PIGS (gene)

Phosphatidylinositol glycan anchor biosynthesis, class S
Identifiers
Symbols	PIGS ; DKFZp686K20216; FLJ45226
External IDs	OMIM: 610271 MGI: 2687325 HomoloGene: 41963 GeneCards: PIGS Gene
Gene ontology Molecular function • GPI-anchor transamidase activity • protein binding Cellular component • endoplasmic reticulum membrane • membrane • GPI-anchor transamidase complex Biological process • C-terminal protein lipidation • attachment of GPI anchor to protein • post-translational protein modification • cellular protein metabolic process Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	94005	276846
Ensembl	ENSG00000087111	ENSMUSG00000041958
UniProt	Q96S52	Q6PD26
RefSeq (mRNA)	NM_033198	NM_201406
RefSeq (protein)	NP_149975	NP_958808
Location (UCSC)	Chr 17: 28.55 – 28.57 Mb	Chr 11: 78.33 – 78.34 Mb
PubMed search

GPI transamidase component PIG-S is an enzyme that in humans is encoded by the PIGS gene.^[1] This gene encodes a protein that is involved in GPI-anchor biosynthesis. The glycosylphosphatidylinositol (GPI) anchor is a glycolipid found on many blood cells and serves to anchor proteins to the cell surface. This gene encodes an essential component of the multisubunit enzyme, GPI transamidase. GPI transamidase mediates GPI anchoring in the endoplasmic reticulum, by catalyzing the transfer of fully assembled GPI units to proteins.^[1]

References

1. "Entrez Gene: PIGS phosphatidylinositol glycan anchor biosynthesis, class S".

Further reading

• Ohishi K, Inoue N, Kinoshita T (2001). "PIG-S and PIG-T, essential for GPI anchor attachment to proteins, form a complex with GAA1 and GPI8.". EMBO J. 20 (15): 4088–98. doi:10.1093/emboj/20.15.4088. PMC 149153. PMID 11483512.
• Vainauskas S, Maeda Y, Kurniawan H, et al. (2002). "Structural requirements for the recruitment of Gaa1 into a functional glycosylphosphatidylinositol transamidase complex.". J. Biol. Chem. 277 (34): 30535–42. doi:10.1074/jbc.M205402200. PMID 12052837.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Ohishi K, Nagamune K, Maeda Y, Kinoshita T (2003). "Two subunits of glycosylphosphatidylinositol transamidase, GPI8 and PIG-T, form a functionally important intermolecular disulfide bridge.". J. Biol. Chem. 278 (16): 13959–67. doi:10.1074/jbc.M300586200. PMID 12582175.
• Hong Y, Ohishi K, Kang JY, et al. (2004). "Human PIG-U and yeast Cdc91p are the fifth subunit of GPI transamidase that attaches GPI-anchors to proteins.". Mol. Biol. Cell 14 (5): 1780–9. doi:10.1091/mbc.E02-12-0794. PMC 165076. PMID 12802054.
• Clark HF, Gurney AL, Abaya E, et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC 403697. PMID 12975309.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Vainauskas S, Menon AK (2005). "Endoplasmic reticulum localization of Gaa1 and PIG-T, subunits of the glycosylphosphatidylinositol transamidase complex.". J. Biol. Chem. 280 (16): 16402–9. doi:10.1074/jbc.M414253200. PMID 15713669.
• Otsuki T, Ota T, Nishikawa T, et al. (2007). "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries.". DNA Res. 12 (2): 117–26. doi:10.1093/dnares/12.2.117. PMID 16303743.