T0MJC2 · T0MJC2_CAMFR
- ProteinPhospholipase A2
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids111 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
- 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,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-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H+This 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.
- H2O + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine = (9Z)-octadecenoate + H+ + N-hexadecanoyl-1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamineThis 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 | negative regulation of T cell proliferation | |
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
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Tylopoda > Camelidae > Camelus
Accessions
- Primary accessionT0MJC2
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Disulfide bond | 21↔37 | |||||
Sequence: CGWGGKGTPVDAIDWCC | ||||||
Disulfide bond | 36↔90 | |||||
Sequence: CCWWHDVCYAELERKGYNVLTQSYRYRVRQGLVTCELGSHCQMELCACDQKLVHC | ||||||
Disulfide bond | 43↔83 | |||||
Sequence: CYAELERKGYNVLTQSYRYRVRQGLVTCELGSHCQMELCAC | ||||||
Disulfide bond | 70↔81 | |||||
Sequence: CELGSHCQMELC |
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-111 | Phospholipase A2 | ||||
Sequence: MIEDVTGKPALESFGFYGCYCGWGGKGTPVDAIDWCCWWHDVCYAELERKGYNVLTQSYRYRVRQGLVTCELGSHCQMELCACDQKLVHCLKRNRRSYSSLYQYFPNFLCI |
Sequence similarities
Belongs to the phospholipase A2 family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length111
- Mass (Da)12,934
- Last updated2013-10-16 v1
- Checksum5E88F7258E698658
Keywords
- Technical term