A0A7J8KEJ4 · A0A7J8KEJ4_ROUAE
- ProteinPhospholipase A2
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids148 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
Catalytic activity
- 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + hexadecanoate + H+This reaction proceeds in the forward direction.
- 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + (9Z,12Z)-octadecadienoate + H+This reaction proceeds in the forward direction.
- 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O = 1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + (9Z)-octadecenoate + H+This reaction proceeds in the forward direction.
- 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + (9Z)-octadecenoate + H+This reaction proceeds in the forward direction.
- N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O = N-hexadecanoyl-1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + (9Z)-octadecenoate + H+This reaction proceeds in the forward direction.
Cofactor
Note: Binds 1 Ca2+ ion per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 49 | Ca2+ (UniProtKB | ChEBI) | |||
Binding site | 51 | Ca2+ (UniProtKB | ChEBI) | |||
Active site | 67 | ||||
Binding site | 68 | Ca2+ (UniProtKB | ChEBI) | |||
Active site | 112 | ||||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | calcium ion binding | |
Molecular Function | calcium-dependent phospholipase A2 activity | |
Molecular Function | phospholipid binding | |
Biological Process | arachidonic acid secretion | |
Biological Process | lipid catabolic process | |
Biological Process | negative regulation of T cell proliferation | |
Biological Process | phospholipid metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhospholipase A2
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Chiroptera > Yinpterochiroptera > Pteropodoidea > Pteropodidae > Rousettinae > Rousettus
Accessions
- Primary accessionA0A7J8KEJ4
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-20 | ||||
Chain | PRO_5029950211 | 21-148 | Phospholipase A2 | ||
Disulfide bond | 46↔141 | ||||
Disulfide bond | 48↔64 | ||||
Disulfide bond | 63↔118 | ||||
Disulfide bond | 70↔111 | ||||
Disulfide bond | 79↔104 | ||||
Disulfide bond | 97↔109 | ||||
Keywords
- PTM
Structure
Sequence
- Sequence statusComplete
- Length148
- Mass (Da)17,102
- Last updated2021-04-07 v1
- MD5 Checksum46877956A4485E88763E13096A2AB601
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JACASE010000001 EMBL· GenBank· DDBJ | KAF6507244.1 EMBL· GenBank· DDBJ | Genomic DNA |