Please note: this site relies heavily on the use of javascript. Without a javascript-enabled browser, this site will not function correctly. Please enable javascript and reload the page, or switch to a different browser.
127  structures 2651  species 0  interactions 20296  sequences 415  architectures

Family: Lipase_3 (PF01764)

Summary: Lipase (class 3)

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 "Triacylglycerol lipase". More...

Triacylglycerol lipase Edit Wikipedia article

Triacylglycerol lipase
Identifiers
EC no.3.1.1.3
CAS no.9001-62-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Lipase (class 3)
PDB 3tgl EBI.jpg
Structure of Triacyl-glycerol acylhydrolase.
Identifiers
SymbolLipase_3
PfamPF01764
InterProIPR002921
PROSITEPDOC00110
SCOP23tgl / SCOPe / SUPFAM
OPM superfamily127
OPM protein3tgl
CDDcd00519

Triacylglycerol lipase (also Triglyceride lipase) EC 3.1.1.3, are enzymes that hydrolyse ester linkages of triglycerides.[1] These lipases are widely distributed in animals, plants and prokaryotes. This family was also called class 3 lipases as they are only distantly related to other lipase families.[2][3][4][5][6] This enzyme catalyses the following chemical reaction

triacylglycerol + H2O ⇌ diacylglycerol + a carboxylate

Human proteins containing this domain

DAGLA; DAGLB; LOC221955; The pancreatic enzyme acts only on an ester-water interface.

Nomenclature

Other names include lipase, butyrinase, tributyrinase, Tween hydrolase, steapsin, triacetinase, tributyrin esterase, Tweenase, amno N-AP, Takedo 1969-4-9, Meito MY 30, Tweenesterase, GA 56, capalase L, triglyceride hydrolase, triolein hydrolase, tween-hydrolyzing esterase, amano CE, cacordase, triglyceridase, triacylglycerol ester hydrolase, amano P, amano AP, PPL, glycerol-ester hydrolase, GEH, meito Sangyo OF lipase, hepatic lipase, lipazin, post-heparin plasma protamine-resistant lipase, salt-resistant post-heparin lipase, heparin releasable hepatic lipase, amano CES, amano B, tributyrase, triglyceride lipase, liver lipase, hepatic monoacylglycerol acyltransferase).

See also

References

  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. ^ Korn ED, Quigley TW (June 1957). "Lipoprotein lipase of chicken adipose tissue". The Journal of Biological Chemistry. 226 (2): 833–9. doi:10.1016/S0021-9258(18)70867-3. PMID 13438870.
  3. ^ Lynn WS, Perryman NC (July 1960). "Properties and purification of adipose tissue lipase". The Journal of Biological Chemistry. 235 (7): 1912–6. doi:10.1016/S0021-9258(18)69335-4. PMID 14419169.
  4. ^ Sarda L, Desnuelle P (December 1958). "[Actions of pancreatic lipase on esters in emulsions]". Biochimica et Biophysica Acta. 30 (3): 513–21. doi:10.1016/0006-3002(58)90097-0. PMID 13618257.
  5. ^ Singer, T.P.; Hofstee, B.H.J. (1948). "Studies on wheat germ lipase. I. Methods of estimation, purification and general properties of the enzyme". Arch. Biochem. 18 (2): 229–243. PMID 18875045.
  6. ^ Singer, T.P.; Hofstee, B.H.J. (1948). "Studies on wheat germ lipase. II. Kinetics". Arch. Biochem. 18 (2): 245–259. PMID 18875046.

External links

This article incorporates text from the public domain Pfam and InterPro: IPR002921

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

This is the Wikipedia entry entitled "Triglyceride lipase". More...

Triglyceride lipase Edit Wikipedia article

  • From a merge: This is a redirect from a page that was merged into another page. This redirect was kept in order to preserve this page's edit history after its content was merged into the target page's content. Please do not remove the tag that generates this text (unless the need to recreate content on this page has been demonstrated) or delete this page.

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 (class 3) Provide feedback

No Pfam abstract.

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR002921

This entry represents a domain with an alpha/beta hydrolase fold found in feruloyl esterase A [ PUBMED:15081808 ]. It is similar to that found in fungal lipases [ PUBMED:7656005 ].

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

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

Loading domain graphics...

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 (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

View options

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
(47)
Full
(20296)
Representative proteomes UniProt
(37397)
RP15
(4527)
RP35
(11019)
RP55
(17249)
RP75
(22851)
Jalview View  View  View  View  View  View  View 
HTML View             
PP/heatmap 1            

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(47)
Full
(20296)
Representative proteomes UniProt
(37397)
RP15
(4527)
RP35
(11019)
RP55
(17249)
RP75
(22851)
Alignment:
Format:
Order:
Sequence:
Gaps:
Download/view:

Download options

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
(47)
Full
(20296)
Representative proteomes UniProt
(37397)
RP15
(4527)
RP35
(11019)
RP55
(17249)
RP75
(22851)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download  
Gzipped 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.

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: Pfam-B_893 (release 4.2)
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Bashton M , Bateman A
Number in seed: 47
Number in full: 20296
Average length of the domain: 140.40 aa
Average identity of full alignment: 21 %
Average coverage of the sequence by the domain: 26.71 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 22.0 22.0
Trusted cut-off 22.0 22.0
Noise cut-off 21.9 21.9
Model length: 142
Family (HMM) version: 28
Download: download the raw HMM for this family

Species distribution

Sunburst controls

Hide

Weight segments by...


Change the size of the sunburst

Small
Large

Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence

Selections

Align selected sequences to HMM

Generate a FASTA-format file

Clear selection

This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

Loading sunburst data...

Tree controls

Hide

The tree shows the occurrence of this domain across different species. More...

Loading...

Please note: for large trees this can take some time. While the tree is loading, you can safely switch away from this tab but if you browse away from the family page entirely, the tree will not be loaded.

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_3 domain has been found. There are 127 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 sequence.

Loading structure mapping...

AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A0P0V7I2 View 3D Structure Click here
A0A0P0VBK1 View 3D Structure Click here
A0A0P0VBR4 View 3D Structure Click here
A0A0P0VM05 View 3D Structure Click here
A0A0P0W2G6 View 3D Structure Click here
A0A0P0WCB7 View 3D Structure Click here
A0A0P0WI13 View 3D Structure Click here
A0A0P0WL87 View 3D Structure Click here
A0A0P0WLY0 View 3D Structure Click here
A0A0P0X9X0 View 3D Structure Click here
A0A0P0XXD6 View 3D Structure Click here
A0A0P0Y0L8 View 3D Structure Click here
A0A0P0Y2C1 View 3D Structure Click here
A0A0P0YC44 View 3D Structure Click here
A0A0P0YCI2 View 3D Structure Click here
A0A0R0F2G9 View 3D Structure Click here
A0A0R0FEC7 View 3D Structure Click here
A0A0R0FFT1 View 3D Structure Click here
A0A0R0FMW4 View 3D Structure Click here
A0A0R0GT63 View 3D Structure Click here
A0A0R0GX50 View 3D Structure Click here
A0A0R0HCN9 View 3D Structure Click here
A0A0R0I183 View 3D Structure Click here
A0A0R0I3K9 View 3D Structure Click here
A0A0R0IB80 View 3D Structure Click here
A0A0R0ISW8 View 3D Structure Click here
A0A0R0J7P2 View 3D Structure Click here
A0A0R0K4K3 View 3D Structure Click here
A0A0R0KJN8 View 3D Structure Click here
A0A0R0LB34 View 3D Structure Click here
A0A0R0LBK7 View 3D Structure Click here
A0A0R0LCE1 View 3D Structure Click here
A0A0R0LER5 View 3D Structure Click here
A0A1D6EH29 View 3D Structure Click here
A0A1D6ELR7 View 3D Structure Click here
A0A1D6ELU3 View 3D Structure Click here
A0A1D6FAS4 View 3D Structure Click here
A0A1D6FHM9 View 3D Structure Click here
A0A1D6FKV7 View 3D Structure Click here
A0A1D6FU87 View 3D Structure Click here