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group 10 secretory phospholipase A2; group X secretory phospholipase A2; GX sPLA2; sPLA2-X; phosphatidylcholine 2-acylhydrolase 10 (PLA2G10)
Function:
- PA2 catalyzes Ca+2-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides
- facilitates releae of arachidonic acid from cell membrane phospholipids
- prefers phosphatidylethanolamine & phosphatidylcholine liposomes to those of phosphatidylserine
phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Cofactor: binds 1 Ca+2 per subunit
Structure: belongs to the phospholipase A2 family
Compartment: secreted
Expression:
- found in spleen, thymus, peripheral blood leukocytes, pancreas, lung, & colon
General
Ca+2 binding protein
glycoprotein
phospholipase A2; phosphatidylcholine 2-acylhydrolase (PLA2)
secreted protein
Properties
SIZE: entity length = 165 aa
MW = 18 kD
COMPARTMENT: extracellular compartment
MOTIF: signal sequence {1-31}
cysteine residue {C53}
MODIFICATION: cysteine residue {C111}
cysteine residue {C67}
MODIFICATION: cysteine residue {C157}
Ca+2-binding site
SITE: 68-68
cysteine residue {C69}
MODIFICATION: cysteine residue {C85}
Ca+2-binding site
SITE: 70-70
Ca+2-binding site
SITE: 72-72
cysteine residue {C84}
MODIFICATION: cysteine residue {C139}
cysteine residue {C85}
MODIFICATION: cysteine residue {C69}
histidine residue {H88}
Ca+2-binding site
SITE: 89-89
cysteine residue {C90}
MODIFICATION: cysteine residue {C164}
cysteine residue {C91}
MODIFICATION: cysteine residue {C132}
cysteine residue {C100}
MODIFICATION: cysteine residue {C125}
cysteine residue {C111}
MODIFICATION: cysteine residue {C53}
N-glycosylation site {N113}
cysteine residue {C118}
MODIFICATION: cysteine residue {C130}
cysteine residue {C125}
MODIFICATION: cysteine residue {C100}
cysteine residue {C130}
MODIFICATION: cysteine residue {C118}
cysteine residue {C132}
MODIFICATION: cysteine residue {C91}
aspartate residue {D133}
cysteine residue {C139}
MODIFICATION: cysteine residue {C84}
cysteine residue {C157}
MODIFICATION: cysteine residue {C67}
cysteine residue {C164}
MODIFICATION: cysteine residue {C90}
Database Correlations
OMIM 603603
UniProt O15496
Pfam PF00068
Entrez Gene 8399
Kegg hsa:8399
ENZYME 3.1.1.4
References
UniProt :accession O15496