Primary Information |
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| BoMiProt ID | Bomi93 |
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| Protein Name | Wiskott-Aldrich syndrome protein family member 2 |
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| Organism | Bos taurus |
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| Uniprot ID | A2VDK6 |
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| Milk Fraction | Exosome |
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| Ref Sequence ID | NP_001074980.1 |
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| Aminoacid Length | 493 |
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| Molecular Weight | 54031 |
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| FASTA Sequence |
Download |
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| Gene Name | WASF2 |
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| Gene ID | 504482 |
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| Protein Existence Status | Reviewed: Experimental evidence at transcript level |
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Secondary Information |
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| Presence in other biological fluids/tissue/cells | N-WASP because it is ubiquitous but enriched in neural tissues |
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| Protein Function | function as nucleation-promoting factors for the ubiquitously
expressed Arp2/3 complex, which drives the generation of
branched actin filaments which regulates diverse
cellular processes, including the formation of lamellipodia and
filopodia, endocytosis and/or phagocytosis at the plasma
membrane, and the generation of cargo-laden vesicles from
organelles including the Golgi, endoplasmic reticulum (ER) and the
endo-lysosomal network; promote actin dynamics at the
centrosome, influencing nuclear shape and membrane remodeling
events leading to the generation of autophagosomes; key organizer involved in the remodeling of actin cytoskeleton to regulate cell movement, cell signaling, and cell division |
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| Biochemical Properties | WASp as isolated from bovine thymus, is inactive in the presence or absence of
0.5
m
M GTP-Cdc42; allowed by Phosphatidylinositol 4,5 bisphosphate
to activate actin
nucleation by Arp2/3 complex; N WASP interacts with the SH3 domain of Ash⧸Grb2; WASP proteins have several functional domains including an EVH1⧸WH1 domain at the N-terminus, a basic region, a GDB⧸CRIB motif, a proline-rich region in the center, and a VCA (verprolin-like, cofilin-like, and acidic) domain at the C-terminus- proline-rich region is an SH3 domain-binding region; WASP and are direct, specific
effectors of Cdc42 and are thought to mediate most
of the cytoskeletal effects of active Cdc42; bind directly to GTP-bound
Cdc42, through their GBD; Under resting conditions,
WASP/N-WASP activity is autoinhibited via intramolecular
interaction between the GBD and the VCA modules,
preventing binding and/or activation of the Arp2/3
complex |
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| PTMs | WASP is constitutively phosphorylated
by caseine kinase 2 at the junction of the C and A
domains of the VCA module |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
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| Predicted Disorder Regions | (173-204), (211-230), (236-435) |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Significance of PTMs | serine phosphorylation strongly increases the affinity of the VCA
module for the Arp2/3 complex in vitro; it is also necessary
for the Cdc42-dependent induction of actin polymerization
by full-length WASP; tyrosine-phosphorylation in N-WASP |
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| Additional Comments | Five WASP family members exist in
mammals: WASP, N-WASP, and three WASP family verprolin
homologous (WAVE) proteins; tyrosine-phosphorylated N-WASP is degraded
by the proteasome pathway |
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| Bibliography | 1. Panchal, S. C., Kaiser, D. A., Torres, E., Pollard, T. D., & Rosen, M. K. (2003). A conserved amphipathic helix in WASP/Scar proteins is essential for activation of Arp2/3 complex. Nature Structural Biology, 10(8), 591–598. https://doi.org/10.1038/nsb952.
2. Cory, G. O. C., Cramer, R., Blanchoin, L., & Ridley, A. J. (2003). Phosphorylation of the WASP-VCA domain increases its affinity for the Arp2/3 complex and enhances actin polymerization by WASP. Molecular Cell, 11(5), 1229–1239. https://doi.org/10.1016/s1097-2765(03)00172-2.
3. Higgs, H. N., & Pollard, T. D. (2000). Activation by Cdc42 and PIP 2 of Wiskott-Aldrich syndrome protein ( WASp ) stimulates actin nucleation by Arp2 / 3 complex WASp alone is inactive in the presence or absence of. The Journal of Cell Biology, 150(6), 1311–1320. https://doi.org/10.1083/jcb.150.6.1311. |
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