EC Number |
General Information |
Reference |
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2.4.1.B72 | evolution |
DPY-19 exhibits topological and sequential homology to the N-glycan oligosaccharyltransferase, highlighting an evolutionary link between N- and C-glycosylation. The enzyme is related to the OST family involved in N-glycosylation |
736804 |
2.4.1.B72 | evolution |
isozyme DPY19L1 activity is conserved in mammals and Caenorhabditis elegans, whereas DPY19L3 has acquired another activity, mannosylation of W3 of the WxxWxxWxxC motif in TSRs. DPY19L1 and DPY19L3 act on the first two and the third tryptophan, respectively |
760067 |
2.4.1.B72 | evolution |
Plasmodium falciparum DPY19 exhibits a different acceptor specificity than the mammalian enzymes |
759899 |
2.4.1.B72 | malfunction |
a DPY-19 mutant shows a dumpy phenotype and a defect in Q neuroblast migration |
759311 |
2.4.1.B72 | malfunction |
identical Q neuroblast migration phenotypes of dpy-19 and mig-21 mutants |
736804 |
2.4.1.B72 | malfunction |
inactivation of DPY19L1 but not DPY19L3 strongly reduces the secretion of UNC5A TSRs and leads to the accumulation of the membrane bound protein in the endoplasmmic reticulum |
760067 |
2.4.1.B72 | malfunction |
knockdown of DPY19L3 inhibits the secretion of Rspo1. Lec15.2 cells lack dolichol-phosphate-mannose synthesis activity |
736780 |
2.4.1.B72 | malfunction |
no activity in CHO cell mutant cells Lec35.1 |
736405 |
2.4.1.B72 | malfunction |
Pf DPY19 gene disruption is not associated with a growth phenotype, not even under endoplasmic reticulum-stressing conditions that could impair protein folding |
759899 |
2.4.1.B72 | more |
among the different types of protein glycosylation, C-mannosylation of tryptophan residues stands out because of the unique linkage formed between sugar and protein. Instead of the typical O- or N-glycosidic linkage, a C-C bond is used for attachment of a single mannose. C-mannose is characteristically found in thrombospondin type 1 repeats and in the WSXWS motif of type I cytokine receptors |
736804 |