Abstract
We have previously reported the cloning of two partial cDNAs corresponding to two quail (Coturnix coturnix japonica) receptor tyrosine kinases (RTKs), named Quek 1 and Quek 2, and their expression in endothelial cells of the early avian embryo. We here report the cloning of the full-size cDNAs for both molecules. Sequence comparison shows that Quek 1 and 2 share an overall amino acid (aa) identity of 49%. They both comprise seven extracellular immunoglobulin-like (Ig-like) domains, a single transmembrane domain, and an intracellular kinase domain split into two by a 70 aa insertion. These structural characteristics are shared by the members of the recently discovered VEGF receptor (VEGFR) family. We have compared the sequences of Quek 1 and 2 to the other VEGFRs. At the aa level, Quek 1 is most closely related to KDR/flk-1 (VEGFR 2) (aa identity of 69% and 71%, respectively). Quek 2 shows a similar degree of aa identity to flt-4 (VEGFR 3). Quek 1 and 2 display a lower homology to flt-1 (VEGFR 1) (about 45% aa identity). These data suggest that Quek 1 and 2 are the avian homologues of VEGFRs 2 and 3, respectively.
| Original language | English |
|---|---|
| Pages (from-to) | 3-8 |
| Number of pages | 6 |
| Journal | Gene |
| Volume | 174 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 26 Sept 1996 |
| Externally published | Yes |
Keywords
- Amino acid sequence
- Coturnix cotutnix japonica
- Embryonic development
- Endothelial cell
- Receptor tyrosine kinase
- Recombinant DNA
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