SCUBA

PLAAT3 — Phospholipase A and acyltransferase 3

PLAAT3 belongs to a gene co-expression module in 5 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.

PLAAT3's module in each cell type

Cell typeModuleShares the module with
Gamma-delta T cellsLysosomal Biogenesis
Protein processing & ER
ABI3, APLP2, ATP10A, B3GALT4, BAX, CD63, CTNNA1, DOCK5 +14 more
Lymphatic endothelialLymphatic Valve Identity
Valve formation
ALCAM, C12orf57, C17orf58, CFH, CLDN11, DEGS2, EBPL, EDNRB +13 moreView in SCUBA
MacrophagesAntimicrobial Oxidative Defense
Antibacterial
ADAMDEC1, ALDOA, APOL3, CALHM6, CLEC10A, COX16, CPVL, DEFA5 +30 moreView in SCUBA
MonocytesInflammatory Monocyte Activation
Inflammatory
ANG, ANXA2, CD99, IGFBP7, MGST1, RNASE2, S100A10, ST14View in SCUBA
Natural Killer cellsSeptin Cytoskeletal Assembly
Cytoskeleton & motility
ALDOA, EEF1G, MIF, NME2, POLD4, SEPTIN1, SEPTIN2, SEPTIN6View in SCUBA

About the gene

SynonymsAdPLA, H-REV107-1, HRASLS3, HREV107, HREV107-3, MGC118754., PLA2G16, PLAAT-3
Chromosome11: 63573195-63616883
Predicted locationIntracellular, Membrane
Essential geneNo
Protein classEnzymes, Metabolic proteins, Predicted intracellular proteins, Predicted membrane proteins, RAS pathway related proteins
Molecular functionHydrolase, Transferase
Biological processHost-virus interaction, Lipid degradation, Lipid metabolism

Function

Exhibits both phospholipase A1/2 and acyltransferase activities. Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids. For most substrates, PLA1 activity is much higher than PLA2 activity. Shows O-acyltransferase activity,catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid. Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N- acylphosphatidylethanolamine (NAPE), which serves as precursor for N- acylethanolamines (NAEs). Exhibits high N-acyltransferase activity and low phospholipase A1/2 activity. Required for complete organelle rupture and degradation that occur during eye lens terminal differentiation, when fiber cells that compose the lens degrade all membrane-bound organelles in order to provide lens with transparency to allow the passage of light. Organelle membrane degradation is probably catalyzed by the phospholipase activity (By similarity). (Microbial infection) Acts as a host factor for picornaviruses: required during early infection to promote viral genome release into the cytoplasm. May act as a cellular sensor of membrane damage at sites of virus entry, which relocalizes to sites of membrane rupture upon virus unfection. Facilitates safe passage of the RNA away from LGALS8, enabling viral genome translation by host ribosome. May also be involved in initiating pore formation, increasing pore size or in maintaining pores for genome delivery. The lipid- modifying enzyme activity is required for this process

Human Protein Atlas · Open Targets · UniProt

Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.