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GPI Anchor Biosynthesis Report: PIG-K family

Molecular Function: part of the transamidase complex, protease
Cellular Localization:mainly ER lumen
Domain Architecture: N Signal Peptide-----globular Domain-------|TM (optional)|-- C

Protein Organism Sequence Length GenBank Entry
T00731 Arabidopsis thaliana 428 gi|7485988|
AN0871.1 Aspergillus nidulans 397  
P49048 Caenorhabditis elegans 322 gi|3123309|
orf6.3728.prot Candida albicans 383  
AAF45703.1 Drosophila melanogaster 322 gi|7290241|
XP_039644.1 Homo sapiens 395 gi|14724559|
CAB55340.1 Leishmania mexicana 349 gi|5834624|
BAB29018.1 Mus musculus 395 gi|12851374|
XP_327545.1 Neurospora crassa 401 gi|32414131|
AAAA01008908 Oryza sativa 404 19933218
AAL29895.1 Paramecium tetraurelia 309 gi|16923219|
CAB96076.1 Plasmodium falciparum 493 gi|8919190|
NP_010618.1 Saccharomyces cerevisiae 411 gi|6320538|
CAC13970.1 Schizosaccharomyces pombe 380 gi|10862894|
CAC67556.1 Trypanosoma brucei 319 gi|15485606|

Fasta-File of the Family-Members

Alignments PIG-K: - MView
- Clustal
OMIM: Entry 605087

PubMed: 11598210 The GPI transamidase complex of Saccharomyces cerevisiae contains Gaa1p, Gpi8p, and Gpi16p.
Mol Biol Cell 2001 Oct;12(10):3295-306
PubMed: 11483512 PIG-S and PIG-T, essential for GPI anchor attachment to proteins, form a complex with GAA1 and GPI8.
EMBO J 2001 Aug 1;20(15):4088-98
PubMed: 11298746 Endoplasmic reticulum proteins involved in glycosylphosphatidylinositol-anchor attachment: photocrosslinking studies in a cell-free system.
Eur J Biochem 2001 Apr;268(8):2290-300
PubMed: 10793132 Gaa1p and gpi8p are components of a glycosylphosphatidylinositol (GPI) transamidase that mediates attachment of GPI to proteins.
Mol Biol Cell 2000 May;11(5):1523-33
PubMed: 10727241 Active site determination of Gpi8p, a caspase-related enzyme required for glycosylphosphatidylinositol anchor addition to proteins.
Biochemistry 2000 Mar 28;39(12):3461-71
PubMed: 8978684 Yeast Gpi8p is essential for GPI anchor attachment onto proteins.
EMBO J 1996 Dec 2;15(23):6575-83
PubMed: 8755508 COOH-terminal processing of nascent polypeptides by the glycosylphosphatidylinositol transamidase in the presence of hydrazine is governed by the same parameters as glycosylphosphatidylinositol addition.
Proc Natl Acad Sci U S A 1996 Jul 23;93(15):7528-33
PubMed: 7642644 An active carbonyl formed during glycosylphosphatidylinositol addition to a protein is evidence of catalysis by a transamidase.
J Biol Chem 1995 Aug 18;270(33):19576-82
PubMed: 7878018 Cleavage without anchor addition accompanies the processing of a nascent protein to its glycosylphosphatidylinositol-anchored form.
Proc Natl Acad Sci U S A 1995 Feb 28;92(5):1550-4
PubMed: 7651176 Processing of nascent proteins to glycosylphosphatidylinositol-anchored forms in cell-free systems.
Methods Enzymol 1995;250:536-47

Author: on internet.
Last modified: 25th November 2003