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11  structures 271  species 1  interaction 1560  sequences 69  architectures

Family: WH2 (PF02205)

Summary: WH2 motif

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WH2 motif Edit Wikipedia article

WH2 motif
PDB 2d1k EBI.jpg
Ternary complex of the WH2 domain of mim with actin-dnase I[1]
Identifiers
Symbol WH2
Pfam PF02205
InterPro IPR003124
SMART WH2
SCOP 1ej5
SUPERFAMILY 1ej5

Function[edit]

The WH2 motif or WH2 domain is an evolutionarily conserved sequence motif contained in proteins.[2] It is found in WASP proteins which control actin polymerisation, therefore, WH2 is important in cellular processes such as cell contractility, cell motility, cell trafficking and cell signalling.[3]

Motif[edit]

The WH2 motif (for Wiskott-Aldrich syndrome homology region 2) has been shown in WAS and Scar1/WASF1 (mammalian homologue) to interact via their WH2 motifs with actin.

The WH2 (WASP-Homology 2, or Wiskott-Aldrich homology 2) domain is an ~18 amino acids actin-binding motif. This domain was first recognized as an essential element for the regulation of the cytoskeleton by the mammalian Wiskott-Aldrich syndrome protein (WASP) family. WH2 proteins occur in eukaryotes from yeast to mammals, in insect viruses, and in some bacteria. The WH2 domain is found as a modular part of larger proteins; it can be associated with the WH1 or EVH1 domain and with the CRIB domain, and the WH2 domain can occur as a tandem repeat. The WH2 domain binds to actin monomers and can facilitate the assembly of actin monomers into actin filaments.[4][5]

Examples[edit]

Human genes encoding proteins containing the WH2 motif include:

References[edit]

  1. ^ PDB 2d1k; Lee SH, Kerff F, Chereau D, Ferron F, Klug A, Dominguez R (February 2007). "Structural basis for the actin-binding function of missing-in-metastasis". Structure 15 (2): 145–55. doi:10.1016/j.str.2006.12.005. PMC 1853380. PMID 17292833. 
  2. ^ Machesky LM, Insall RH (1998). "Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex". Curr. Biol. 8 (25): 1347–56. doi:10.1016/S0960-9822(98)00015-3. PMID 9889097. 
  3. ^ Veltman DM, Insall RH (2010). "WASP family proteins: their evolution and its physiological implications.". Mol Biol Cell 21 (16): 2880–93. doi:10.1091/mbc.E10-04-0372. PMC 2921111. PMID 20573979. 
  4. ^ Machesky LM, Insall RH, Volkman LE (2001). "WASP homology sequences in baculoviruses". Trends Cell Biol. 11 (7): 286–287. doi:10.1016/S0962-8924(01)02009-8. PMID 11434350. 
  5. ^ Lappalainen P, Paunola E, Mattila PK (2002). "WH2 domain: a small, versatile adapter for actin monomers". FEBS Lett. 513 (1): 92–97. doi:10.1016/S0014-5793(01)03242-2. PMID 11911886. 

This article incorporates text from the public domain Pfam and InterPro IPR003124

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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WH2 motif Provide feedback

The WH2 motif (for Wiskott Aldrich syndrome homology region 2) has been shown in WASP P42768 and Scar1 (mammalian homologue) to be the region that interacts with actin.

Literature references

  1. Machesky LM, Insall RH; , Curr Biol 1998;8:1347-1356.: Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex. PUBMED:9889097 EPMC:9889097


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR003124

The WH2 (WASP-Homology 2, or Wiskott-Aldrich homology 2) domain is an ~18 amino acids actin-binding motif. This domain was first recognised as an essential element for the regulation of the cytoskeleton by the mammalian Wiskott-Aldrich syndrome protein (WASP) family. WH2 proteins occur in eukaryotes from yeast to mammals, in insect viruses, and in some bacteria. The WH2 domain is found as a modular part of larger proteins; it can be associated with the WH1 or EVH1 domain and with the CRIB domain, and the WH2 domain can occur as a tandem repeat. The WH2 domain binds actin monomers and can facilitate the assembly of actin monomers into newly forming actin filaments [PUBMED:11434350, PUBMED:11911886].

Gene Ontology

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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

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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.

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(57)
Full
(1560)
Representative proteomes NCBI
(1462)
Meta
(8)
RP15
(213)
RP35
(324)
RP55
(544)
RP75
(837)
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  Seed
(57)
Full
(1560)
Representative proteomes NCBI
(1462)
Meta
(8)
RP15
(213)
RP35
(324)
RP55
(544)
RP75
(837)
Alignment:
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  Seed
(57)
Full
(1560)
Representative proteomes NCBI
(1462)
Meta
(8)
RP15
(213)
RP35
(324)
RP55
(544)
RP75
(837)
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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.

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Curation and family details

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Seed source: Alignment kindly provided by SMART
Previous IDs: none
Type: Family
Author: SMART
Number in seed: 57
Number in full: 1560
Average length of the domain: 26.60 aa
Average identity of full alignment: 38 %
Average coverage of the sequence by the domain: 5.24 %

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 23.1 13.0
Trusted cut-off 23.1 13.0
Noise cut-off 23.0 12.9
Model length: 30
Family (HMM) version: 15
Download: download the raw HMM for this family

Species distribution

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Interactions

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

Actin

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 WH2 domain has been found. There are 11 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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