2.4.1.B72: C-mannosyltransferase
This is an abbreviated version!
For detailed information about C-mannosyltransferase, go to the full flat file.
Word Map on EC 2.4.1.B72
-
2.4.1.B72
-
c-mannosylation
-
elegans
-
thrombospondin
-
neuroblast
-
acrosome
-
round-headed
-
netrin
- 2.4.1.B72
-
c-mannosylation
- elegans
- thrombospondin
-
neuroblast
-
acrosome
-
round-headed
- netrin
Reaction
transfers a D-mannosyl residue from dolichyl D-mannosyl phosphate to the tryptophan residue of a protein acceptor forming a C-C bond =
Synonyms
C-mannosyltransferase, DPY-19, Dpy-19-like C-mannosyltransferase, Dpy-19-like protein 3, dpy19, DPY19L1, DPY19L3, DPY19L4, dumpy-19, Dumpy-19 protein homologue, Pf DPY-19, PF3D7_0806200, protein dpy-19 homolog 3, protein dumpy-19
ECTree
Advanced search results
General Information
General Information on EC 2.4.1.B72 - C-mannosyltransferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
evolution
malfunction
physiological function
additional information
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
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
evolution
Plasmodium falciparum DPY19 exhibits a different acceptor specificity than the mammalian enzymes
identical Q neuroblast migration phenotypes of dpy-19 and mig-21 mutants
malfunction
knockdown of DPY19L3 inhibits the secretion of Rspo1. Lec15.2 cells lack dolichol-phosphate-mannose synthesis activity
malfunction
a DPY-19 mutant shows a dumpy phenotype and a defect in Q neuroblast migration
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
malfunction
Pf DPY19 gene disruption is not associated with a growth phenotype, not even under endoplasmic reticulum-stressing conditions that could impair protein folding
Caenorhabditis elegans surface receptors MIG-21 and UNC-5 are acceptor substrates of DPY-19, and C-mannosylation is essential for the secretion of soluble MIG-21
physiological function
DPY19L3-mediated C-mannosylation of Rspo1 at W156 is required for its secretion. R-spondin1 (Rspo1) is a secreted protein that enhances Wnt signaling, which has crucial functions in embryonic development and several cancers. C-mannosylation is a posttranslational modification of the first tryptophan residue in the consensus sequence W-X-X-W/C (in which X represents any amino acid) by an endoplasmic reticulum-localized enzyme. C-mannosylation is important for proteinprotein interactions. Enhancement of canonical Wnt signaling by Rspo1 is regulated by C-mannosylation
physiological function
-
the enzyme catalyzes post-translational modification of thrombospondin type-1 repeats in ADAMTS-like and punctin-1 by C-mannosylation of tryptophan
physiological function
apicomplexan C-mannosyltransferases modify thrombospondin type I-containing adhesins of the TRAP family
physiological function
apicomplexan C-mannosyltransferases modify thrombospondin type I-containing adhesins of the TRAP family. Plasmodium falciparum Dpy19 is a C-mannosyltransferase
physiological function
apicomplexan C-mannosyltransferases modify thrombospondin type I-containing adhesins of the TRAP family. Toxoplasma gondii Dpy19 is a C-mannosyltransferase
physiological function
enzyme DPY19L3 is a C-mannosyltransferase of R-spondin1 in human cells. DPY19L3 is predicted to be a multipass transmembrane protein that localizes to the endoplasmic reticulum (ER)
physiological function
mannosylation by DPY19L1 but not DPY19L3 is required for transport of UNC5A from the endoplasmic reticulum to the cell surface. The importance of C-mannosylation for protein secretion might reflect a function in protein folding
physiological function
Plasmodium falciparum C-mannosyltransferase (Pf DPY-19) is demonstrated to modify thrombospondin type 1 repeat (TSR) domains in vitro, exhibiting a different acceptor specificity than their mammalian counterparts. The Plasmodium falciparum C-mannosyltransferase is dispensable for parasite asexual blood stage development
physiological function
the importance of C-mannosylation for protein secretion might reflect a function in protein folding
physiological function
the importance of C-mannosylation for protein secretion might reflect a function in protein folding
physiological function
-
apicomplexan C-mannosyltransferases modify thrombospondin type I-containing adhesins of the TRAP family. Toxoplasma gondii Dpy19 is a C-mannosyltransferase
-
physiological function
-
apicomplexan C-mannosyltransferases modify thrombospondin type I-containing adhesins of the TRAP family. Toxoplasma gondii Dpy19 is a C-mannosyltransferase
-
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
additional information
-
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
additional information
the C-terminal luminal region of DPY19L3 is important for the C-mannosyltransferase activity, while N-glycosylations are not
additional information
-
the C-terminal luminal region of DPY19L3 is important for the C-mannosyltransferase activity, while N-glycosylations are not