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Primary Information | |
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| BoMiProt ID | Bomi7995 |
| Protein Name | Phospholipase A2 |
| Organism | Bos taurus |
| Uniprot ID | P00593 |
| Milk Fraction | Whey,MFGM |
| Ref Sequence ID | NP_777071.2 |
| Aminoacid Length | 145 |
| Molecular Weight | 16002 |
| FASTA Sequence | Download |
| Gene Name | PLA2G1B |
| Gene ID | 282457 |
| Protein Existence Status | reviewed |
Secondary Information | |
| Presence in other biological fluids/tissue/cells | Keratinocytes |
| Protein Function | Secretory calcium-dependent phospholipase A2 that primarily targets dietary phospholipids in the intestinal tract. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols. |
| Biochemical Properties | Binds 1 Ca2+ ion per subunit.molecular weight of 13 782 and consists of a single polypeptide chain of 123 amino acids cross-linked by seven disulfide bridges. asparagine at position 6 in the bovine phospholipase A, |
| Significance in milk | Affects inflammatory responses in bovine mammary epithelial cells |
| PTMs | Autocatalytic cleavage, Disulfide bond, Pyrrolidone carboxylic acid, Proteolytic cleavage |
| Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | NA |
| SCOP | Class : All alpha proteins Fold : Phospholipase A2, PLA2 Superfamily : Phospholipase A2, PLA2 Family : Vertebrate phospholipase A2 Domain Name : 1G4I A:1-123 |
| CATH | Matched CATH superfamily 1.20.90.10 |
| Predicted Disorder Regions | NA |
| DisProt Annotation | |
| TM Helix Prediction | No TM helices |
| Significance of PTMs | Activated by trypsin cleavage in the duodenum. Can also be activated by thrombin or autocatalytically. |
| PDB ID | 1BP2,1BPQ,1BVM,1C74,1CEH,1FDK,1G4I,1GH4,1IRB,1KVW,1KVX,1KVY,1MKS,1MKT,1MKU,1MKV,1O2E,1O3W,1UNE,1VKQ,1VL9,2B96,2BAX,2BCH,2BD1,2BP2,2BPP,2ZP3,2ZP4,2ZP5,3BP2,4BP2, |
| Bibliography | Fleer EA, Verheij HM, De Haas GH. The primary structure of bovine pancreatic phospholipase A2. Eur J Biochem. 1978 Jan 2;82(1):261-9. doi: 10.1111/j.1432-1033.1978.tb12019.x. PMID: 620674. |