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GPI Anchor Biosynthesis Report: PIG-A family

Molecular Function: part of the UDP-GlcNAc transferase complex, enzymatic component
Complex: PIG-A/ GPI3, PIG-H/ GPI15, PIG-C/ GPI2, PIG-Q/ GPI1, PIG-P/ YDR437W, DPM2
Cellular Localization:ER membrane, cytosol
Domain Architecture:(cytosol) N -----globular Domain 1----------globular Domain 2-----|TM|-- C (ER lumen)

Protein Organism Sequence Length GenBank Entry
AAK62657.1 Arabidopsis thaliana 447 gi|14517534|
T20374 Caenorhabditis elegans 444 gi|7498233|
orf6.7084.prot Candida albicans 452  
AAF57802 Drosophila melanogaster 479 gi|7302724|
NP_002632.1 Homo sapiens 484 gi|11863130|
A55731 Mus musculus 485 gi|1083342|
AAF76891.1 Paramecium tetraurelia 442 gi|8571458|
NP_015150 Saccharomyces cerevisiae 452 gi|9755344|
T40367 Schizosaccharomyces pombe 456 gi|7492221|

Fasta-File of the Family-Members

Alignments: - MView
- Clustal
OMIM: Entry 311770

PubMed: 10716631 Characterisation of the enzymatic complex for the first step in glycosylphosphatidylinositol biosynthesis.
Int J Biochem Cell Biol 2000 Mar;32(3):339-50
PubMed: 9463366 The first step of glycosylphosphatidylinositol biosynthesis is mediated by a complex of PIG-A, PIG-H, PIG-C and GPI1.
EMBO J 1998 Feb 16;17(4):877-85
PubMed: 9398536 Structural and functional analysis of the Pig-a protein that is mutated in paroxysmal nocturnal hemoglobinuria.
Blood Cells Mol Dis 1997 Dec;23(3):350-60
PubMed: 8900170 PIG-A and PIG-H, which participate in glycosylphosphatidylinositol anchor biosynthesis, form a protein complex in the endoplasmic reticulum.
J Biol Chem 1996 Oct 25;271(43):26868-75
PubMed: 7680492 The cloning of PIG-A, a component in the early step of GPI-anchor biosynthesis.
Science 1993 Feb 26;259(5099):1318-20

Author: on internet.
Last modified: 24th January 2003