A0A7L1W412 · A0A7L1W412_9PASS
- ProteinPhospholipid phosphatase 1
- GenePlpp1
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids264 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
Catalytic activity
- (9Z)-octadecenoyl-sn-glycero-3-phosphate + H2O = (9Z-octadecenoyl)-glycerol + phosphateThis reaction proceeds in the forward direction.
- 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1,2-di-(9Z-octadecenoyl)-sn-glycerol + phosphateThis reaction proceeds in the forward direction.
- 1,2-dihexadecanoyl-sn-glycero-3-phosphate + H2O = 1,2-dihexadecanoyl-sn-glycerol + phosphateThis reaction proceeds in the forward direction.
- 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1-(9Z-octadecenoyl)-sn-glycerol + phosphateThis reaction proceeds in the forward direction.
- 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + phosphateThis reaction proceeds in the forward direction.
- H2O + N-(9Z-octadecenoyl)-ethanolamine phosphate = N-(9Z-octadecenoyl) ethanolamine + phosphateThis reaction proceeds in the forward direction.
- H2O + N-(octanoyl)-sphing-4-enine-1-phosphate = N-octanoylsphing-4-enine + phosphateThis reaction proceeds in the forward direction.
- H2O + monoacyl-sn-glycero-3-phosphate = a monoacylglycerol + phosphateThis reaction proceeds in the forward direction.
- H2O + sphing-4-enine 1-phosphate = phosphate + sphing-4-enineThis reaction proceeds in the forward direction.
- an N-acylsphing-4-enine 1-phosphate + H2O = an N-acylsphing-4-enine + phosphateThis reaction proceeds in the forward direction.
Pathway
Lipid metabolism; phospholipid metabolism.
Phospholipid metabolism.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | apical plasma membrane | |
Cellular Component | caveola | |
Molecular Function | lysophosphatidic acid phosphatase activity | |
Molecular Function | phosphatidate phosphatase activity | |
Biological Process | phospholipid dephosphorylation | |
Biological Process | phospholipid metabolic process | |
Biological Process | signal transduction |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhospholipid phosphatase 1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Passeriformes > Certhiidae > Certhiinae > Certhia
Accessions
- Primary accessionA0A7L1W412
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Apical cell membrane ; Multi-pass membrane protein
Cell membrane ; Multi-pass membrane protein
Membrane raft ; Multi-pass membrane protein
Membrane, caveola ; Multi-pass membrane protein
Membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 39-62 | Helical | ||||
Sequence: LLAGIIIPFSIIVIILGETLSVFY | ||||||
Transmembrane | 74-92 | Helical | ||||
Sequence: NYIATIYKAIGTFIFGAAA | ||||||
Transmembrane | 146-166 | Helical | ||||
Sequence: LSFYSGHSSFSMYCMLFVALY | ||||||
Transmembrane | 178-197 | Helical | ||||
Sequence: LVRPTIQFGLIAASIYVGLS | ||||||
Transmembrane | 209-231 | Helical | ||||
Sequence: VLTGLIQGAVVAVLIVVYVSDFF |
Keywords
- Cellular component
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 83-224 | Phosphatidic acid phosphatase type 2/haloperoxidase | ||||
Sequence: IGTFIFGAAASQSLTDIAKYSIGRLRPHFIAVCQPDWTRINCSLGYIENFTCHGDKAKINEGRLSFYSGHSSFSMYCMLFVALYLQARMKGDWARLVRPTIQFGLIAASIYVGLSRVSDYKHHWSDVLTGLIQGAVVAVLIV | ||||||
Region | 242-264 | Disordered | ||||
Sequence: EDSHTTLHETPTNGNHFGSNHQP | ||||||
Compositional bias | 249-264 | Polar residues | ||||
Sequence: HETPTNGNHFGSNHQP |
Sequence similarities
Belongs to the PA-phosphatase related phosphoesterase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusFragment
- Length264
- Mass (Da)29,616
- Last updated2021-04-07 v1
- ChecksumFCAB5241C0D2CE80
Features
Showing features for non-terminal residue, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: A | ||||||
Compositional bias | 249-264 | Polar residues | ||||
Sequence: HETPTNGNHFGSNHQP | ||||||
Non-terminal residue | 264 | |||||
Sequence: P |
Keywords
- Technical term