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GPI Biosynthesis Report< | ![]() |
| GPI Biosynthesis Main Page | GPI Site Motif | GPI Site Prediction | Home Page B.E. |

| Molecular Function: | Phosphoethanolamine Transferase I |
|---|---|
| Complex: | - |
| Cellular Localization: | ER membrane, ER lumen |
| Domain Architecture: | (cytosol) N --|TM|-----globular Domain(s)-----|multiple TM regions|-- C (?) |
| Orthologues |
|---|
| Protein | Organism | Sequence Length | GenBank Entry |
| NP_186787.1 | Arabidopsis thaliana | 921 | gi|15232100| |
| AAF59557.2 | Caenorhabditis elegans | 929 | gi|16950509| |
| AAF56048.1 | Drosophila melanogaster | 919 | gi|7300908| |
| NP_036459.1 | Homo sapiens | 931 | gi|6912500| |
| NP_038812.1 | Mus musculus | 931 | gi|7305383| |
| NP_012756.1 | Saccharomyces cerevisiae | 919 | gi|6322683| |
| T40715 | Schizosaccharomyces pombe | 935 | gi|7491747| |
Fasta-File of the Family-Members
| Alignments PIG-N: |
- MView - Clustal |
|---|---|
| OMIM: | Entry 606097 |
| PIG-N, GPI7, PIG-O |
- Alignment MView - Alignment Clustal - Tree |
| Literature |
|---|
| PubMed: 11746679 | Conserved core structure and active site residues in alkaline phosphatase superfamily enzymes. Proteins 2001 Dec 1;45(4):318-24 |
| PubMed: 11297516 | Its8, a fission yeast homolog of Mcd4 and Pig-n, is involved in GPI anchor synthesis and shares an essential function with calcineurin in cytokinesis. J Biol Chem 2001 Apr 27;276(17):13579-86 |
| PubMed: 10574991 | Pig-n, a mammalian homologue of yeast Mcd4p, is involved in transferring phosphoethanolamine to the first mannose of the glycosylphosphatidylinositol. J Biol Chem 1999 Dec 3;274(49):35099-106 |
| PubMed: 10069808 | MCD4 encodes a conserved endoplasmic reticulum membrane protein essential for glycosylphosphatidylinositol anchor synthesis in yeast. Mol Biol Cell 1999 Mar;10(3):627-48 |
| PubMed: 9576863 | Saccharomyces cerevisiae GPI10, the functional homologue of human PIG-B, is required for glycosylphosphatidylinositol-anchor synthesis. Biochem J 1998 May 15;332 ( Pt 1):153-9 |

Author: Birgit.Eisenhaber@nt.imp.univie.ac.at on internet.