EC Number   |
Natural Substrates |
|---|
   2.4.1.B72 | dolichyl D-mannosyl phosphate + MIG-21 protein |
C-mannosylation at a tryptophan residue |
| 2.4.1.B72 | dolichyl D-mannosyl phosphate + UNC-5 protein |
C-mannosylation at a tryptophan residue |
| 2.4.1.B72 | more |
cell surface receptors MIG-21 and UNC-5 are acceptor substrates of enzyme DPY-19 |
| 2.4.1.B72 | more |
DPY19L3 is the C-mannosyltransferase of Rspo1 at residue W156 |
| 2.4.1.B72 | more |
protein C-mannosylation is the attachment of alpha-mannopyranose to tryptophan via a C-C linkage. This post-translational modification typically occurs within the sequence motif WXXW, which is frequently present in thrombospondin type-1 repeats (TSRs). TSRs are especially numerous in and a defining feature of the ADAMTS superfamily. Predicted C-mannosylation sites in the ADAMTS superfamily, overview |
| 2.4.1.B72 | more |
C-mannosylation is initially described as a modification of the first tryptophan in the WxxW consensus sequence, but is also observed on tryptophans that are not part of this motif. In addition to WxxW, WxxC is also considered to be a consensus sequence for C-mannosylation |
| 2.4.1.B72 | more |
mammalian C-mannosyltransferases DPY19L1 and DPY19L3 do not have a dual WxxW/C recognition motif, but are active C-mannosyltransferases with distinct substrate specificities |
| 2.4.1.B72 | more |
the enzyme can transfer mannose to adhesive thrombospondin type 1 repeats (TSRs) and type I cytokine receptors. Enzyme Dpy19 of Caenorhabditis elegans can transfer mannose to a short WXXW peptide |
| 2.4.1.B72 | more |
the micronemal adhesin thrombospondin-related anonymous protein (TRAP) is C-hexosylated in Plasmodium falciparum sporozoites. When expressed in a mammalian cell line deficient in C-mannosylation, the Plasmodium falciparum Dpy19 homologue is able to modify TSR domains of the micronemal adhesins TRAP/MIC2 family involved in parasite motility and invasion. In vitro, the apicomplexan enzyme can transfer mannose to a WXXWXXC peptide but, in contrast to Caenorhabditis elegans or mammalian C-mannosyltransferases, is inactive on a short WXXW peptide |
| 2.4.1.B72 | more |
the micronemal protein MIC2 secreted by Toxoplasma gondii tachyzoites is C-hexosylated. When expressed in a mammalian cell line deficient in C-mannosylation, the Toxoplasma gondii Dpy19 homologue is able to modify TSR domains of the micronemal adhesins TRAP/MIC2 family involved in parasite motility and invasion. In vitro, the apicomplexan enzyme can transfer mannose to a WXXWXXC peptide but, in contrast to Caenorhabditis elegans or mammalian C-mannosyltransferases, is inactive on a short WXXW peptide. MIC2 secreted by Toxoplasma tachyzoites is C-mannosylated |
