Q9QUL3 · PA2GE_MOUSE
- ProteinGroup IIE secretory phospholipase A2
- GenePla2g2e
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids142 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids (PubMed:10531313, PubMed:11922621).
Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity), releasing various unsaturated fatty acids including oleoate, linoleoate, arachidonate, docosahexaenoate and lysophosphatidylethanolamines in preference to lysophosphatidylcholines (By similarity).
In response to high-fat diet, hydrolyzes minor lipoprotein phospholipids including phosphatidylserines, phosphatidylinositols and phosphatidylglycerols, altering lipoprotein composition and fat storage in adipose tissue and liver (PubMed:24910243).
May act in an autocrine and paracrine manner (By similarity).
Contributes to lipid remodeling of cellular membranes and generation of lipid mediators involved in pathogen clearance. Cleaves sn-2 fatty acyl chains of phosphatidylglycerols and phosphatidylethanolamines, which are major components of membrane phospholipids in bacteria (By similarity).
Acts as a hair follicle phospholipase A2. Selectively releases lysophosphatidylethanolamines (LPE) and various unsaturated fatty acids in skin to regulate hair follicle homeostasis (PubMed:27226633).
May regulate the inflammatory response by releasing arachidonate, a precursor of prostaglandins and leukotrienes. Upon allergen exposure, may participate in allergic inflammatory response by enhancing leukotriene C4 synthesis and degranulation in mast cells (PubMed:11922621).
Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity), releasing various unsaturated fatty acids including oleoate, linoleoate, arachidonate, docosahexaenoate and lysophosphatidylethanolamines in preference to lysophosphatidylcholines (By similarity).
In response to high-fat diet, hydrolyzes minor lipoprotein phospholipids including phosphatidylserines, phosphatidylinositols and phosphatidylglycerols, altering lipoprotein composition and fat storage in adipose tissue and liver (PubMed:24910243).
May act in an autocrine and paracrine manner (By similarity).
Contributes to lipid remodeling of cellular membranes and generation of lipid mediators involved in pathogen clearance. Cleaves sn-2 fatty acyl chains of phosphatidylglycerols and phosphatidylethanolamines, which are major components of membrane phospholipids in bacteria (By similarity).
Acts as a hair follicle phospholipase A2. Selectively releases lysophosphatidylethanolamines (LPE) and various unsaturated fatty acids in skin to regulate hair follicle homeostasis (PubMed:27226633).
May regulate the inflammatory response by releasing arachidonate, a precursor of prostaglandins and leukotrienes. Upon allergen exposure, may participate in allergic inflammatory response by enhancing leukotriene C4 synthesis and degranulation in mast cells (PubMed:11922621).
Catalytic activity
- a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + H2O = a 1-acyl-sn-glycero-3-phosphoethanolamine + a fatty acid + H+
- 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O = (9Z)-octadecenoate + 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 = (9Z,12Z)-octadecadienoate + 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 = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H+This reaction proceeds in the forward direction.
- 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O = 1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H+ + hexadecanoateThis reaction proceeds in the forward direction.
- 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphoglycerol + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphoglycerol + 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-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-(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-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphocholine + H2O = (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H+This reaction proceeds in the forward direction.
Cofactor
Note: Binds 2 Ca2+ ions per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 41 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 43 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 45 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 45 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 47 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 47 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 49 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 49 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Active site | 65 | |||||
Sequence: H | ||||||
Binding site | 66 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 66 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 109 | |||||
Sequence: D | ||||||
Binding site | 130 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 132 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | extracellular region | |
Molecular Function | calcium ion binding | |
Molecular Function | calcium-dependent phospholipase A2 activity | |
Molecular Function | phospholipid binding | |
Biological Process | arachidonic acid secretion | |
Biological Process | inflammatory response | |
Biological Process | lipid catabolic process | |
Biological Process | low-density lipoprotein particle remodeling | |
Biological Process | negative regulation of T cell proliferation | |
Biological Process | phosphatidylcholine metabolic process | |
Biological Process | phosphatidylglycerol metabolic process | |
Biological Process | phospholipid metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGroup IIE secretory phospholipase A2
- EC number
- Short namesGIIE sPLA2; sPLA2-IIE
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9QUL3
Proteomes
Organism-specific databases
Phenotypes & Variants
Disruption phenotype
Mutant mice show abnormal hair follicle ultrastructure characterized by defects in the companion layer, the inner root sheath (IRS) and hair shaft. Mutant IRS cells have large cytoplasmic cysts and pyknotic nuclei and are devoid of keratohyalin granules, whereas the cuticle is abnormally dissociated from the hair cortex and medulla, indicative of impaired hair follicle development (PubMed:27226633).
Mutant mice are protected from obesity and hyperlipidemia in response to high-fat diet (PubMed:24910243).
Mutant mice are protected from obesity and hyperlipidemia in response to high-fat diet (PubMed:24910243).
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 6 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MKPPIALACLCLLVPLAGG | ||||||
Chain | PRO_0000022758 | 20-142 | Group IIE secretory phospholipase A2 | |||
Sequence: NLVQFGVMIERMTGKPALQYNDYGCYCGVGGSHWPVDETDWCCHAHDCCYGRLEKLGCDPKLEKYLFSITRDNIFCAGRTACQRHTCECDKRAALCFRHNLNTYNRKYAHYPNKLCTGPTPPC | ||||||
Disulfide bond | 44↔135 | |||||
Sequence: CYCGVGGSHWPVDETDWCCHAHDCCYGRLEKLGCDPKLEKYLFSITRDNIFCAGRTACQRHTCECDKRAALCFRHNLNTYNRKYAHYPNKLC | ||||||
Disulfide bond | 46↔62 | |||||
Sequence: CGVGGSHWPVDETDWCC | ||||||
Disulfide bond | 61↔115 | |||||
Sequence: CCHAHDCCYGRLEKLGCDPKLEKYLFSITRDNIFCAGRTACQRHTCECDKRAALC | ||||||
Disulfide bond | 67↔142 | |||||
Sequence: CCYGRLEKLGCDPKLEKYLFSITRDNIFCAGRTACQRHTCECDKRAALCFRHNLNTYNRKYAHYPNKLCTGPTPPC | ||||||
Disulfide bond | 68↔108 | |||||
Sequence: CYGRLEKLGCDPKLEKYLFSITRDNIFCAGRTACQRHTCEC | ||||||
Disulfide bond | 77↔101 | |||||
Sequence: CDPKLEKYLFSITRDNIFCAGRTAC | ||||||
Disulfide bond | 95↔106 | |||||
Sequence: CAGRTACQRHTC |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in skin and uterus, and at lower levels in various other tissues (PubMed:10531313, PubMed:10681567, PubMed:11922621, PubMed:27226633).
Expressed in hair follicles, specifically localized in companion cells of the outer root sheath and cuticular cells of the inner root sheath in hair follicles during anagen (PubMed:27226633).
Expressed in white and brown adipose tissue (PubMed:24910243).
Expressed in hair follicles, specifically localized in companion cells of the outer root sheath and cuticular cells of the inner root sheath in hair follicles during anagen (PubMed:27226633).
Expressed in white and brown adipose tissue (PubMed:24910243).
Induction
Up-regulated in thymus, small intestine, brain, heart, testis, kidney and lung upon endotoxin challenge (PubMed:10681567, PubMed:11922621).
Detected in alveolar macrophage-like cells upon endotoxin challenge (PubMed:10681567).
Up-regulated in white and brown adipocytes upon high-fat diet (PubMed:24910243).
Up-regulated in ear epidermis in response to topical dermatitis agent 2,4-dinitrobenzene (DNFB) (PubMed:11922621).
Detected in alveolar macrophage-like cells upon endotoxin challenge (PubMed:10681567).
Up-regulated in white and brown adipocytes upon high-fat diet (PubMed:24910243).
Up-regulated in ear epidermis in response to topical dermatitis agent 2,4-dinitrobenzene (DNFB) (PubMed:11922621).
Developmental stage
Expressed abundantly in hair follicles during the anagen phase. Low expression is observed before birth, then follows hair cycle progression: up-regulated markedly during P5-P15 (anagen phase), declining to nearly the basal level during P20-P25 (catagen and telogen) and then increasing again at P30 (next anagen).
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length142
- Mass (Da)15,943
- Last updated2000-05-01 v1
- Checksum8B0E3CC710A1F946
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A2APQ4 | A2APQ4_MOUSE | Pla2g2e | 80 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF166098 EMBL· GenBank· DDBJ | AAF04499.1 EMBL· GenBank· DDBJ | mRNA | ||
AF112984 EMBL· GenBank· DDBJ | AAF22290.1 EMBL· GenBank· DDBJ | mRNA | ||
BC027524 EMBL· GenBank· DDBJ | AAH27524.1 EMBL· GenBank· DDBJ | mRNA |