Search by BoMiProt ID - Bomi5007


Primary Information

BoMiProt ID Bomi5007
Protein Name Cytosolic phospholipase A2(cPLA2)/Phospholipase A2 group IVA/
Organism Bos taurus
Uniprot IdA4IFJ5
Milk FractionWhey,MFGM
Aminoacid Length 749
Molecular Weight 85350
Fasta Sequence https://www.uniprot.org/uniprot/A4IFJ5.fasta
Gene Name PLA2G4A/CPLA2/ PLA2G4
Gene Id 525072
Protein Existence Status reviewed

Secondary Information

Protein Function   a key enzyme in the regulation of prostaglandin and leukotriene biosynthetic pathways,
Biochemical Properties calcium-dependent phospholipase, which catalyzes the release of free fatty acids from the sn-2 position of membrane glycerophospholipids.
PTMs formation of an isopeptide bond by Transglutaminases (TG)
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
Predicted Disorder Regions 431-461
DisProt Annotation
TM Helix Prediction No TM helices
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.
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.