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group IIF secretory phospholipase A2; GIIF sPLA2; sPLA2-IIF; phosphatidylcholine 2-acylhydrolase 2F (PLA2G2F)
Function:
- catalyzes Ca+2-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides
- hydrolyzes phosphatidylglycerol versus phosphatidylcholine with a 15-fold preference
Cofactor: binds 1 Ca+2 per subunit
Structure: belongs to the phospholipase A2 family
Compartment: secreted
Alternative splicing: named isoforms=2
Expression:
- expressed at high levels in placenta, testis, thymus
- expressed at lower levels in heart, kidney, liver & prostate
General
Ca+2 binding protein
glycoprotein
phospholipase A2; phosphatidylcholine 2-acylhydrolase (PLA2)
secreted protein
Properties
SIZE: entity length = 168 aa
MW = 19 kD
COMPARTMENT: extracellular compartment
MOTIF: signal sequence {1-20}
cysteine residue {C46}
MODIFICATION: cysteine residue {C138}
Ca+2-binding site
SITE: 47-47
cysteine residue {C48}
MODIFICATION: cysteine residue {C64}
Ca+2-binding site
SITE: 49-49
Ca+2-binding site
SITE: 51-51
cysteine residue {C63}
MODIFICATION: cysteine residue {C120}
cysteine residue {C64}
MODIFICATION: cysteine residue {C48}
histidine residue {H67}
Ca+2-binding site
SITE: 68-68
cysteine residue {C69}
MODIFICATION: cysteine residue {C145}
cysteine residue {C70}
MODIFICATION: cysteine residue {C113}
cysteine residue {C79}
MODIFICATION: cysteine residue {C106}
N-glycosylation site {N92}
cysteine residue {C98}
MODIFICATION: cysteine residue {C111}
N-glycosylation site {N102}
cysteine residue {C106}
MODIFICATION: cysteine residue {C79}
cysteine residue {C111}
MODIFICATION: cysteine residue {C98}
cysteine residue {C113}
MODIFICATION: cysteine residue {C70}
aspartate residue {D114}
cysteine residue {C120}
MODIFICATION: cysteine residue {C63}
N-glycosylation site {N123}
cysteine residue {C138}
MODIFICATION: cysteine residue {C46}
N-glycosylation site {N144}
cysteine residue {C145}
MODIFICATION: cysteine residue {C69}
Database Correlations
UniProt Q9BZM2
Pfam PF00068
Entrez Gene 64600
Kegg hsa:64600
ENZYME 3.1.1.4
References
UniProt :accession Q9BZM2