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Phosphatidylinositol glycan anchor biosynthesis, class V

This gene encodes a mannosyltransferase enzyme involved in the biosynthesis of glycosylphosphatidylinositol (GPI). GPI is a complex glycolipid that functions as a membrane anchor for many proteins and plays a role in multiple cellular processes including protein sorting and signal transduction. The encoded protein is localized to the endoplasmic reticulum and transfers the second mannose to the GPI backbone. Mutations in this gene are associated with hyperphosphatasia mental retardation syndrome. Alternatively spliced transcript variants have been observed for this gene. [provided by RefSeq, Feb 2011] (from NCBI)
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Top mentioned proteins: MT1, PIG-M, ACID, glycosyltransferase, PIG-L
Papers on GPI-MT-II
Mechanism for release of alkaline phosphatase caused by glycosylphosphatidylinositol deficiency in patients with hyperphosphatasia mental retardation syndrome.
Kinoshita et al., Ōsaka, Japan. In J Biol Chem, 2012
Hyperphosphatasia resulted from secretion of ALP, a GPI-anchored protein normally expressed on the cell surface, into serum due to PIGV deficiency.
Hyperphosphatasia-mental retardation syndrome due to PIGV mutations: expanded clinical spectrum.
Meinecke et al., Berlin, Germany. In Am J Med Genet A, 2011
novel compound heterozygous mutations in the PIGV gene c.467G>A and c.1022C>A and a homozygous mutation c.1022C>A in hyperphosphatasia-mental retardation syndrome
Identity-by-descent filtering of exome sequence data identifies PIGV mutations in hyperphosphatasia mental retardation syndrome.
Robinson et al., Berlin, Germany. In Nat Genet, 2010
PIGV mutations are associated with hyperphosphatasia mental retardation syndrome.
Babesia bovis contains an abundant parasite-specific protein-free glycerophosphatidylinositol and the genes predicted for its assembly.
Florin-Christensen et al., Argentina. In Vet Parasitol, 2010
The potential of B. bovis to assemble the presented free GPI species was verified by the existence of seven genes in its genome that putatively encode the following GPI biosynthetic enzymes: PI N-acetyl-GlcN-transferase (PIG-A and GPI-1), N-acetyl-GlcN-PI-de-N-acetylase (PIG-L), acyltransferase (PIG-W), dolichyl-phosphate mannosyl transferase (DPM-1), GPI mannosyltransferase I (PIG-M), and GPI mannosyltransferase II (PIG-V).
PIG-V involved in transferring the second mannose in glycosylphosphatidylinositol.
Kinoshita et al., Suita, Japan. In J Biol Chem, 2005
PIG-V is the second mannosyltransferase in GPI anchor biosynthesis.
Saccharomyces cerevisiae Ybr004c and its human homologue are required for addition of the second mannose during glycosylphosphatidylinositol precursor assembly.
Taron et al., Beverly, United States. In Febs J, 2005
A bioinformatics-based strategy identified the essential Saccharomyces cerevisiae Ybr004c protein as a candidate for the second GPI alpha-mannosyltransferase (GPI-MT-II).
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