A0A3B3IRX2 · A0A3B3IRX2_HUMAN
- ProteinPhospholipase A2
- GenePLA2G2A
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids117 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
Catalytic activity
- 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-(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.
- 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-(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-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-octadecenoyl)-sn-glycero-3-phosphoglycerol + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphoglycerol + H+This reaction proceeds in the forward direction.
- a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + H2O = a 1-acyl-sn-glycero-3-phosphoethanolamine + a fatty acid + H+This reaction proceeds in the forward direction.
Cofactor
Note: Binds 1 Ca2+ ion per subunit.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | mitochondrial outer membrane | |
Molecular Function | calcium ion binding | |
Molecular Function | phospholipase A2 activity | |
Biological Process | arachidonic acid secretion | |
Biological Process | defense response to bacterium | |
Biological Process | killing of cells of another organism | |
Biological Process | lipid catabolic process | |
Biological Process | phosphatidylcholine metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhospholipase A2
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionA0A3B3IRX2
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Mitochondrion outer membrane ; Peripheral membrane protein
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 99 variants from UniProt as well as other sources including ClinVar and dbSNP.
Genetic variation databases
PTM/Processing
Features
Showing features for disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Disulfide bond | 19↔110 | |||||
Sequence: CHCGVGGRGSPKDATDRCCVTHDCCYKRLEKRGCGTKFLSYKFSNSGSRITCAKQDSCRSQLCECDKAAATCFARNKTTYNKKYQYYSNKHC | ||||||
Disulfide bond | 21↔37 | |||||
Sequence: CGVGGRGSPKDATDRCC | ||||||
Disulfide bond | 36↔90 | |||||
Sequence: CCVTHDCCYKRLEKRGCGTKFLSYKFSNSGSRITCAKQDSCRSQLCECDKAAATC | ||||||
Disulfide bond | 42↔117 | |||||
Sequence: CCYKRLEKRGCGTKFLSYKFSNSGSRITCAKQDSCRSQLCECDKAAATCFARNKTTYNKKYQYYSNKHCRGSTPRC | ||||||
Disulfide bond | 43↔83 | |||||
Sequence: CYKRLEKRGCGTKFLSYKFSNSGSRITCAKQDSCRSQLCEC | ||||||
Disulfide bond | 52↔76 | |||||
Sequence: CGTKFLSYKFSNSGSRITCAKQDSC | ||||||
Disulfide bond | 70↔81 | |||||
Sequence: CAKQDSCRSQLC |
Keywords
- PTM
Proteomic databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-111 | Phospholipase A2 | ||||
Sequence: MIKLTTGKEAALSYGFYGCHCGVGGRGSPKDATDRCCVTHDCCYKRLEKRGCGTKFLSYKFSNSGSRITCAKQDSCRSQLCECDKAAATCFARNKTTYNKKYQYYSNKHCR |
Sequence similarities
Belongs to the phospholipase A2 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length117
- Mass (Da)13,037
- Last updated2018-12-05 v1
- Checksum4014EF0446E2EF35
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
P14555 | PA2GA_HUMAN | PLA2G2A | 144 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL358253 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |