PIGC

Phosphatidylinositol N-acetylglucosaminyltransferase subunit C is an enzyme that in humans is encoded by the PIGC gene.[5][6][7]

PIGC
Identifiers
Aliases	PIGC, GPI2, phosphatidylinositol glycan anchor biosynthesis class C, MRT62, GPIBD16
External IDs	OMIM: 601730 MGI: 1914542 HomoloGene: 7109 GeneCards: PIGC
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1q24.3 Start 172,370,189 bp[1] End 172,444,086 bp[1]
Gene location (Mouse) Chr. Chromosome 1 (mouse)[2] Band 1|1 H2.1 Start 161,969,186 bp[2] End 161,973,435 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • transferase activity • phosphatidylinositol N-acetylglucosaminyltransferase activity • catalytic activity • transferase activity, transferring glycosyl groups Cellular component • integral component of membrane • endoplasmic reticulum membrane • glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex • endoplasmic reticulum • membrane Biological process • GPI anchor biosynthetic process • preassembly of GPI anchor in ER membrane Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	5279	67292
Ensembl	ENSG00000135845	ENSMUSG00000026698
UniProt	Q92535	Q9CXR4
RefSeq (mRNA)	NM_153747 NM_002642	NM_001039045 NM_026078
RefSeq (protein)	NP_002633 NP_714969	NP_001034134 NP_080354
Location (UCSC)	Chr 1: 172.37 – 172.44 Mb	Chr 1: 161.97 – 161.97 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

This gene encodes an endoplasmic reticulum associated protein that is involved in glycosylphosphatidylinositol (GPI) lipid anchor biosynthesis. The GPI lipid anchor is a glycolipid found on many blood cells and serves to anchor proteins to the cell surface. The encoded protein is one subunit of the GPI N-acetylglucosaminyl (GlcNAc) transferase that transfers GlcNAc to phosphatidylinositol (PI) on the cytoplasmic side of the endoplasmic reticulum. Two alternatively spliced transcripts that encode the same protein have been found for this gene. A pseudogene on chromosome 11 has also been characterized.[7]

Interactions

PIGC has been shown to interact with PIGQ.[8]

References

1. GRCh38: Ensembl release 89: ENSG00000135845 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000026698 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Inoue N, Watanabe R, Takeda J, Kinoshita T (Oct 1996). "PIG-C, one of the three human genes involved in the first step of glycosylphosphatidylinositol biosynthesis is a homologue of Saccharomyces cerevisiae GPI2". Biochem Biophys Res Commun. 226 (1): 193–9. doi:10.1006/bbrc.1996.1332. PMID 8806613.
6. Hong Y, Ohishi K, Inoue N, Endo Y, Fujita T, Takeda J, Kinoshita T (Nov 1997). "Structures and chromosomal localizations of the glycosylphosphatidylinositol synthesis gene PIGC and its pseudogene PIGCP1". Genomics. 44 (3): 347–9. doi:10.1006/geno.1997.4893. PMID 9325057.
7. "Entrez Gene: PIGC phosphatidylinositol glycan anchor biosynthesis, class C".
8. Watanabe, R; Inoue N; Westfall B; Taron C H; Orlean P; Takeda J; Kinoshita T (Feb 1998). "The first step of glycosylphosphatidylinositol biosynthesis is mediated by a complex of PIG-A, PIG-H, PIG-C and GPI1". EMBO J. ENGLAND. 17 (4): 877–85. doi:10.1093/emboj/17.4.877. ISSN 0261-4189. PMC 1170437. PMID 9463366.

Further reading

• Eisenhaber B, Maurer-Stroh S, Novatchkova M, et al. (2003). "Enzymes and auxiliary factors for GPI lipid anchor biosynthesis and post-translational transfer to proteins". BioEssays. 25 (4): 367–85. doi:10.1002/bies.10254. PMID 12655644.
• Adams MD, Kerlavage AR, Fleischmann RD, et al. (1995). "Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence" (PDF). Nature. 377 (6547 Suppl): 3–174. PMID 7566098.
• Watanabe R, Kinoshita T, Masaki R, et al. (1996). "PIG-A and PIG-H, which participate in glycosylphosphatidylinositol anchor biosynthesis, form a protein complex in the endoplasmic reticulum". J. Biol. Chem. 271 (43): 26868–75. doi:10.1074/jbc.271.43.26868. PMID 8900170.
• Watanabe R, Inoue N, Westfall B, et al. (1998). "The first step of glycosylphosphatidylinositol biosynthesis is mediated by a complex of PIG-A, PIG-H, PIG-C and GPI1". EMBO J. 17 (4): 877–85. doi:10.1093/emboj/17.4.877. PMC 1170437. PMID 9463366.
• Watanabe R, Murakami Y, Marmor MD, et al. (2000). "Initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-P and is regulated by DPM2". EMBO J. 19 (16): 4402–11. doi:10.1093/emboj/19.16.4402. PMC 302040. PMID 10944123.
• 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• 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.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. Bibcode:2006Natur.441..315G. doi:10.1038/nature04727. PMID 16710414.