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34  structures 1609  species 1  interaction 2722  sequences 15  architectures

Family: MAPEG (PF01124)

Summary: MAPEG family

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This is the Wikipedia entry entitled "MAPEG family". More...

MAPEG family Edit Wikipedia article

MAPEG family
Protein LTC4S PDB 2PNO.png
Crystal structure of human leukotriene C4 synthase. [1]
Identifiers
Symbol MAPEG
Pfam PF01124
InterPro IPR001129
PROSITE PS01297
SCOP 2pno
SUPERFAMILY 2pno

In molecular biology the MAPEG (Membrane-Associated Proteins in Eicosanoid and Glutathione metabolism) family of proteins are a group of membrane associated proteins with highly divergent functions.[2] Included are the 5-lipoxygenase-activating protein (gene FLAP), leukotriene C4 synthase (EC 2.5.1.37), which catalyzes the production of leukotriene C4 (LTC4) from leukotriene A4 (LTA4), and microsomal glutathione S-transferase II (EC 2.5.1.18) (GST-II), which also produces LTC4 from LTA4.

Another example is prostaglandin E synthase. This enzyme catalyses the synthesis of PGE2 from PGH2 (produced by cyclooxygenase from arachidonic acid). Because of structural similarities in the active sites of FLAP, LTC4 synthase, and PGE synthase, substrates for each enzyme can compete with one another and modulate synthetic activity.

Subfamilies[edit]

  • 5-lipoxygenase-activating protein IPR001129

Human proteins containing this domain[edit]

References[edit]

  1. ^ Ago, H.; Kanaoka, Y.; Irikura, D.; Lam, B. K.; Shimamura, T.; Austen, K. F.; Miyano, M. (2007). "Crystal structure of a human membrane protein involved in cysteinyl leukotriene biosynthesis". Nature 448 (7153): 609–612. doi:10.1038/nature05936. PMID 17632548.  edit
  2. ^ Jakobsson, P. J.; Morgenstern, R.; Mancini, J.; Ford-Hutchinson, A.; Persson, B. (2008). "Common structural features of mapeg-a widespread superfamily of membrane associated proteins with highly divergent functions in eicosanoid and glutathione metabolism". Protein Science 8 (3): 689–692. doi:10.1110/ps.8.3.689. PMC 2144274. PMID 10091672.  edit

This article incorporates text from the public domain Pfam and InterPro IPR001129

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.

MAPEG family Provide feedback

This family is has been called MAPEG (Membrane Associated Proteins in Eicosanoid and Glutathione metabolism). It includes proteins such as Prostaglandin E synthase. This enzyme catalyses the synthesis of PGE2 from PGH2 (produced by cyclooxygenase from arachidonic acid). Because of structural similarities in the active sites of FLAP, LTC4 synthase and PGE synthase, substrates for each enzyme can compete with one another and modulate synthetic activity.

Literature references

  1. Jakobsson PJ, Morgenstern R, Mancini J, Ford-Hutchinson A, Persson B; , Protein Sci 1999;8:689-692.: Common structural features of MAPEG -- a widespread superfamily of membrane associated proteins with highly divergent functions in eicosanoid and glutathione metabolism. PUBMED:10091672 EPMC:10091672


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR001129

This entry represents a widespread superfamily known as MAPEG (Membrane Associated Proteins in Eicosanoid and Glutathione metabolism) [PUBMED:10091672]. Included are:

  • 5-lipoxygenase activating protein (gene FLAP), which seems to be required for the activation of 5-lipoxygenase.
  • Leukotriene C4 synthase (EC), which catalyses the production of LTC4 from LTA4.
  • Microsomal glutathione S-transferase II (EC) (GST-II), which also produces LTC4 from LTA4.
  • Prostaglandin E synthase, which catalyses the synthesis of PGE2 from PGH2 (produced by cyclooxygenase from arachidonic acid).

Because of structural similarities in the active sites of FLAP, LTC4 synthase and PGE synthase, substrates for each enzyme can compete with one another and modulate synthetic activity.

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...

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
(319)
Full
(2722)
Representative proteomes NCBI
(2147)
Meta
(1247)
RP15
(315)
RP35
(546)
RP55
(790)
RP75
(1052)
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available

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

Format an alignment

  Seed
(319)
Full
(2722)
Representative proteomes NCBI
(2147)
Meta
(1247)
RP15
(315)
RP35
(546)
RP55
(790)
RP75
(1052)
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
(319)
Full
(2722)
Representative proteomes NCBI
(2147)
Meta
(1247)
RP15
(315)
RP35
(546)
RP55
(790)
RP75
(1052)
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: [1]
Previous IDs: FLAP;
Type: Family
Author: Finn RD, Bateman A, Brock T
Number in seed: 319
Number in full: 2722
Average length of the domain: 123.10 aa
Average identity of full alignment: 21 %
Average coverage of the sequence by the domain: 86.01 %

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 20.9 20.9
Trusted cut-off 20.9 21.0
Noise cut-off 20.8 20.6
Model length: 129
Family (HMM) version: 13
Download: download the raw HMM for this family

Species distribution

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Interactions

There is 1 interaction for this family. More...

MAPEG

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 MAPEG domain has been found. There are 34 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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