colipase PLAT Lipase

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 Lipase domain has been found. There are 16 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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