Primary Information |
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BoMiProt ID | Bomi5007 |
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Protein Name | Cytosolic phospholipase A2(cPLA2)/Phospholipase A2 group IVA/ |
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Organism | Bos taurus |
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Uniprot ID | A4IFJ5 |
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Milk Fraction | Whey,MFGM |
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Aminoacid Length | 749 |
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Molecular Weight | 85350 |
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FASTA Sequence |
Download |
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Gene Name | PLA2G4A/CPLA2/ PLA2G4 |
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Gene ID | 525072 |
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Protein Existence Status | reviewed |
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Secondary Information |
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Protein Function | a key enzyme in the regulation of prostaglandin and leukotriene biosynthetic pathways, |
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Biochemical Properties | calcium-dependent phospholipase, which catalyzes the release of free fatty acids from the sn-2 position of membrane glycerophospholipids. |
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PTMs | formation of an isopeptide bond by Transglutaminases (TG) |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|A4IFJ5|PA24A_BOVIN Cytosolic phospholipase A2 OS=Bos taurus OX=9913 GN=PLA2G4A PE=1 SV=1
MS*2FIDPYQHIIVEHHYSHKFTVVVLRATKVTKGTFGDMLDTPDPYVELFISSTPDSRKRT
RHFNNDINPVWNETFEFILDPNQENILEITLMDANYVMDETLGTTTFPISSMKVGEKKQV
PFIFNQVTEMILEMSLEVCSSPDLRFSMALCDQEKAFRQQRKENIKENMKKLLGPKNSEG
LHSTRDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYIAGLSGSTWYMSTLYSH
PDFPEKGPEEINKELMKNVSHNPLLLLT*268PQKIKRYVESLWRKKSSGQPVTFTDIFGMLIG
ETLIHNRMNTTLSSLKEKVNTGQCPLPLFTCLHVKPDVSELMFADWVEFSPFEIGMAKYG
TFMAPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSILFNRVLGVSGSQSKGSTMEEE
LENITAKHIVSNDS*434S*435DS*437DDESQGPKGTEHEEAEREYQNDNQASWVQRMLMALVSDSALFN
TREGRAGKVHNFMLGLNLNTSYPMS*505PLRDFTMQES*515LDEDELDAAVADPDEFEQIYEPLDV
KSKKIHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWAKMN
KLPFPKIDPYVFDREGLKECYVFKPKNPDVEKDCPTIIHFVLANINFRKYKAPGVPRETN
EEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMYFNTLNNIDVIKNAIVESIEYRR
QNPSRCS*727VS*729LSSVEARRFFNKEFLSKPTA
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Predicted Disorder Regions | 431-461 |
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DisProt Annotation | |
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TM Helix Prediction | No TM helices |
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Significance of PTMs | Transglutaminases (TG) catalyzes post-translational modification of PLA2 which dramatically increases the activity of this enzyme.Results in intramolecular covalent cross-linking of PLA2 by cross-linking a specific glutamine and a lysine residue between two proteins or with in same protein. |
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Bibliography | Cordella-Miele E, Miele L, Mukherjee AB. A novel transglutaminase-mediated post-translational modification of phospholipase A2 dramatically increases its catalytic activity. J Biol Chem. 1990 Oct 5;265(28):17180-8. PMID: 1976627. |