Summary: Fringe-like
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Fringe-like Provide feedback
The drosophila protein fringe (FNG) is a glucosaminyltransferase that controls the response of the Notch receptor to specific ligands [2]. FNG is localised to the Golgi apparatus [1] (not secreted as previously thought). Modification of Notch occurs through glycosylation by FNG. The xenopus homologue, lunatic fringe, has been implicated in a variety of functions.
Literature references
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Munro S, Freeman M; , Curr Biol 2000;10:813-820.: The Notch signalling regulator Fringe acts in the Golgi apparatus and requires the glycosyltransferase signature motif DXD. PUBMED:10899003 EPMC:10899003
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Munro S, Freeman M; , Curr Biol 2000;10:813-820.: The Notch signalling regulator Fringe acts in the Golgi apparatus and requires the glycosyltransferase signature motif DXD. PUBMED:10899003 EPMC:10899003
Internal database links
SCOOP: | CHGN DUF604 Galactosyl_T |
Similarity to PfamA using HHSearch: | Galactosyl_T DUF604 |
This tab holds annotation information from the InterPro database.
InterPro entry IPR003378
The Notch receptor is a large, cell surface transmembrane protein involved in a wide variety of developmental processes in higher organisms [PUBMED:10221902]. It becomes activated when its extracellular region binds to ligands located on adjacent cells. Much of this extracellular region is composed of EGF-like repeats, many of which can be O-fucosylated. A number of these O-fucosylated repeats can in turn be further modified by the action of a beta-1,3-N-acetylglucosaminyltransferase enzyme known as Fringe [PUBMED:12417415]. Fringe potentiates the activation of Notch by Delta ligands, while inhibiting activation by Serrate/Jagged ligands. This regulation of Notch signalling by Fringe is important in many processes [PUBMED:14570055].
Four distinct Fringe proteins have so far been studied in detail; Drosophila Fringe (Dfng) and its three mammalian homologues Lunatic Fringe (Lfng), Radical Fringe (Rfng) and Manic Fringe (Mfng). Dfng, Lfng and Rfng have all been shown to play important roles in developmental processes within their host, though the phenotype of mutants can vary between species e.g. Rfng mutants are retarded in wing development in chickens, but have no obvious phenotype in mice [PUBMED:7954826, PUBMED:12001066, PUBMED:9121551]. Mfng mutants have not, so far, been charcterised. Biochemical studies indicate that the Fringe proteins are fucose-specific transferases requiring manganese for activity and utilising UDP-N-acetylglucosamine as a donor substrate [PUBMED:16221665]. The three mammalian proteins show distinct variations in their catalytic efficiencies with different substrates.
Dfng is a glucosaminyltransferase that controls the response of the Notch receptor to specific ligands which is localised to the Golgi apparatus [PUBMED:10899003] (not secreted as previously thought). Modification of Notch occurs through glycosylation by Dfng.
This entry consists of Fringe proteins and related glycosyltransferase enzymes including:
- Beta-1,3-glucosyltransferase, which glucosylates O-linked fucosylglycan on thrombospondin type 1 repeat domains [PUBMED:16899492].
- Core 1 beta1,3-galactosyltransferase 1, generates the core T antigen, which is a precursor for many extended O-glycans in glycoproteins and plays a central role in many processes, such as angiogenesis, thrombopoiesis and kidney homeostasis development [PUBMED:11673471].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Cellular component | membrane (GO:0016020) |
Molecular function | transferase activity, transferring glycosyl groups (GO:0016757) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan GT-A (CL0110), which has the following description:
This is the GT-A clan that contains diverse glycosyltransferases that possess a Rossmann like fold [1].
The clan contains the following 52 members:
Anp1 Branch Caps_synth Cellulose_synt CgtA CHGN Chitin_synth_1 Chitin_synth_2 CofC CTP_transf_3 DUF2064 DUF273 DUF604 Fringe Galactosyl_T GlcNAc Gly_transf_sug Glyco_tranf_2_2 Glyco_tranf_2_3 Glyco_tranf_2_4 Glyco_tranf_2_5 Glyco_trans_2_3 Glyco_transf_15 Glyco_transf_21 Glyco_transf_24 Glyco_transf_25 Glyco_transf_34 Glyco_transf_43 Glyco_transf_49 Glyco_transf_6 Glyco_transf_64 Glyco_transf_7C Glyco_transf_7N Glyco_transf_8 Glyco_transf_88 Glyco_transf_92 Glycos_transf_2 GNT-I IspD Mannosyl_trans3 MGAT2 NTP_transf_3 NTP_transferase Nucleotid_trans Osmo_MPGsynth Pox_P35 RGP Rhamno_transf STELLO TcdA_TcdB UDP-g_GGTase UDPGPAlignments
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, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...
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Seed (27) |
Full (4066) |
Representative proteomes | UniProt (7010) |
NCBI (16284) |
Meta (8) |
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RP15 (772) |
RP35 (1521) |
RP55 (2722) |
RP75 (4120) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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Seed (27) |
Full (4066) |
Representative proteomes | UniProt (7010) |
NCBI (16284) |
Meta (8) |
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RP15 (772) |
RP35 (1521) |
RP55 (2722) |
RP75 (4120) |
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Raw Stockholm | |||||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
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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
Seed source: | Pfam-B_1900 (release 5.4) |
Previous IDs: | none |
Type: | Family |
Sequence Ontology: | SO:0100021 |
Author: |
Mian N |
Number in seed: | 27 |
Number in full: | 4066 |
Average length of the domain: | 180.30 aa |
Average identity of full alignment: | 20 % |
Average coverage of the sequence by the domain: | 48.13 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 252 | ||||||||||||
Family (HMM) version: | 17 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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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 Fringe domain has been found. There are 2 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.
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