Summary: Fascin domain
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Fascin domain Provide feedback
This family consists of several eukaryotic fascin or singed proteins. The fascins are a structurally unique and evolutionarily conserved group of actin cross-linking proteins. Fascins function in the organisation of two major forms of actin-based structures: dynamic, cortical cell protrusions and cytoplasmic microfilament bundles. The cortical structures, which include filopodia, spikes, lamellipodial ribs, oocyte microvilli and the dendrites of dendritic cells, have roles in cell-matrix adhesion, cell interactions and cell migration, whereas the cytoplasmic actin bundles appear to participate in cell architecture . Dictyostelium hisactophilin, another actin-binding protein, is a submembranous pH sensor that signals slight changes of the H+ concentration to actin by inducing actin polymerisation and binding to microfilaments only at pH values below seven . Members of this family are histidine rich, typically contain the repeated motif of HHXH .
Bryan J, Edwards R, Matsudaira P, Otto J, Wulfkuhle J; , Proc Natl Acad Sci U S A 1993;90:9115-9119.: Fascin, an echinoid actin-bundling protein, is a homolog of the Drosophila singed gene product. PUBMED:8415664 EPMC:8415664
Habazettl J, Gondol D, Wiltscheck R, Otlewski J, Schleicher M, Holak TA; , Nature 1992;359:855-858.: Structure of hisactophilin is similar to interleukin-1 beta and fibroblast growth factor. PUBMED:1436061 EPMC:1436061
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR022768
This family consists of several eukaryotic fascin or singed proteins. The fascins are a structurally unique and evolutionarily conserved group of actin cross-linking proteins. Fascins function in the organisation of two major forms of actin-based structures: dynamic, cortical cell protrusions and cytoplasmic microfilament bundles. The cortical structures, which include filopodia, spikes, lamellipodial ribs, oocyte microvilli and the dendrites of dendritic cells, have roles in cell-matrix adhesion, cell interactions and cell migration, whereas the cytoplasmic actin bundles appear to participate in cell architecture [PUBMED:11948621]. Dictyostelium hisactophilin, another actin-binding protein, is a submembranous pH sensor that signals slight changes of the H+ concentration to actin by inducing actin polymerisation and binding to microfilaments only at pH values below seven [PUBMED:11948621]. Members of this family are histidine rich, typically contain the repeated motif of HHXH [PUBMED:1436061].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||actin filament binding (GO:0051015)|
|protein binding, bridging (GO:0030674)|
- the number of sequences which exhibit this architecture
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This example describes an architecture with one
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This family corresponds to a large set of related beta-trefoil proteins . The beta-trefoil is formed by six two-stranded hairpins . Three of these form a barrel structure and the other three are in a triangular array that caps the barrel. The arrangement of the secondary structures gives the molecules a pseudo 3-fold axis.
The clan contains the following 15 members:AbfB Agglutinin Botulinum_HA-17 CDtoxinA DUF569 Fascin FGF FRG1 IL1 Ins145_P3_rec Kunitz_legume MIR Ricin_B_lectin RicinB_lectin_2 Toxin_R_bind_C
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||Pfam-B_11660 (release 9.0)|
|Author:||Moxon SJ, Bateman A, Finn RD|
|Number in seed:||23|
|Number in full:||817|
|Average length of the domain:||107.60 aa|
|Average identity of full alignment:||21 %|
|Average coverage of the sequence by the domain:||63.95 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||8|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 Fascin domain has been found. There are 30 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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