Q68DD2 · PA24F_HUMAN
- ProteinCytosolic phospholipase A2 zeta
- GenePLA2G4F
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids849 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Has calcium-dependent phospholipase and lysophospholipase activities with a potential role in membrane lipid remodeling and biosynthesis of lipid mediators (PubMed:29158256).
Preferentially hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) (PubMed:29158256).
Selectively hydrolyzes sn-2 arachidonoyl group from membrane phospholipids, providing the precursor for eicosanoid biosynthesis (PubMed:29158256).
In myocardial mitochondria, plays a major role in arachidonate release that is metabolically channeled to the formation of cardioprotective eicosanoids, epoxyeicosatrienoates (EETs) (PubMed:29158256).
Preferentially hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) (PubMed:29158256).
Selectively hydrolyzes sn-2 arachidonoyl group from membrane phospholipids, providing the precursor for eicosanoid biosynthesis (PubMed:29158256).
In myocardial mitochondria, plays a major role in arachidonate release that is metabolically channeled to the formation of cardioprotective eicosanoids, epoxyeicosatrienoates (EETs) (PubMed:29158256).
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-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,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-(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-(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-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-2-O-hexadecyl-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 2-O-hexadecyl-sn-glycero-3-phosphocholine + H+This reaction proceeds in the forward direction.
- 1-O-hexadecyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-O-hexadecyl-sn-glycero-3-phosphocholine + H+This reaction proceeds in the forward direction.
- 1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H+ + hexadecanoate + sn-glycerol 3-phosphocholineThis reaction proceeds in the forward direction.
Cofactor
Activity regulation
Stimulated by cytosolic Ca2+.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 60 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 60 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 66 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 116 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 116 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 118 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 118 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 123 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 395 | Nucleophile | ||||
Sequence: S | ||||||
Active site | 680 | Proton acceptor | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | mitochondrion | |
Cellular Component | ruffle membrane | |
Cellular Component | vesicle | |
Molecular Function | calcium ion binding | |
Molecular Function | calcium-dependent phospholipase A2 activity | |
Molecular Function | calcium-dependent phospholipid binding | |
Molecular Function | lysophospholipase activity | |
Molecular Function | phospholipase A1 activity | |
Biological Process | arachidonic acid secretion | |
Biological Process | cellular response to antibiotic | |
Biological Process | cellular response to organic cyclic compound | |
Biological Process | glycerophospholipid catabolic process | |
Biological Process | phosphatidylglycerol acyl-chain remodeling | |
Biological Process | prostaglandin biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCytosolic phospholipase A2 zeta
- EC number
- Short namescPLA2-zeta
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ68DD2
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_053553 | 30 | in dbSNP:rs636604 | |||
Sequence: G → V | ||||||
Natural variant | VAR_027054 | 740 | in dbSNP:rs1356410 | |||
Sequence: M → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,118 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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000247027 | 1-849 | Cytosolic phospholipase A2 zeta | |||
Sequence: MLWALWPRWLADKMLPLLGAVLLQKREKRGPLWRHWRRETYPYYDLQVKVLRATNIRGTDLLSKADCYVQLWLPTASPSPAQTRIVANCSDPEWNETFHYQIHGAVKNVLELTLYDKDILGSDQLSLLLFDLRSLKCGQPHKHTFPLNHQDSQELQVEFVLEKSQVPASEVITNGVLVAHPCLRIQGTLRGDGTAPREEYGSRQLQLAVPGAYEKPQLLPLQPPTEPGLPPTFTFHVNPVLSSRLHVELMELLAAVQSGPSAELEAQTSKLGEGGILLSSLPLGQEEQCSVALGEGQEVALSMKVEMSSGDLDLRLGFDLSDGEQEFLDRRKQVVSKALQQVLGLSEALDSGQVPVVAVLGSGGGTRAMSSLYGSLAGLQELGLLDTVTYLSGVSGSTWCISTLYRDPAWSQVALQGPIERAQVHVCSSKMGALSTERLQYYTQELGVRERSGHSVSLIDLWGLLVEYLLYQEENPAKLSDQQEAVRQGQNPYPIYTSVNVRTNLSGEDFAEWCEFTPYEVGFPKYGAYVPTELFGSELFMGRLLQLQPEPRICYLQGMWGSAFATSLDEIFLKTAGSGLSFLEWYRGSVNITDDCQKPQLHNPSRLRTRLLTPQGPFSQAVLDIFTSRFTSAQSFNFTRGLCLHKDYVAGREFVAWKDTHPDAFPNQLTPMRDCLYLVDGGFAINSPFPLALLPQRAVDLILSFDYSLEAPFEVLKMTEKYCLDRGIPFPSIEVGPEDMEEARECYLFAKAEDPRSPIVLHFPLVNRTFRTHLAPGVERQTAEEKAFGDFVINRPDTPYGMMNFTYEPQDFYRLVALSRYNVLNNVETLKCALQLALDRHQARERAGA |
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in myocardium (at protein level).
Gene expression databases
Organism-specific databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 27-145 | C2 | ||||
Sequence: EKRGPLWRHWRRETYPYYDLQVKVLRATNIRGTDLLSKADCYVQLWLPTASPSPAQTRIVANCSDPEWNETFHYQIHGAVKNVLELTLYDKDILGSDQLSLLLFDLRSLKCGQPHKHTF | ||||||
Domain | 306-849 | PLA2c | ||||
Sequence: EMSSGDLDLRLGFDLSDGEQEFLDRRKQVVSKALQQVLGLSEALDSGQVPVVAVLGSGGGTRAMSSLYGSLAGLQELGLLDTVTYLSGVSGSTWCISTLYRDPAWSQVALQGPIERAQVHVCSSKMGALSTERLQYYTQELGVRERSGHSVSLIDLWGLLVEYLLYQEENPAKLSDQQEAVRQGQNPYPIYTSVNVRTNLSGEDFAEWCEFTPYEVGFPKYGAYVPTELFGSELFMGRLLQLQPEPRICYLQGMWGSAFATSLDEIFLKTAGSGLSFLEWYRGSVNITDDCQKPQLHNPSRLRTRLLTPQGPFSQAVLDIFTSRFTSAQSFNFTRGLCLHKDYVAGREFVAWKDTHPDAFPNQLTPMRDCLYLVDGGFAINSPFPLALLPQRAVDLILSFDYSLEAPFEVLKMTEKYCLDRGIPFPSIEVGPEDMEEARECYLFAKAEDPRSPIVLHFPLVNRTFRTHLAPGVERQTAEEKAFGDFVINRPDTPYGMMNFTYEPQDFYRLVALSRYNVLNNVETLKCALQLALDRHQARERAGA |
Domain
The N-terminal C2 domain associates with lipid membranes upon calcium binding. It modulates enzyme activity by presenting the active site to its substrate in response to elevations of cytosolic Ca2+ (By similarity).
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q68DD2-1
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
- Length849
- Mass (Da)95,082
- Last updated2011-01-11 v3
- ChecksumB2231EC3A9494598
Q68DD2-2
- Name2
Q68DD2-3
- Name3
- Differences from canonical
- 352-352: G → GQV
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 203 | in Ref. 1; BAD18801 | ||||
Sequence: R → G | ||||||
Sequence conflict | 262 | in Ref. 1; BAD18801 | ||||
Sequence: A → T | ||||||
Alternative sequence | VSP_019887 | 352 | in isoform 3 | |||
Sequence: G → GQV | ||||||
Sequence conflict | 363 | in Ref. 3; CAH18288 | ||||
Sequence: G → E | ||||||
Alternative sequence | VSP_019888 | 433-454 | in isoform 2 | |||
Sequence: ALSTERLQYYTQELGVRERSGH → DVRVSPCQLPRLHSSNLDHSLW | ||||||
Alternative sequence | VSP_019889 | 455-849 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK172836 EMBL· GenBank· DDBJ | BAD18801.1 EMBL· GenBank· DDBJ | mRNA | ||
AC036103 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CR749451 EMBL· GenBank· DDBJ | CAH18288.1 EMBL· GenBank· DDBJ | mRNA |