Involved in the fucosylation of N-glycans (PubMed:15364955, PubMed:17369288, PubMed:23754284, PubMed:26538210, PubMed:26002521). Preferentially catalyzes the addition of fucose in alpha 1-3 linkage to the distal GlcNAc residue in N-glycans (PubMed:23754284). Catalyzes the transfer of fucose to Gal-beta-1-4-GlcNAc-alpha-pNP (LN-pNP) and Gal-beta-1-4-GlcNAc-beta-1-3-Gal-beta-1-4-Glc (LNnT) (PubMed:17369288). Unlike alpha-(1,3)-fucosyltransferase fut-1, does not transfer fucose to Man-alpha-1-3-(Man-alpha-1-6)-Man-beta-1-4-GlcNAc-beta-1-4-GlcNAc-beta-1-Asn (M3), Man-alpha-1-3-(Man-alpha-1-6)-Man-beta-1-4-GlcNAc-beta-1-4-(Fuc-alpha-1-6)-GlcNAc-beta-1-Asn (M3F6) and GlcNAc-beta-1-2-Man-alpha-1-3-(GlcNAc-beta-1-2-Man-alpha-1-6)-Man-beta-1-4-GlcNAc-beta-1-4(Fuc-alpha-1-6)-GlcNAc-beta-1-Asn (GnM3F6) (PubMed:17369288). Unlike other alpha-(1,3)-fucosyltransferases, appears not to require a divalent metal cation as cofactor. Inhibited by divalent metal cations. Optimum temperature is 23 degrees Celsius. Very low activity at 37 degrees Celsius. Protein modification; protein glycosylation. Expressed in larvae and adult. No visible phenotype (PubMed:17369288). Loss of several tetra-fucosylated N-glycans (PubMed:15364955). Loss of tetra- and tri-fucosylated N-glycans in a fut-8 or fut-1 mutant background (PubMed:26538210). fut-1, fut-6 and fut-8 triple mutants lack all N-glycan core fucose with only one fucose present in the bisecting galactose, thus resulting in the loss of tetra-, tri- and bi-fucosylated N-glycans (PubMed:26002521). Belongs to the glycosyltransferase 10 family.