A0A7J7F7X3 · A0A7J7F7X3_DICBM
- ProteinPhospholipase A1 member A
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids463 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Hydrolyzes the ester bond of the acyl group attached at the sn-1 position of phosphatidylserines (phospholipase A1 activity) and 1-acyl-2-lysophosphatidylserines (lysophospholipase activity) in the pathway of phosphatidylserines acyl chain remodeling. Cleaves phosphatidylserines exposed on the outer leaflet of the plasma membrane of apoptotic cells producing 2-acyl-1-lysophosphatidylserines, which in turn enhance mast cell activation and histamine production. Has no activity toward other glycerophospholipids including phosphatidylcholines, phosphatidylethanolamines, phosphatidic acids or phosphatidylinositols, or glycerolipids such as triolein.
Catalytic activity
- 1,2-di-(9Z)-octadecenoyl-sn-glycero-3-phospho-L-serine + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + (9Z)-octadecenoate + H+This reaction proceeds in the forward direction.
- 1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = sn-glycero-3-phospho-L-serine + (9Z)-octadecenoate + H+This reaction proceeds in the forward direction.
- 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-L-serine + H2O = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phospho-L-serine + hexadecanoate + H+This reaction proceeds in the forward direction.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 173 | Nucleophile | ||||
Sequence: S | ||||||
Active site | 197 | Charge relay system | ||||
Sequence: D | ||||||
Binding site | 211 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 213 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 216 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 267 | Charge relay system | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular space | |
Molecular Function | lipoprotein lipase activity | |
Molecular Function | metal ion binding | |
Biological Process | fatty acid biosynthetic process | |
Biological Process | triglyceride catabolic process |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhospholipase A1 member A
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Perissodactyla > Rhinocerotidae > Diceros
Accessions
- Primary accessionA0A7J7F7X3
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-24 | |||||
Sequence: MPPGLWERRCWVWGLLLWLSVGNA | ||||||
Chain | PRO_5029905585 | 25-463 | Phospholipase A1 member A | |||
Sequence: GDAPPTQQPKCTDFQNANLLRGTNLKVQFLLFTPSDPSCGQLVEESSDIQNSGFNVTLGTKLIIHGFRALGTKPSWIGKFIGALLRAVDANVIAVDWVYGSSGAYFSAVENVVKLGLEISRFLRKLLVGAEELRVLGVSESSIHILGVSLGAHVGGMVGHFYKGQLGRITGLDPAGPEYTRASLEERLDAGDALFVEAIHTDTDNLGIRIPVGHVDYFVNGGQDQPGCPSFIHAGYSYLICDHMRAVHLYISALENSCPLMAFPCASYKAFLAGHCLDCFNPFLLSCPRIGLVEQDGVKIEPLPKEVRVYLLTSSKAPYCVHHSFVEFYLQEPRKKDTSIAVTFLSGNVTSSVKITIPRQQLQGKGVIAHPNPQCQINQVKLKLQASNRVWKKDRTTIVGTFCTAPLPVHDNKKMVCLPEPVNLQASVTVSHDLKITCV |
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 17-343 | Lipase | ||||
Sequence: LWLSVGNAGDAPPTQQPKCTDFQNANLLRGTNLKVQFLLFTPSDPSCGQLVEESSDIQNSGFNVTLGTKLIIHGFRALGTKPSWIGKFIGALLRAVDANVIAVDWVYGSSGAYFSAVENVVKLGLEISRFLRKLLVGAEELRVLGVSESSIHILGVSLGAHVGGMVGHFYKGQLGRITGLDPAGPEYTRASLEERLDAGDALFVEAIHTDTDNLGIRIPVGHVDYFVNGGQDQPGCPSFIHAGYSYLICDHMRAVHLYISALENSCPLMAFPCASYKAFLAGHCLDCFNPFLLSCPRIGLVEQDGVKIEPLPKEVRVYLLTSSKAPY |
Sequence similarities
Belongs to the AB hydrolase superfamily. Lipase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length463
- Mass (Da)50,664
- Last updated2021-04-07 v1
- ChecksumC0903F1F41450234
Keywords
- Technical term