Homo sapiens Protein: PLA2G6
Summary
InnateDB Protein IDBP-293649.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol PLA2G6
Protein Name phospholipase A2, group VI (cytosolic, calcium-independent)
Synonyms CaI-PLA2; GVI; INAD1; iPLA2; IPLA2-VIA; iPLA2beta; NBIA2; NBIA2A; NBIA2B; PARK14; PLA2; PNPLA9;
Species Homo sapiens
Ensembl Protein ENSP00000386100
InnateDB Gene IDBG-7325 (PLA2G6)
Protein Structure
UniProt Annotation
Function Catalyzes the release of fatty acids from phospholipids. It has been implicated in normal phospholipid remodeling, nitric oxide-induced or vasopressin-induced arachidonic acid release and in leukotriene and prostaglandin production. May participate in fas mediated apoptosis and in regulating transmembrane ion flux in glucose-stimulated B-cells. Has a role in cardiolipin (CL) deacylation. Required for both speed and directionality of monocyte MCP1/CCL2-induced chemotaxis through regulation of F- actin polymerization at the pseudopods.Isoform ankyrin-iPLA2-1 and isoform ankyrin-iPLA2-2, which lack the catalytic domain, are probably involved in the negative regulation of iPLA2 activity.
Subcellular Localization Isoform LH-iPLA2: Membrane; Peripheral membrane protein. Note=Recruited to the membrane-enriched pseudopod upon MCP1/CCL2 stimulation in monocytes.Isoform SH-iPLA2: Cytoplasm.
Disease Associations Neurodegeneration with brain iron accumulation 2B (NBIA2B) [MIM:610217]: A neurodegenerative disorder associated with iron accumulation in the brain, primarily in the basal ganglia. It is characterized by progressive extrapyramidal dysfunction leading to rigidity, dystonia, dysarthria and sensorimotor impairment. {ECO:0000269PubMed:16783378}. Note=The disease is caused by mutations affecting the gene represented in this entry.Neurodegeneration with brain iron accumulation 2A (NBIA2A) [MIM:256600]: A neurodegenerative disease characterized by pathologic axonal swelling and spheroid bodies in the central nervous system. Onset is within the first 2 years of life with death by age 10 years. {ECO:0000269PubMed:16783378, ECO:0000269PubMed:17033970, ECO:0000269PubMed:23749988}. Note=The disease is caused by mutations affecting the gene represented in this entry.Parkinson disease 14 (PARK14) [MIM:612953]: An adult- onset progressive neurodegenerative disorder characterized by parkinsonism, dystonia, severe cognitive decline, cerebral and cerebellar atrophy and absent iron in the basal ganglia on magnetic resonance imaging. {ECO:0000269PubMed:18570303}. Note=The disease is caused by mutations affecting the gene represented in this entry.
Tissue Specificity Four different transcripts were found to be expressed in a distinct tissue distribution.
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 10 experimentally validated interaction(s) in this database.
Experimentally validated
Total 10 [view]
Protein-Protein 5 [view]
Protein-DNA 5 [view]
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0004623 phospholipase A2 activity
GO:0005515 protein binding
GO:0005516 calmodulin binding
Biological Process
GO:0006629 lipid metabolic process
GO:0006644 phospholipid metabolic process
GO:0006935 chemotaxis
GO:0008152 metabolic process
GO:0008219 cell death
GO:0016042 lipid catabolic process
GO:0032049 cardiolipin biosynthetic process
GO:0035965 cardiolipin acyl-chain remodeling
GO:0036151 phosphatidylcholine acyl-chain remodeling
GO:0036152 phosphatidylethanolamine acyl-chain remodeling
GO:0038096 Fc-gamma receptor signaling pathway involved in phagocytosis
GO:0044281 small molecule metabolic process
GO:0045087 innate immune response
GO:0046474 glycerophospholipid biosynthetic process
Cellular Component
GO:0005829 cytosol
GO:0016020 membrane
Protein Structure and Domains
PDB ID
InterPro IPR002110 Ankyrin repeat
IPR002641 Patatin/Phospholipase A2-related
IPR016035 Acyl transferase/acyl hydrolase/lysophospholipase
IPR020683 Ankyrin repeat-containing domain
PFAM PF00023
PF13606
PF01734
PF11929
PF12796
PRINTS PR01415
PIRSF
SMART SM00248
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt O60733
PhosphoSite PhosphoSite-O60733
TrEMBL M0R3D9
UniProt Splice Variant
Entrez Gene 8398
UniGene Hs.641914
RefSeq NP_001186491
HUGO HGNC:9039
OMIM 603604
CCDS CCDS33645
HPRD 04675
IMGT
EMBL AF064594 AF102988 AF102989 AF116252 AF116253 AF116254 AF116255 AF116256 AF116257 AF116258 AF116259 AF116260 AF116261 AF116262 AF116263 AF116264 AF116265 AF116266 AF116267 AF117677 AF117678 AF117679 AF117680 AF117681 AF117682 AF117683 AF117684 AF117685 AF117686 AF117687 AF117688 AF117689 AF117690 AF117691 AF117692 AK291212 AL021977 AL022322 AL080187 AY522921 BC036742 BC051904 CH471095 CR456543
GenPept AAC97486 AAD30424 AAD41722 AAD41723 AAF34728 AAH36742 AAH51904 AAR92478 BAF83901 CAA18446 CAB45768 CAG30429 CAQ10446 EAW60219 EAW60220