Description: Homo sapiens phosphatidylinositol glycan anchor biosynthesis, class N (PIGN), transcript variant 2, mRNA. RefSeq Summary (NM_176787): This gene encodes a protein that is involved in glycosylphosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is a glycolipid found on many blood cells and serves to anchor proteins to the cell surface. This protein is expressed in the endoplasmic reticulum and transfers phosphoethanolamine (EtNP) to the first mannose of the GPI anchor. Two alternatively spliced variants, which encode an identical isoform, have been reported. [provided by RefSeq, Jul 2008]. Transcript (Including UTRs) Position: hg19 chr18:59,711,458-59,828,618 Size: 117,161 Total Exon Count: 28 Strand: - Coding Region Position: hg19 chr18:59,713,089-59,828,586 Size: 115,498 Coding Exon Count: 28
ID:PIGN_HUMAN DESCRIPTION: RecName: Full=GPI ethanolamine phosphate transferase 1; EC=2.-.-.-; AltName: Full=MCD4 homolog; AltName: Full=Phosphatidylinositol-glycan biosynthesis class N protein; Short=PIG-N; FUNCTION: Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor (By similarity). PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol- anchor biosynthesis. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein (By similarity). DISEASE: Defects in PIGN are the cause of multiple congenital anomalies-hypotonia-seizures syndrome type 1 (MCAHS1) [MIM:614080]. An autosomal recessive disorder characterized by neonatal hypotonia, lack of psychomotor development, seizures, dysmorphic features, and variable congenital anomalies involving the cardiac, urinary, and gastrointestinal systems. Most affected individuals die before 3 years of age. SIMILARITY: Belongs to the PIGG/PIGN/PIGO family. PIGN subfamily.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on O95427
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
US Server
