Summary: Laminin EGF domain
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This is the Wikipedia entry entitled "Laminin". More...
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Laminin EGF domain Provide feedback
This family is like PF00008 but has 8 conserved cysteines instead of six.
Literature references
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Engel J; , Biochemistry 1992;31:10643-10651.: Laminins and other strange proteins. PUBMED:1420180 EPMC:1420180
Internal database links
SCOOP: | EGF_2 Laminin_B |
Similarity to PfamA using HHSearch: | EGF_2 |
External database links
HOMSTRAD: | EGF_Lam |
PRINTS: | PR00011 |
PROSITE: | PDOC00021 |
PROSITE profile: | PS50027 |
SCOP: | 1tle |
This tab holds annotation information from the InterPro database.
InterPro entry IPR002049
Laminins [PUBMED:2404817] are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation. They are composed of distinct but related alpha, beta and gamma chains. The three chains form a cross-shaped molecule that consist of a long arm and three short globular arms. The long arm consist of a coiled coil structure contributed by all three chains and cross-linked by interchain disulphide bonds. Beside different types of globular domains each subunit contains, in its first half, consecutive repeats of about 60 amino acids in length that include eight conserved cysteines [PUBMED:2666164]. The tertiary structure [PUBMED:8648630, PUBMED:8648631] of this domain is remotely similar in its N-terminal to that of the EGF-like module (see PROSITEDOC). It is known as a 'LE' or 'laminin-type EGF-like' domain. The number of copies of the LE domain in the different forms of laminins is highly variable; from 3 up to 22 copies have been found. A schematic representation of the topology of the four disulphide bonds in the LE domain is shown below.
+-------------------+ +-|-----------+ | +--------+ +-----------------+ | | | | | | | | xxCxCxxxxxxxxxxxCxxxxxxxCxxCxxxxxGxxCxxCxxgaagxxxxxxxxxxxCxx sssssssssssssssssssssssssssssssssss 'C': conserved cysteine involved in a disulphide bond 'a': conserved aromatic residue 'G': conserved glycine (lower case = less conserved) 's': region similar to the EGF-like domainIn mouse laminin gamma-1 chain, the seventh LE domain has been shown to be the only one that binds with a high affinity to nidogen [PUBMED:7781764]. The binding-sites are located on the surface within the loops C1-C3 and C5-C6 [PUBMED:8648630, PUBMED:8648631]. Long consecutive arrays of LE domains in laminins form rod-like elements of limited flexibility [PUBMED:2404817], which determine the spacing in the formation of laminin networks of basement membranes [PUBMED:8349613].
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 EGF (CL0001), which has the following description:
Members of this clan all belong to the EGF superfamily. This particular superfamily is characterised as having least 6 cysteine residues. These cysteines form disulphide bonds, in the order 1-3, 2-4, 5-6, which are essential for the stability of the EGF fold. These disulphide bonds are stacked in a ladder-like arrangement. The Laminin EGF family is distinguished by having an an additional disulphide bond. The function of the domains within this family remains unclear, but they are thought to largely perform a structural role. More often than not, these domains are arranged in tandem repeats in extracellular proteins.
The clan contains the following 21 members:
cEGF CFC DSL EGF EGF_2 EGF_3 EGF_alliinase EGF_CA EGF_MSP1_1 EGF_Tenascin Fibrillin_U_N FOLN FXa_inhibition Gla hEGF I-EGF_1 Laminin_EGF Plasmod_Pvs28 Sushi Sushi_2 Tme5_EGF_likeAlignments
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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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 (72) |
Full (64649) |
Representative proteomes | UniProt (109947) |
NCBI (193148) |
Meta (34) |
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RP15 (10140) |
RP35 (21507) |
RP55 (44883) |
RP75 (67395) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
not generated,
— not available.
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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 (72) |
Full (64649) |
Representative proteomes | UniProt (109947) |
NCBI (193148) |
Meta (34) |
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---|---|---|---|---|---|---|---|---|---|
RP15 (10140) |
RP35 (21507) |
RP55 (44883) |
RP75 (67395) |
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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.
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
Seed source: | Swissprot_feature_table |
Previous IDs: | none |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Sonnhammer ELL |
Number in seed: | 72 |
Number in full: | 64649 |
Average length of the domain: | 49.50 aa |
Average identity of full alignment: | 30 % |
Average coverage of the sequence by the domain: | 18.64 % |
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: | 49 | ||||||||||||
Family (HMM) version: | 25 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Interactions
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 Laminin_EGF domain has been found. There are 50 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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