UniProtKB - Q9NWW9 (PLAT2_HUMAN)
Phospholipase A and acyltransferase 2
PLAAT2
Functioni
Exhibits both phospholipase A1/2 and acyltransferase activities (PubMed:19615464, PubMed:22825852, PubMed:22605381, 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:19615464, PubMed:22825852, PubMed:22605381).
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:19615464, PubMed:22825852, PubMed:22605381).
Catalyzes N-acylation of PE using both sn-1 and sn-2 palmitoyl groups of PC as acyl donor (PubMed:22605381).
Exhibits high phospholipase A1/2 activity and low N-acyltransferase activity (PubMed:22825852).
1 Publication3 PublicationsCatalytic activityi
- a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H+3 PublicationsEC:3.1.1.43 PublicationsThis reaction proceeds in the forward1 Publication direction.
- a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H+3 PublicationsEC:3.1.1.323 PublicationsThis reaction proceeds in the forward1 Publication direction.
- a 1,2-diacyl-sn-glycero-3-phosphocholine + a 1,2-diacyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-sn-glycero-3-phosphocholine + H+ + N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine1 PublicationThis reaction proceeds in the forward1 Publication direction.
- a 1,2-diacyl-sn-glycero-3-phosphocholine + a 1,2-diacyl-sn-glycero-3-phosphoethanolamine = a 2-acyl-sn-glycero-3-phosphocholine + H+ + N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine1 PublicationThis reaction proceeds in the forward1 Publication direction.
- 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H+ + hexadecanoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 2-hexadecanoyl-sn-glycero-3-phosphocholine + H+ + hexadecanoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H+ + hexadecanoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H+1 PublicationThis reaction proceeds in the forward1 Publication 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+ + hexadecanoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H+1 PublicationThis reaction proceeds in the forward1 Publication direction.
- 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine + H2O = 2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphoethanolamine + H+ + hexadecanoate1 PublicationThis reaction proceeds in the forward1 Publication 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+1 PublicationThis reaction proceeds in the forward1 Publication 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+ + hexadecanoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine = 2-hexadecanoyl-sn-glycero-3-phosphocholine + H+ + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine1 PublicationThis reaction proceeds in the forward1 Publication direction.
- 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H+ + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine2 PublicationsThis reaction proceeds in the forward2 Publications direction.
- 1-hexanoyl-2-acyl-sn-glycero-3-phosphocholine + H2O = 1-hexanoyl-sn-glycero-3-phosphocholine + a fatty acid + H+1 PublicationThis reaction proceeds in the forward1 Publication 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+1 PublicationThis reaction proceeds in the forward1 Publication 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+1 PublicationThis reaction proceeds in the forward1 Publication direction.
- 1,2-diheptanoyl-sn-glycero-3-phosphocholine + 1,2-dihexanoyl-sn-glycero-3-phosphocholine = 1-heptanoyl-2-hexanoyl-sn-glycero-3-phosphocholine + 1-hexanoyl-2-heptanoyl-sn-glycero-3-phosphocholine1 PublicationThis reaction proceeds in the forward1 Publication direction.
- 1,2-diheptanoyl-sn-glycero-3-phosphocholine + 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine = 1-heptanoyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + 1-hexadecanoyl-2-heptanoyl-sn-glycero-3-phosphocholine1 PublicationThis reaction proceeds in the forward1 Publication direction.
- 1,2-diheptanoyl-sn-glycero-3-phosphocholine + 1,2-dihexanoyl-sn-glycero-3-phosphoethanolamine = 1-heptanoyl-2-hexanoyl-sn-glycero-3-phosphoethanolamine + 1-hexanoyl-2-heptanoyl-sn-glycero-3-phosphocholine1 PublicationThis reaction proceeds in the forward1 Publication direction.
- 1-hexanoyl-2-acyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + H+ + hexanoate1 PublicationThis reaction proceeds in the forward1 Publication 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-phosphoethanolamine1 PublicationThis reaction proceeds in the forward1 Publication direction.
Kineticsi
- KM=300 µM for dipalmitoyl-PC1 Publication
- Vmax=670 nmol/min/mg enzyme with dipalmitoyl-PC as substrate1 Publication
- Vmax=122 nmol/min/mg enzyme with dipalmitoyl-PE as substrate1 Publication
- Vmax=103 nmol/min/mg enzyme using dipalmitoyl-PC as an acyl donor and PE as an acyl acceptor1 Publication
pH dependencei
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 23 | PROSITE-ProRule annotation1 Publication | 1 | |
Active sitei | 35 | PROSITE-ProRule annotation1 Publication | 1 | |
Active sitei | 113 | Acyl-thioester intermediatePROSITE-ProRule annotation1 Publication | 1 |
GO - Molecular functioni
- 1-acyl-2-lysophosphatidylserine acylhydrolase activity Source: UniProtKB-EC
- acyltransferase activity Source: Reactome
- N-acyltransferase activity Source: UniProtKB
- phosphatidylserine 1-acylhydrolase activity Source: UniProtKB-EC
- phospholipase A1 activity Source: UniProtKB
- phospholipase A2 activity Source: UniProtKB
GO - Biological processi
- lipid catabolic process Source: UniProtKB-KW
- N-acylphosphatidylethanolamine metabolic process Source: UniProtKB
- phosphatidylethanolamine acyl-chain remodeling Source: Reactome
Keywordsi
Molecular function | Acyltransferase, Hydrolase, Transferase |
Biological process | Lipid degradation, Lipid metabolism |
Enzyme and pathway databases
BRENDAi | 2.7.1.22, 2681 |
PathwayCommonsi | Q9NWW9 |
Reactomei | R-HSA-1482839, Acyl chain remodelling of PE |
SignaLinki | Q9NWW9 |
Chemistry databases
SwissLipidsi | SLP:000001075 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:17824, PLAAT2 |
MIMi | 613866, gene |
neXtProti | NX_Q9NWW9 |
VEuPathDBi | HostDB:ENSG00000133328 |
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm 1 Publication
Other locations
- Membrane Sequence analysis; Single-pass membrane protein Sequence analysis
Note: Exhibits a granular pattern in the cytoplasm with preferential perinuclear localization.1 Publication
Cytosol
- cytosol Source: Reactome
Other locations
- cytoplasm Source: GO_Central
- integral component of membrane Source: UniProtKB-KW
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 133 | CytoplasmicSequence analysisAdd BLAST | 133 | |
Transmembranei | 134 – 154 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 155 – 162 | LumenalSequence analysis | 8 |
Keywords - Cellular componenti
Cytoplasm, MembranePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 113 | C → S: Loss of N-acyltransferase activity. 1 Publication | 1 |
Organism-specific databases
DisGeNETi | 54979 |
OpenTargetsi | ENSG00000133328 |
PharmGKBi | PA29446 |
Miscellaneous databases
Pharosi | Q9NWW9, Tchem |
Chemistry databases
ChEMBLi | CHEMBL4630860 |
Genetic variation databases
BioMutai | HRASLS2 |
DMDMi | 23396611 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000152483 | 1 – 162 | Phospholipase A and acyltransferase 2Add BLAST | 162 |
Proteomic databases
MassIVEi | Q9NWW9 |
PaxDbi | Q9NWW9 |
PeptideAtlasi | Q9NWW9 |
PRIDEi | Q9NWW9 |
ProteomicsDBi | 82995 |
PTM databases
iPTMneti | Q9NWW9 |
PhosphoSitePlusi | Q9NWW9 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSG00000133328, Expressed in epithelium of bronchus and 178 other tissues |
Genevisiblei | Q9NWW9, HS |
Organism-specific databases
HPAi | ENSG00000133328, Tissue enriched (intestine) |
Interactioni
Binary interactionsi
Q9NWW9
Protein-protein interaction databases
BioGRIDi | 120315, 17 interactors |
IntActi | Q9NWW9, 6 interactors |
STRINGi | 9606.ENSP00000255695 |
Chemistry databases
BindingDBi | Q9NWW9 |
Miscellaneous databases
RNActi | Q9NWW9, protein |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 13 – 129 | LRATPROSITE-ProRule annotationAdd BLAST | 117 |
Sequence similaritiesi
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | ENOG502S0JN, Eukaryota |
GeneTreei | ENSGT00940000154853 |
HOGENOMi | CLU_109418_0_1_1 |
InParanoidi | Q9NWW9 |
OMAi | RQVQKAG |
OrthoDBi | 1602481at2759 |
PhylomeDBi | Q9NWW9 |
TreeFami | TF330836 |
Family and domain databases
DisProti | DP02737 |
InterProi | View protein in InterPro IPR007053, LRAT_dom |
Pfami | View protein in Pfam PF04970, LRAT, 1 hit |
PROSITEi | View protein in PROSITE PS51934, LRAT, 1 hit |
i Sequence
Sequence statusi: Complete.
10 20 30 40 50
MALARPRPRL GDLIEISRFG YAHWAIYVGD GYVVHLAPAS EIAGAGAASV
60 70 80 90 100
LSALTNKAIV KKELLSVVAG GDNYRVNNKH DDRYTPLPSN KIVKRAEELV
110 120 130 140 150
GQELPYSLTS DNCEHFVNHL RYGVSRSDQV TGAVTTVGVA AGLLAAASLV
160
GILLARSKRE RQ
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AB453251 mRNA Translation: BAH22445.1 AK000563 mRNA Translation: BAA91256.1 CH471076 Genomic DNA Translation: EAW74157.1 |
CCDSi | CCDS8046.1 |
RefSeqi | NP_060348.1, NM_017878.1 |
Genome annotation databases
Ensembli | ENST00000255695.2; ENSP00000255695.1; ENSG00000133328.4 |
GeneIDi | 54979 |
KEGGi | hsa:54979 |
MANE-Selecti | ENST00000255695.2; ENSP00000255695.1; NM_017878.2; NP_060348.1 |
UCSCi | uc001nxg.1, human |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AB453251 mRNA Translation: BAH22445.1 AK000563 mRNA Translation: BAA91256.1 CH471076 Genomic DNA Translation: EAW74157.1 |
CCDSi | CCDS8046.1 |
RefSeqi | NP_060348.1, NM_017878.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
4DPZ | X-ray | 1.25 | X | 1-129 | [»] | |
AlphaFoldDBi | Q9NWW9 | |||||
SMRi | Q9NWW9 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 120315, 17 interactors |
IntActi | Q9NWW9, 6 interactors |
STRINGi | 9606.ENSP00000255695 |
Chemistry databases
BindingDBi | Q9NWW9 |
ChEMBLi | CHEMBL4630860 |
SwissLipidsi | SLP:000001075 |
PTM databases
iPTMneti | Q9NWW9 |
PhosphoSitePlusi | Q9NWW9 |
Genetic variation databases
BioMutai | HRASLS2 |
DMDMi | 23396611 |
Proteomic databases
MassIVEi | Q9NWW9 |
PaxDbi | Q9NWW9 |
PeptideAtlasi | Q9NWW9 |
PRIDEi | Q9NWW9 |
ProteomicsDBi | 82995 |
Protocols and materials databases
Antibodypediai | 28975, 93 antibodies from 25 providers |
DNASUi | 54979 |
Genome annotation databases
Ensembli | ENST00000255695.2; ENSP00000255695.1; ENSG00000133328.4 |
GeneIDi | 54979 |
KEGGi | hsa:54979 |
MANE-Selecti | ENST00000255695.2; ENSP00000255695.1; NM_017878.2; NP_060348.1 |
UCSCi | uc001nxg.1, human |
Organism-specific databases
CTDi | 54979 |
DisGeNETi | 54979 |
GeneCardsi | PLAAT2 |
HGNCi | HGNC:17824, PLAAT2 |
HPAi | ENSG00000133328, Tissue enriched (intestine) |
MIMi | 613866, gene |
neXtProti | NX_Q9NWW9 |
OpenTargetsi | ENSG00000133328 |
PharmGKBi | PA29446 |
VEuPathDBi | HostDB:ENSG00000133328 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | ENOG502S0JN, Eukaryota |
GeneTreei | ENSGT00940000154853 |
HOGENOMi | CLU_109418_0_1_1 |
InParanoidi | Q9NWW9 |
OMAi | RQVQKAG |
OrthoDBi | 1602481at2759 |
PhylomeDBi | Q9NWW9 |
TreeFami | TF330836 |
Enzyme and pathway databases
BRENDAi | 2.7.1.22, 2681 |
PathwayCommonsi | Q9NWW9 |
Reactomei | R-HSA-1482839, Acyl chain remodelling of PE |
SignaLinki | Q9NWW9 |
Miscellaneous databases
BioGRID-ORCSi | 54979, 14 hits in 1068 CRISPR screens |
GenomeRNAii | 54979 |
Pharosi | Q9NWW9, Tchem |
PROi | PR:Q9NWW9 |
RNActi | Q9NWW9, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000133328, Expressed in epithelium of bronchus and 178 other tissues |
Genevisiblei | Q9NWW9, HS |
Family and domain databases
DisProti | DP02737 |
InterProi | View protein in InterPro IPR007053, LRAT_dom |
Pfami | View protein in Pfam PF04970, LRAT, 1 hit |
PROSITEi | View protein in PROSITE PS51934, LRAT, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | PLAT2_HUMAN | |
Accessioni | Q9NWW9Primary (citable) accession number: Q9NWW9 Secondary accession number(s): B9A7L8 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | September 19, 2002 |
Last sequence update: | October 1, 2000 | |
Last modified: | May 25, 2022 | |
This is version 132 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Human chromosome 11
Human chromosome 11: entries, gene names and cross-references to MIM - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families