PGAP6 — Post-GPI attachment to proteins 6
PGAP6 belongs to a gene co-expression module in 3 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.
PGAP6's module in each cell type
| Cell type | Module | Shares the module with | |
|---|---|---|---|
| Gamma-delta T cells | Polycomb Transcriptional Control DNA/chromatin regulation | AMFR, ATMIN, BRD7, CBX4, CCNY, CD81, CDK2AP1, CSNK1E +17 more | |
| Macrophages | Monocyte Innate Signaling Innate immunity | ADAMTSL4, IRAK1, LILRB3, MMP24OS, MYO1G, PLIN3, SHKBP1, STXBP2 +2 more | View in SCUBA |
| Mucosal-associated invariant T cell | Polycomb Repression DNA/chromatin regulation | BTBD6, CBX4, CD81, CSNK1G2, CTBP1, DUS1L, GNB1, GRK6 +15 more |
About the gene
| Synonyms | M83, TMEM6, TMEM8, TMEM8A |
|---|---|
| Chromosome | 16: 370788-387113 |
| Predicted location | Intracellular, Membrane |
| Essential gene | No |
| Protein class | Enzymes, Predicted intracellular proteins, Predicted membrane proteins, Transporters |
| Molecular function | Hydrolase |
| Biological process | Lipid metabolism |
Function
Involved in the lipid remodeling steps of GPI-anchor maturation. Lipid remodeling steps consist in the generation of 2 saturated fatty chains at the sn-2 position of GPI-anchor proteins (GPI-AP). Has phospholipase A2 activity that removes an acyl-chain at the sn-2 position of GPI-anchors during the remodeling of GPI. Required for the shedding of the GPI-AP CRIPTO, but not CFC1, at the cell surface. Shedding of CRIPTO modulates Nodal signaling by allowing soluble CRIPTO to act as a Nodal coreceptor on other cells. Also indirectly involved in the translocation of RAC1 from the cytosol to the plasma membrane by maintaining the steady state amount of CAV1-enriched plasma membrane subdomains, stabilizing RAC1 at the plasma membrane. In contrast to myomaker (TMEM8C), has no fusogenic activity.
Human Protein Atlas · Open Targets · UniProt
Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.