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. 2000 Sep 1;20(17):6540–6550. doi: 10.1523/JNEUROSCI.20-17-06540.2000

Fig. 3.

Fig. 3.

Structural comparison of netrin-G1 and other UNC-6/netrins. A, Domain structures of members of the UNC-6/netrin family are schematically represented. The percent identity in amino acid sequence between homologous domains is shown. Netrin-G1a is anchored on cell membrane by a GPI linkage, whereas netrin-1 and netrin-3 are secreted. The C domains of classical netrins are highly charged (indicated by ++). The C-terminal sequence of netrin-G1a, named C′, is distinctly different from the C domain of classical netrins.B, Kyte-Doolittle hydrophobicity plot of deduced netrin-G1a and mouse netrin-1 amino acid sequences. Two hydrophobic stretches were observed at both N and C termini in netrin-G1a. The latter stretch is unique to netrin-G1 among members of the UNC-6/netrin family. C, A phylogenetic tree was constructed based on the amino acid sequences of C. elegans UNC-6 (P34710), chick netrin-1 (Q90922), chick netrin-2 (Q90923), mouse netrin-1 (AAC52971), mouse netrin-3 (AAD40063), human netrin-1 (NP004813), human NTN2L (NP006172), zebrafish netrin-1 (AAB70266), zebrafish netrin-1a (AAC60252), Drosophila netrin-A (Q24567),Drosophila netrin-B (Q24568), and netrin-G1a (AB038667) using CLUSTAL X program (ftp://ftp-igbmc.u-strasbg.fr/pub/ClustalX/). Netrin-G1 is evolutionarily distant from other members of the family, implying that the netrin-G1 may serve as a prototype of a novel subfamily.