S9YCH0 · S9YCH0_CAMFR
- ProteinPhospholipase A2
- GeneLOC102513958
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids159 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
- 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.
Cofactor
Note: Binds 1 Ca2+ ion per subunit.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
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 | lipid catabolic process | |
Biological Process | phospholipid 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
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Tylopoda > Camelidae > Camelus
Accessions
- Primary accessionS9YCH0
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-27 | |||||
Sequence: MGPLPLCQPVGLSLLLLLGPVLWLSAA | ||||||
Chain | PRO_5042312655 | 28-159 | Phospholipase A2 | |||
Sequence: SQRSHVHRRGLIELAGTVECAGTRSSMAYVNYGCYCGLGGHGQPLDAVDWCCHHHDCCYNRAEDAGCSPKLERYSWQCVNHSIQCGPAEDKCQELMCKCDQEVASCLAQTEYNLKYLFYPSFLCGTDSPKCD | ||||||
Disulfide bond | 61↔151 | |||||
Sequence: CYCGLGGHGQPLDAVDWCCHHHDCCYNRAEDAGCSPKLERYSWQCVNHSIQCGPAEDKCQELMCKCDQEVASCLAQTEYNLKYLFYPSFLC | ||||||
Disulfide bond | 63↔79 | |||||
Sequence: CGLGGHGQPLDAVDWCC | ||||||
Disulfide bond | 78↔133 | |||||
Sequence: CCHHHDCCYNRAEDAGCSPKLERYSWQCVNHSIQCGPAEDKCQELMCKCDQEVASC | ||||||
Disulfide bond | 84↔158 | |||||
Sequence: CCYNRAEDAGCSPKLERYSWQCVNHSIQCGPAEDKCQELMCKCDQEVASCLAQTEYNLKYLFYPSFLCGTDSPKC | ||||||
Disulfide bond | 85↔126 | |||||
Sequence: CYNRAEDAGCSPKLERYSWQCVNHSIQCGPAEDKCQELMCKC | ||||||
Disulfide bond | 94↔119 | |||||
Sequence: CSPKLERYSWQCVNHSIQCGPAEDKC | ||||||
Disulfide bond | 112↔124 | |||||
Sequence: CGPAEDKCQELMC |
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 37-152 | Phospholipase A2 | ||||
Sequence: GLIELAGTVECAGTRSSMAYVNYGCYCGLGGHGQPLDAVDWCCHHHDCCYNRAEDAGCSPKLERYSWQCVNHSIQCGPAEDKCQELMCKCDQEVASCLAQTEYNLKYLFYPSFLCG |
Sequence similarities
Belongs to the phospholipase A2 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length159
- Mass (Da)17,483
- Last updated2013-10-16 v1
- ChecksumD2C4A12BD0A77E88
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KB016683 EMBL· GenBank· DDBJ | EPY85171.1 EMBL· GenBank· DDBJ | Genomic DNA |