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2  structures 251  species 0  interactions 629  sequences 13  architectures

Family: VASP_tetra (PF08776)

Summary: VASP tetramerisation domain

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This is the Wikipedia entry entitled "Ena/Vasp homology proteins". More...

Ena/Vasp homology proteins Edit Wikipedia article

Domain organisation of EVH proteins
VASP_tetra
PDB 1usd EBI.jpg
human vasp tetramerisation domain l352m
Identifiers
Symbol VASP_tetra
Pfam PF08776
InterPro IPR014885

'ENA/VASP Homology proteins' or 'EVH' proteins are a family of closely related proteins involved in cell motility in vertebrate and invertebrate animals. EVH proteins are modular proteins that are involved in actin polymerization, as well as interaction with other proteins. Within the cell, Ena/VASP proteins are found at the leading edge of Lamellipodia and at the tips of filopodia.[1] Ena, the founding member of the family was discovered in a drosophila genetic screen for mutations that act as dominant suppressors of the abl non receptor tyrosine kinase. Invertebrate animals have one Ena homologue, whereas mammals have three, in mice named Mena, VASP, and Evl.

Ena/VASP proteins promote the spatially regulated actin polymerization required for efficient chemotaxis in response to attractive and repulsive guidance cues. Mice lacking functional copies of all three family members display pleiotropic phenotypes including exencephaly, edema, failures in neurite formation, and embryonic lethality.

A sub-domain of EVH is the EVH1 domain.

VASP

Vasodilator-stimulated phosphoprotein (VASP) 45-residue-long tetramerization protein domain which regulates actin dynamics in the cytoskeleton. This is vital for processes such as cell adhesion and cell migration.

Function

Vasodilator-stimulated phosphoprotein (VASP) is an actin cytoskeletal regulatory protein. VASP is often found in dynamic actin structures like filopodia and lamellipodia, but its precise function in their formation is controversial. VASP accelerates filament elongation by delivering monomeric actin to the growing barbed (+) end.[2]

Structure

The structure is a right-handed alpha helical coiled-coil structure.[3]

References

  1. ^ Bear and Gertler; Gertler, FB (2009). "Ena/VASP: towards resolving a controversy at the barbed end". J Cell Sci. 122 (Pt 12): 1947–53. doi:10.1242/jcs.038125. PMC 2723151Freely accessible. PMID 19494122. 
  2. ^ Breitsprecher D, Kiesewetter AK, Linkner J, Urbanke C, Resch GP, Small JV, Faix J (2008). "Clustering of VASP actively drives processive, WH2 domain-mediated actin filament elongation". EMBO J. 27 (22): 2943–54. doi:10.1038/emboj.2008.211. PMC 2585163Freely accessible. PMID 18923426. 
  3. ^ Kühnel K, Jarchau T, Wolf E, Schlichting I, Walter U, Wittinghofer A, Strelkov SV (December 2004). "The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat". Proc. Natl. Acad. Sci. U.S.A. 101 (49): 17027–32. doi:10.1073/pnas.0403069101. PMC 535362Freely accessible. PMID 15569942. 

This article incorporates text from the public domain Pfam and InterPro IPR014885


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.

VASP tetramerisation domain Provide feedback

Vasodilator-stimulated phosphoprotein (VASP) is an actin cytoskeletal regulatory protein. This region corresponds to the tetramerisation domain which forms a right handed alpha helical coiled coil structure [1].

Literature references

  1. Kuhnel K, Jarchau T, Wolf E, Schlichting I, Walter U, Wittinghofer A, Strelkov SV; , Proc Natl Acad Sci U S A. 2004;101:17027-17032.: The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat. PUBMED:15569942 EPMC:15569942


This tab holds annotation information from the InterPro database.

InterPro entry IPR014885

Vasodilator-stimulated phosphoprotein (VASP) is an actin cytoskeletal regulatory protein. This region corresponds to the tetramerisation domain which forms a right handed alpha helical coiled coil structure [PUBMED:15569942].

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 (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
(24)
Full
(629)
Representative proteomes UniProt
(1019)
NCBI
(3110)
Meta
(1)
RP15
(105)
RP35
(232)
RP55
(398)
RP75
(484)
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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
(24)
Full
(629)
Representative proteomes UniProt
(1019)
NCBI
(3110)
Meta
(1)
RP15
(105)
RP35
(232)
RP55
(398)
RP75
(484)
Alignment:
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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
(24)
Full
(629)
Representative proteomes UniProt
(1019)
NCBI
(3110)
Meta
(1)
RP15
(105)
RP35
(232)
RP55
(398)
RP75
(484)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   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.

HMM logo

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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 View help on the curation process

Seed source: pdb_1usd
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Mistry J
Number in seed: 24
Number in full: 629
Average length of the domain: 36.00 aa
Average identity of full alignment: 56 %
Average coverage of the sequence by the domain: 7.11 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.6 21.6
Trusted cut-off 22.1 21.8
Noise cut-off 21.5 21.3
Model length: 37
Family (HMM) version: 11
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 VASP_tetra 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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