J4KMY5 · PLA2_BEAB2
- ProteinSecretory phospholipase A2
- GenePLA2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids190 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Secretory phospholipase that catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (PubMed:35276754).
Increases the ability to utilize insect-derived nutrients and lipids, and promotes lipid dropplets accumulation (PubMed:35276754).
Plays a role in virulence, including more efficient penetration of the insect cuticle and evasion of host immune response by repressing the expression of host immunity genes (PubMed:35276754).
Increases the ability to utilize insect-derived nutrients and lipids, and promotes lipid dropplets accumulation (PubMed:35276754).
Plays a role in virulence, including more efficient penetration of the insect cuticle and evasion of host immune response by repressing the expression of host immunity genes (PubMed:35276754).
Catalytic activity
- a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H+This reaction proceeds in the forward direction.
Cofactor
Note: Binds 1 Ca2+ ion per subunit.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.56 mM | phosphatidyl-choline |
pH Dependence
Optimum pH is 7.0-11.0.
Temperature Dependence
Optimum temperature is 35 degrees Celsius.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | lipid droplet | |
Molecular Function | metal ion binding | |
Molecular Function | phospholipase A2 activity | |
Biological Process | arachidonic acid secretion | |
Biological Process | lipid catabolic process | |
Biological Process | phospholipid metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSecretory phospholipase A2
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Cordycipitaceae > Beauveria
Accessions
- Primary accessionJ4KMY5
Proteomes
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Decreases the ability to penetrate the host cuticle and impairs the repression of host immunity genes.
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-15 | |||||
Sequence: MKLAYFSSLLPLALA | ||||||
Chain | PRO_5012361776 | 16-190 | Secretory phospholipase A2 | |||
Sequence: APASVVDPREPKEDITDRYLFSTPLPTFLEYREKENPDSLDWTSDGCTHASNNPFGFPFEPACQRHDFGYRNYQAQTRFESDSRYRIDLNFYNDMIFQCTDVSALRSCHGLADVYYAGVRMFGGFAKRDEMGAVVASATDPKESAEDLIAVYYTALQEYHQAVKADQADGLLPRL | ||||||
Disulfide bond | 62↔78 | |||||
Sequence: CTHASNNPFGFPFEPAC |
Keywords
- PTM
Structure
Family & Domains
Sequence similarities
Belongs to the phospholipase A2 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length190
- Mass (Da)21,498
- Last updated2012-10-31 v1
- Checksum4BA4B74AF0871E69
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JH725167 EMBL· GenBank· DDBJ | EJP64764.1 EMBL· GenBank· DDBJ | Genomic DNA |