P53816 · PLAT3_HUMAN
- ProteinPhospholipase A and acyltransferase 3
- GenePLAAT3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids162 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Exhibits both phospholipase A1/2 and acyltransferase activities (PubMed:19047760, PubMed:19615464, PubMed:22605381, PubMed:22825852, PubMed:26503625).
Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids (PubMed:19047760, PubMed:19615464, PubMed:22605381, PubMed:22825852, PubMed:22923616).
For most substrates, PLA1 activity is much higher than PLA2 activity (PubMed:19615464).
Shows O-acyltransferase activity,catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid (PubMed:19615464).
Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE), which serves as precursor for N-acylethanolamines (NAEs) (PubMed:19047760, PubMed:19615464, PubMed:22605381, PubMed:22825852).
Exhibits high N-acyltransferase activity and low phospholipase A1/2 activity (PubMed:22825852).
Required for complete organelle rupture and degradation that occur during eye lens terminal differentiation, when fiber cells that compose the lens degrade all membrane-bound organelles in order to provide lens with transparency to allow the passage of light. Organelle membrane degradation is probably catalyzed by the phospholipase activity (By similarity).
Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids (PubMed:19047760, PubMed:19615464, PubMed:22605381, PubMed:22825852, PubMed:22923616).
For most substrates, PLA1 activity is much higher than PLA2 activity (PubMed:19615464).
Shows O-acyltransferase activity,catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid (PubMed:19615464).
Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE), which serves as precursor for N-acylethanolamines (NAEs) (PubMed:19047760, PubMed:19615464, PubMed:22605381, PubMed:22825852).
Exhibits high N-acyltransferase activity and low phospholipase A1/2 activity (PubMed:22825852).
Required for complete organelle rupture and degradation that occur during eye lens terminal differentiation, when fiber cells that compose the lens degrade all membrane-bound organelles in order to provide lens with transparency to allow the passage of light. Organelle membrane degradation is probably catalyzed by the phospholipase activity (By similarity).
(Microbial infection) Acts as a host factor for picornaviruses: required during early infection to promote viral genome release into the cytoplasm (PubMed:28077878).
May act as a cellular sensor of membrane damage at sites of virus entry, which relocalizes to sites of membrane rupture upon virus unfection (PubMed:28077878).
Facilitates safe passage of the RNA away from LGALS8, enabling viral genome translation by host ribosome (PubMed:28077878).
May also be involved in initiating pore formation, increasing pore size or in maintaining pores for genome delivery (PubMed:28077878).
The lipid-modifying enzyme activity is required for this process (PubMed:28077878).
May act as a cellular sensor of membrane damage at sites of virus entry, which relocalizes to sites of membrane rupture upon virus unfection (PubMed:28077878).
Facilitates safe passage of the RNA away from LGALS8, enabling viral genome translation by host ribosome (PubMed:28077878).
May also be involved in initiating pore formation, increasing pore size or in maintaining pores for genome delivery (PubMed:28077878).
The lipid-modifying enzyme activity is required for this process (PubMed:28077878).
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.
- 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H+ + hexadecanoateThis reaction proceeds in the forward direction.
- 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 2-hexadecanoyl-sn-glycero-3-phosphocholine + H+ + hexadecanoateThis reaction proceeds in the forward direction.
- 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H+ + hexadecanoateThis reaction proceeds in the forward direction.
- 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H+This reaction proceeds in the forward direction.
- 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H+This reaction proceeds in the forward direction.
- 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + H+ + hexadecanoateThis reaction proceeds in the forward direction.
- 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H+This reaction proceeds in the forward direction.
- 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine + H2O = 2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphoethanolamine + H+ + hexadecanoateThis reaction proceeds in the forward direction.
- 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H+This reaction proceeds in the forward direction.
- 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine + H2O = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphoethanolamine + H+ + hexadecanoateThis reaction proceeds in the forward direction.
- 1-hexanoyl-2-acyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + H+ + hexanoateThis reaction proceeds in the forward direction.
- 1-hexanoyl-2-acyl-sn-glycero-3-phosphocholine + H2O = 1-hexanoyl-sn-glycero-3-phosphocholine + a fatty acid + H+This reaction proceeds in the forward direction.
- 1,2-diheptadecanoyl-sn-glycero-3-phosphoethanolamine + 1-(9Z-octadecenoyl)-2-hexadecanoyl-sn-glycero-3-phosphocholine = 1,2-diheptadecanoyl-sn-glycero-3-phospho-N-hexadecanoyl-ethanolamine + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H+This reaction proceeds in the forward direction.
- 1,2-diheptadecanoyl-sn-glycero-3-phosphoethanolamine + 1-(9Z-octadecenoyl)-2-hexadecanoyl-sn-glycero-3-phosphocholine = 1,2-diheptadecanoyl-sn-glycero-3-phospho-N-(9Z-octadecenoyl)-ethanolamine + 2-hexadecanoyl-sn-glycero-3-phosphocholine + H+This reaction proceeds in the forward direction.
- 1,2-dihexanoyl-sn-glycero-3-phosphoethanolamine + 2-heptanoyl-sn-glycero-3-phosphocholine = 1-hexanoyl-2-heptanoyl-sn-glycero-3-phosphocholine + hexanoyl-sn-glycero-3-phosphoethanolamineThis reaction proceeds in the forward direction.
- 1-hexadecanoyl-2-octadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H+ + octadecanoateThis reaction proceeds in the forward direction.
- 1-hexadecanoyl-2-octadecanoyl-sn-glycero-3-phosphocholine + H2O = 2-octadecanoyl-sn-glycero-3-phosphocholine + H+ + hexadecanoateThis reaction proceeds in the forward direction.
- 1-octadecanoyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-octadecanoyl-sn-glycero-3-phosphocholine + H+ + hexadecanoateThis reaction proceeds in the forward direction.
- 1-octadecanoyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = 2-hexadecanoyl-sn-glycero-3-phosphocholine + H+ + octadecanoateThis reaction proceeds in the forward direction.
- 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H+This reaction proceeds in the forward direction.
- 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H2O = 2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H+ + hexadecanoateThis reaction proceeds in the forward direction.
- 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H+This reaction proceeds in the forward direction.
- 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = H+ + hexadecanoate + hexadecanoyl-sn-glycero-3-phosphocholineThis reaction proceeds in the forward direction.
- 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H+This reaction proceeds in the forward direction.
- 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine = H+ + hexadecanoyl-sn-glycero-3-phosphocholine + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamineThis reaction proceeds in the forward direction.
- 1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphocholine + H+This reaction proceeds in the forward direction.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
300 μM | dipalmitoyl-PC |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
2.57 μmol/min/mg | with dipalmitoyl-PC as substrate | ||||
267 nmol/min/mg | with dipalmitoyl-PE as substrate |
pH Dependence
Optimum pH is 9.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 23 | |||||
Sequence: H | ||||||
Active site | 35 | |||||
Sequence: H | ||||||
Active site | 113 | Acyl-thioester intermediate | ||||
Sequence: C |
GO annotations
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Chemistry
Names & Taxonomy
Protein names
- Recommended namePhospholipase A and acyltransferase 3
- 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 accessionP53816
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass membrane protein
Peroxisome membrane ; Single-pass membrane protein
Mitochondrion membrane ; Single-pass membrane protein
Lysosome membrane ; Single-pass membrane protein
Endoplasmic reticulum membrane ; Single-pass membrane protein
Note: During eye lens differentiation, recruited from the cytosol to various organelles, including mitochondria, endoplasmic reticulum, nuclear envelope and lysosomes, immediately before organelle degradation. This translocation is triggered by organelle membrane damage and requires the C-terminal transmembrane domain.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-133 | Cytoplasmic | ||||
Sequence: MRAPIPEPKPGDLIEIFRPFYRHWAIYVGDGYVVHLAPPSEVAGAGAASVMSALTDKAIVKKELLYDVAGSDKYQVNNKHDDKYSPLPCSKIIQRAEELVGQEVLYKLTSENCEHFVNELRYGVARSDQVRDV | ||||||
Transmembrane | 134-154 | Helical | ||||
Sequence: IIAASVAGMGLAAMSLIGVMF | ||||||
Topological domain | 155-162 | Lumenal | ||||
Sequence: SRNKRQKQ |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Lipodystrophy, familial partial, 9 (FPLD9)
- Note
- DescriptionAn autosomal recessive form of partial lipodystrophy, a disorder characterized by abnormal subcutaneous fat distribution. FPLD9 patients are lean and show muscular hypertrophy, insulin-resistant diabetes with hyperinsulinemia, hypertriglyceridemia with low high-density lipoprotein (HDL) cholesterol, liver steatosis, and polycystic ovary syndrome with hirsutism. Some patients have more generalized lipoatrophy, whereas others have abnormal fat accumulation in the face and neck regions and show cushingoid or acromegalic facial features. Most patients also have neurologic features, including demyelinating polyneuropathy, developmental delay and intellectual disability.
- See alsoMIM:620683
Natural variants in FPLD9
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_089309 | 113-162 | missing | in FPLD9; likely pathogenic |
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 23 | No effect on PPP2R1A-binding. | ||||
Sequence: H → A | ||||||
Mutagenesis | 39-57 | Induces a major structural rearrangement accompanied by domain-swapping dimerization and changes in substrate-specificity. | ||||
Sequence: PSEVAGAGAASVMSALTDK → DILLALTDDMGRTQKVVSNKRLILGVIVKV | ||||||
Mutagenesis | 113 | No effect on PPP2R1A-binding. Impaired ability to act as a host factor for picornaviruses. | ||||
Sequence: C → S | ||||||
Natural variant | VAR_089309 | 113-162 | in FPLD9; likely pathogenic | |||
Sequence: Missing |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 226 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000152484 | 1-162 | UniProt | Phospholipase A and acyltransferase 3 | |||
Sequence: MRAPIPEPKPGDLIEIFRPFYRHWAIYVGDGYVVHLAPPSEVAGAGAASVMSALTDKAIVKKELLYDVAGSDKYQVNNKHDDKYSPLPCSKIIQRAEELVGQEVLYKLTSENCEHFVNELRYGVARSDQVRDVIIAASVAGMGLAAMSLIGVMFSRNKRQKQ | |||||||
Modified residue (large scale data) | 85 | PRIDE | Phosphoserine | ||||
Sequence: S |
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed. Low expression, if any, in hematopoietic cells and thymus. In testis, confined to round spermatids. Expressed in normal ovarian epithelial cells. Down-regulated in some ovarian carcinomas and testicular germ cell tumors. Highly expressed in white adipose tissue (PubMed:19136964).
Induction
By IFNG and IRF1.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with PPP2R1A; this interaction might decrease PP2A activity.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P53816 | PPP2R1A P30153 | 7 | EBI-746318, EBI-302388 | |
BINARY | P53816 | UBQLN1 Q9UMX0 | 7 | EBI-746318, EBI-741480 | |
BINARY | P53816 | UBQLN1 Q9UMX0-2 | 3 | EBI-746318, EBI-10173939 | |
BINARY | P53816 | UBQLN2 Q9UHD9 | 3 | EBI-746318, EBI-947187 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 13-129 | LRAT | ||||
Sequence: LIEIFRPFYRHWAIYVGDGYVVHLAPPSEVAGAGAASVMSALTDKAIVKKELLYDVAGSDKYQVNNKHDDKYSPLPCSKIIQRAEELVGQEVLYKLTSENCEHFVNELRYGVARSDQ |
Domain
The C-terminal transmembrane domain is required for the targeting of the protein to damaged organelles.
Sequence similarities
Belongs to the H-rev107 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length162
- Mass (Da)17,937
- Last updated2002-01-31 v2
- Checksum3565BFC756A6DA3C
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F5H7E5 | F5H7E5_HUMAN | PLAAT3 | 27 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 90 | in Ref. 1; CAA63423 and 4; BAH08749 | ||||
Sequence: S → T |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X92814 EMBL· GenBank· DDBJ | CAA63423.1 EMBL· GenBank· DDBJ | mRNA | ||
AB030814 EMBL· GenBank· DDBJ | BAB08108.1 EMBL· GenBank· DDBJ | mRNA | ||
AF317086 EMBL· GenBank· DDBJ | AAL26892.1 EMBL· GenBank· DDBJ | mRNA | ||
AB439591 EMBL· GenBank· DDBJ | BAH08749.1 EMBL· GenBank· DDBJ | mRNA | ||
AK313075 EMBL· GenBank· DDBJ | BAG35901.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471076 EMBL· GenBank· DDBJ | EAW74158.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC001387 EMBL· GenBank· DDBJ | AAH01387.1 EMBL· GenBank· DDBJ | mRNA | ||
BC103807 EMBL· GenBank· DDBJ | AAI03808.1 EMBL· GenBank· DDBJ | mRNA |