The F-box/SPRY domain is a conserved structural motif found in proteins involved in ubiquitination pathways. For example:
FBXO45 (F-box protein 45) in humans binds SPRY motifs in N-cadherin (NCad) to regulate neuronal migration .
In prostate cancer, FBXO45 overexpression correlates with poor prognosis and enhanced metastatic potential .
Key functional features of F-box/SPRY proteins include:
| Feature | Role | Example |
|---|---|---|
| F-box domain | Binds Skp1 for ubiquitination | FBXO45 interaction |
| SPRY domain | Substrate recognition | NCad binding |
| Ubiquitin ligase | Targets proteins for degradation | MycBP2 interaction |
While recombinant proteins from Culex quinquefasciatus have been studied, the focus has been on:
Storage proteins (e.g., LSP1 and LSP2), which accumulate during larval stages and degrade during metamorphosis .
CWRC family proteins (Cysteine and Tryptophan-Rich), such as CqDVP-2 and CqDVP-4, which adopt β-trefoil folds for carbohydrate binding .
No studies in the search results describe an F-box/SPRY domain-containing protein designated as "Fsn" in Culex quinquefasciatus.
The term "Fsn" does not appear in any indexed publications related to Culex or mosquito proteomics.
If "Fsn" refers to a hypothetical or uncharacterized protein, its properties might be inferred from homologous systems:
Functional analogy: Could regulate apoptosis or neural development via SPRY-mediated interactions, similar to FBXO45 .
Structural analogy: May require insect cell systems (e.g., Trichoplusia ni) for recombinant expression, as seen with PmFREP in shrimp .
To validate the existence and role of this protein:
KEGG: cqu:CpipJ_CPIJ016123
STRING: 7176.CPIJ016123-PA