PIGK

PIGK
Identifiers
Aliases	PIGK , GPI8, phosphatidylinositol glycan anchor biosynthesis class K, NEDHCAS
External IDs	OMIM: 605087 MGI: 1913863 HomoloGene: 4002 GeneCards: PIGK
Gene location (Human) Chr. Chromosome 1 (human) [1] Band 1p31.1 Start 77,088,989 bp [1] End 77,219,430 bp [1]
Gene location (Mouse) Chr. Chromosome 3 (mouse) [2] Band 3|3 H3 Start 152,714,100 bp [2] End 152,980,408 bp [2]
RNA expression pattern Bgee Top expressed in corpus callosum Achilles tendon kidney islet of Langerhans heart Brodmann area 46 bone marrow glomerulus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function GPI-anchor transamidase activity peptidase activity cysteine-type peptidase activity GPI anchor binding GO:0001948 protein binding hydrolase activity protein disulfide isomerase activity Cellular component integral component of membrane integral component of endoplasmic reticulum membrane endoplasmic reticulum membrane membrane GPI-anchor transamidase complex endoplasmic reticulum Biological process GPI anchor biosynthetic process attachment of GPI anchor to protein protein localization to cell surface proteolysis Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	10026	329777
Ensembl	ENSG00000142892	ENSMUSG00000039047
UniProt	Q92643	Q9CXY9
RefSeq (mRNA)	NM_005482	NM_025662 NM_178016
RefSeq (protein)	NP_005473	NP_079938 NP_821135
Location (UCSC)	Chr 1: 77.09 – 77.22 Mb	Chr 3: 152.71 – 152.98 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

GPI-anchor transamidase is an enzyme that in humans is encoded by the PIGK gene. ^{[5] [6]}

This gene encodes a member of the cysteine protease family C13 that is involved in glycosylphosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is a glycolipid found on many blood cells and serves to anchor proteins to the cell surface. This protein is a member of the multisubunit enzyme GPI transamidase and is thought to be its enzymatic component. GPI transamidase mediates GPI anchoring in the endoplasmic reticulum, by catalyzing the transfer of fully assembled GPI units to proteins. ^[6]

Interactions

PIGK has been shown to interact with PIGT ^[7] and GPAA1. ^{[8] [9]}

References

1. GRCh38: Ensembl release 89: ENSG00000142892 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000039047 - 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. Yu J, Nagarajan S, Knez JJ, Udenfriend S, Chen R, Medof ME (December 1997). "The affected gene underlying the class K glycosylphosphatidylinositol (GPI) surface protein defect codes for the GPI transamidase". Proc Natl Acad Sci U S A. 94 (23): 12580–5. Bibcode:1997PNAS...9412580Y. doi: 10.1073/pnas.94.23.12580 . PMC   25045 . PMID   9356492.
6. "Entrez Gene: PIGK phosphatidylinositol glycan anchor biosynthesis, class K".
7. Ohishi, Kazuhito; Nagamune Kisaburo; Maeda Yusuke; Kinoshita Taroh (April 2003). "Two subunits of glycosylphosphatidylinositol transamidase, GPI8 and PIG-T, form a functionally important intermolecular disulfide bridge". J. Biol. Chem. United States. 278 (16): 13959–67. doi: 10.1074/jbc.M300586200 . ISSN   0021-9258. PMID   12582175.
8. Ohishi, K; Inoue N; Maeda Y; Takeda J; Riezman H; Kinoshita T (May 2000). "Gaa1p and gpi8p are components of a glycosylphosphatidylinositol (GPI) transamidase that mediates attachment of GPI to proteins". Mol. Biol. Cell. UNITED STATES. 11 (5): 1523–33. doi:10.1091/mbc.11.5.1523. ISSN   1059-1524. PMC   14864 . PMID   10793132.
9. Vainauskas, Saulius; Maeda Yusuke; Kurniawan Henry; Kinoshita Taroh; Menon Anant K (August 2002). "Structural requirements for the recruitment of Gaa1 into a functional glycosylphosphatidylinositol transamidase complex". J. Biol. Chem. United States. 277 (34): 30535–42. doi: 10.1074/jbc.M205402200 . ISSN   0021-9258. PMID   12052837.

Further reading

• Benghezal M, Benachour A, Rusconi S, et al. (1997). "Yeast Gpi8p is essential for GPI anchor attachment onto proteins". EMBO J. 15 (23): 6575–83. doi:10.1002/j.1460-2075.1996.tb01048.x. PMC   452482 . PMID   8978684.
• Meyer U, Benghezal M, Imhof I, Conzelmann A (2000). "Active site determination of Gpi8p, a caspase-related enzyme required for glycosylphosphatidylinositol anchor addition to proteins". Biochemistry. 39 (12): 3461–71. doi:10.1021/bi992186o. PMID   10727241.
• Ohishi K, Inoue N, Maeda Y, et al. (2000). "Gaa1p and gpi8p are components of a glycosylphosphatidylinositol (GPI) transamidase that mediates attachment of GPI to proteins". Mol. Biol. Cell. 11 (5): 1523–33. doi:10.1091/mbc.11.5.1523. PMC   14864 . PMID   10793132.
• Spurway TD, Dalley JA, High S, Bulleid NJ (2001). "Early events in glycosylphosphatidylinositol anchor addition. substrate proteins associate with the transamidase subunit gpi8p". J. Biol. Chem. 276 (19): 15975–82. doi: 10.1074/jbc.M010128200 . PMID   11278620.
• 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. Bibcode:2002PNAS...9916899M. 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.
• Chen R, Anderson V, Hiroi Y, Medof ME (2003). "Proprotein interaction with the GPI transamidase". J. Cell. Biochem. 88 (5): 1025–37. doi:10.1002/jcb.10439. PMID   12616539. S2CID   12875152.
• 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.
• 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.
• Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC   1356129 . PMID   16344560.
• 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.

External links

• PIGK human gene location in the UCSC Genome Browser .
• PIGK human gene details in the UCSC Genome Browser .