O43688 · PLPP2_HUMAN
- ProteinPhospholipid phosphatase 2
- GenePLPP2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids288 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Has no apparent extracellular phosphatase activity and therefore most probably acts intracellularly (PubMed:16467304).
Also acts on N-oleoyl ethanolamine phosphate/N-(9Z-octadecenoyl)-ethanolamine phosphate, a potential physiological compound (PubMed:9607309).
Through dephosphorylation of these bioactive lipid mediators produces new bioactive compounds and may regulate signal transduction in different cellular processes (Probable). Indirectly regulates, for instance, cell cycle G1/S phase transition through its phospholipid phosphatase activity (By similarity).
Catalytic activity
- a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-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.
- 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1,2-di-(9Z-octadecenoyl)-sn-glycerol + phosphateThis reaction proceeds in the forward direction.
- H2O + monoacyl-sn-glycero-3-phosphate = a monoacylglycerol + phosphateThis reaction proceeds in the forward direction.
- (9Z)-octadecenoyl-sn-glycero-3-phosphate + H2O = (9Z-octadecenoyl)-glycerol + 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.
- H2O + N-(octanoyl)-sphing-4-enine-1-phosphate = N-octanoylsphing-4-enine + phosphateThis reaction proceeds in the forward direction.
- H2O + N-(9Z-octadecenoyl)-ethanolamine phosphate = N-(9Z-octadecenoyl) ethanolamine + phosphateThis reaction proceeds in the forward direction.
Activity regulation
Insensitive to N-ethylmaleimide (PubMed:9705349).
Inhibited by sphingosine, zinc ions and modestly by propanolol (PubMed:9607309, PubMed:9705349).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
150 μM | 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate | |||||
340 μM | (9Z)-octadecenoyl-sn-glycero-3-phosphate | |||||
138 μM | N-oleoyl ethanolamine phosphatidic acid |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
0.15 nmol/min/mg | with 1,2-dihexadecanoyl-sn-glycero-3-phosphate as substrate | ||||
0.2 nmol/min/mg | with (9Z)-octadecenoyl-sn-glycero-3-phosphate as substrate | ||||
0.17 nmol/min/mg | with N-(octanoyl)-sphing-4-enine-1-phosphate as substrate | ||||
0.69 nmol/min/mg | with sphing-4-enine 1-phosphate as substrate | ||||
34 nmol/min/mg | with 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate as substrate | ||||
49 nmol/min/mg | with (9Z)-octadecenoyl-sn-glycero-3-phosphate as substrate | ||||
17 nmol/min/mg | with N-oleoyl ethanolamine phosphatidic acid as substrate |
Pathway
Features
Showing features for active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 168 | Proton donors | ||||
Sequence: H | ||||||
Active site | 220 | Nucleophile | ||||
Sequence: H | ||||||
Site | 224 | Stabilizes the active site histidine for nucleophilic attack | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | caveola | |
Cellular Component | early endosome | |
Cellular Component | early endosome membrane | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | membrane | |
Cellular Component | plasma membrane | |
Molecular Function | ceramide-1-phosphate phosphatase activity | |
Molecular Function | phosphatidate phosphatase activity | |
Molecular Function | sphingosine-1-phosphate phosphatase activity | |
Biological Process | ceramide metabolic process | |
Biological Process | phospholipid dephosphorylation | |
Biological Process | phospholipid metabolic process | |
Biological Process | signal transduction | |
Biological Process | sphingolipid catabolic process | |
Biological Process | sphingosine metabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Chemistry
Names & Taxonomy
Protein names
- Recommended namePhospholipid phosphatase 2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO43688
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-4 | Cytoplasmic | ||||
Sequence: MQRR | ||||||
Transmembrane | 5-25 | Helical | ||||
Sequence: WVFVLLDVLCLLVASLPFAIL | ||||||
Topological domain | 26-51 | Lumenal | ||||
Sequence: TLVNAPYKRGFYCGDDSIRYPYRPDT | ||||||
Transmembrane | 52-72 | Helical | ||||
Sequence: ITHGLMAGVTITATVILVSAG | ||||||
Topological domain | 73-87 | Cytoplasmic | ||||
Sequence: EAYLVYTDRLYSRSD | ||||||
Transmembrane | 88-108 | Helical | ||||
Sequence: FNNYVAAVYKVLGTFLFGAAV | ||||||
Topological domain | 109-162 | Lumenal | ||||
Sequence: SQSLTDLAKYMIGRLRPNFLAVCDPDWSRVNCSVYVQLEKVCRGNPADVTEARL | ||||||
Transmembrane | 163-183 | Helical | ||||
Sequence: SFYSGHSSFGMYCMVFLALYV | ||||||
Topological domain | 184-196 | Cytoplasmic | ||||
Sequence: QARLCWKWARLLR | ||||||
Transmembrane | 197-217 | Helical | ||||
Sequence: PTVQFFLVAFALYVGYTRVSD | ||||||
Topological domain | 218-226 | Lumenal | ||||
Sequence: YKHHWSDVL | ||||||
Transmembrane | 227-247 | Helical | ||||
Sequence: VGLLQGALVAALTVCYISDFF | ||||||
Topological domain | 248-288 | Cytoplasmic | ||||
Sequence: KARPPQHCLKEEELERKPSLSLTLTLGEADHNHYGYPHSSS |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_061541 | 180 | in dbSNP:rs1138439 | |||
Sequence: A → V | ||||||
Mutagenesis | 214 | Loss of lipid phosphatase activity. | ||||
Sequence: R → K |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 374 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, glycosylation, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000220909 | 1-288 | UniProt | Phospholipid phosphatase 2 | |||
Sequence: MQRRWVFVLLDVLCLLVASLPFAILTLVNAPYKRGFYCGDDSIRYPYRPDTITHGLMAGVTITATVILVSAGEAYLVYTDRLYSRSDFNNYVAAVYKVLGTFLFGAAVSQSLTDLAKYMIGRLRPNFLAVCDPDWSRVNCSVYVQLEKVCRGNPADVTEARLSFYSGHSSFGMYCMVFLALYVQARLCWKWARLLRPTVQFFLVAFALYVGYTRVSDYKHHWSDVLVGLLQGALVAALTVCYISDFFKARPPQHCLKEEELERKPSLSLTLTLGEADHNHYGYPHSSS | |||||||
Glycosylation | 139 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue (large scale data) | 266 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 268 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 270 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 272 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 281 | PRIDE | Phosphotyrosine | ||||
Sequence: Y |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Can also form heterooligomers with PLPP1 and PLPP3 (PubMed:18215144).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O43688 | HNF4A P41235-3 | 3 | EBI-722017, EBI-12690684 | |
BINARY | O43688 | JAGN1 Q8N5M9 | 3 | EBI-722017, EBI-10266796 | |
BINARY | O43688 | NOTCH2NLA Q7Z3S9 | 3 | EBI-722017, EBI-945833 | |
BINARY | O43688 | NSG1 P42857 | 3 | EBI-722017, EBI-6380741 | |
BINARY | O43688 | TRAM1L1 Q8N609 | 3 | EBI-722017, EBI-11996766 | |
BINARY | O43688 | VSTM1 Q6UX27-3 | 3 | EBI-722017, EBI-12190699 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 117-125 | Phosphatase sequence motif I | ||||
Sequence: KYMIGRLRP | ||||||
Region | 165-168 | Phosphatase sequence motif II | ||||
Sequence: YSGH | ||||||
Region | 213-224 | Phosphatase sequence motif III | ||||
Sequence: TRVSDYKHHWSD |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
O43688-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length288
- Mass (Da)32,574
- Last updated1998-06-01 v1
- ChecksumF7C6A09A28DA9AC8
O43688-2
- Name2
- Differences from canonical
- 1-17: MQRRWVFVLLDVLCLLV → MGVARGPGSRGQHPPPRQQEVCAEGPRARLHPAPPGLG
O43688-3
- Name3
- Differences from canonical
- 1-56: Missing
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0J9YXA3 | A0A0J9YXA3_HUMAN | PLPP2 | 208 | ||
K7EMK9 | K7EMK9_HUMAN | PLPP2 | 178 | ||
K7ENH4 | K7ENH4_HUMAN | PLPP2 | 136 |
Features
Showing features for alternative sequence.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF035959 EMBL· GenBank· DDBJ | AAC15968.1 EMBL· GenBank· DDBJ | mRNA | ||
AF047760 EMBL· GenBank· DDBJ | AAC32104.1 EMBL· GenBank· DDBJ | mRNA | ||
AF056083 EMBL· GenBank· DDBJ | AAC25666.1 EMBL· GenBank· DDBJ | mRNA | ||
BT007021 EMBL· GenBank· DDBJ | AAP35667.1 EMBL· GenBank· DDBJ | mRNA | ||
AC016588 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC002806 EMBL· GenBank· DDBJ | AAH02806.1 EMBL· GenBank· DDBJ | mRNA |