WASF3
| third member of the Wiskott-Aldrich syndrome proteins | ||
|---|---|---|
| other names |
Protein WAVE-3, Verprolin homology domain-containing protein 3 |
|
| Properties of human protein | ||
| Mass / length primary structure | 502 amino acids , 55,293 Da | |
| Identifier | ||
| Gene name | WASF3 | |
| External IDs | ||
| Orthologue | ||
| human | House mouse | |
| Entrez | 10810 | 245880 |
| Ensemble | ENSG00000132970 | ENSMUSG00000029636 |
| UniProt | Q9UPY6 | Q8VHI6 |
| Refseq (mRNA) | NM_001291965 | NM_145155 |
| Refseq (protein) | NP_001278894 | NP_660137 |
| Gene locus | Chr 13: 26.56 - 26.69 Mb | Chr 5: 146.38 - 146.47 Mb |
| PubMed search | 10810 |
245880
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The third member of the Wiskott-Aldrich syndrome proteins , or third member of the WASP proteins for short , also called WAVE3 , is a regulatory protein that is encoded in humans by 13 exons in the WASF3 gene on human chromosome 13 . The exact locus is: 13q12.13.
Structure and function
The protein has a WHD (WAVE homology) domain at the N terminus , which it assigns to the WAVE proteins within the family and which can be activated via WASF3. A basic region, a proline-rich sequence and the VCA ( Verprolin - Cofilin - Acid = "acid") domain typical of the protein family follow in the direction of the C terminus . The protein can bind to the Arp 2/3 complex via this domain, activate it and thereby increase the formation of actin filaments . So has WASF3 regulatory influence on the actin cytoskeleton via the Arp 2/3 complex controlled actin nucleation . WAVE3 regulates the cell shape, mobility and various functions of the cell.
activation
The model for activating WASF3 is similar to that of WASF1 and WASF2 , as the WHD domain is crucial. The binding of Sra-1 (or its isoform PIR121), Nap-1, Abi-1 or 2, as well as HSPC300 to the WHD domain is constitutive here. Sra-1 can specifically recognize and bind the activated form of the GTPase Rac , which, with the inclusion of the proteins just mentioned, results in the activation of WAVE3. WAVE3 connects other regulatory proteins with the Arp 2/3 complex. The binding of SH3 -containing motifs to the proline-rich region of WASF3 itself or the binding of SH3 domains from Abi proteins to polyproline motifs of other regulatory proteins could also play a role .