Phospholipase A2; Phospholipase A2 releases fatty acids from the second carbon group of glycerol. Perhaps the best known members are secreted snake venoms, but also found in secreted pancreatic and membrane-associated forms. Structure is all-alpha, with two core disulfide-linked helices and a calcium-binding loop. This alignment represents the major family of PLA2s. A second minor family, defined by the honeybee venom PLA2 PDB:1POC and related sequences from Gila monsters (Heloderma), is not recognized. This minor family conserves the core helix pair but is substantially different elsewhere. The PROSITE pattern PA2_HIS, specific to the first core helix, recognizes both families.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774966  30 FWQFQRMVKHITGRSAFFSYYGYGCYCGLGGRGIPVDATDRCCWAHDCCYHKLKEYGC-QPILNAYQFAIVNGTVTCgct 108
Cdd:pfam00068   1 LWQFGEMIKCTTGRNPPLDYNDYGCYCGLGGSGTPVDATDRCCQAHDCCYERLKKLGCgNPYLLSYNYSCSDGTITC--- 77

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958774966 109 mGGGCLCGQKACECDKLSVYCFKEnlATYEKTFK 142
Cdd:pfam00068  78 -SGNSSCEKQLCECDKAAAECFAR--ATYNKKYK 108

Phospholipase A2; Phospholipase A2 releases fatty acids from the second carbon group of glycerol. Perhaps the best known members are secreted snake venoms, but also found in secreted pancreatic and membrane-associated forms. Structure is all-alpha, with two core disulfide-linked helices and a calcium-binding loop. This alignment represents the major family of PLA2s. A second minor family, defined by the honeybee venom PLA2 PDB:1POC and related sequences from Gila monsters (Heloderma), is not recognized. This minor family conserves the core helix pair but is substantially different elsewhere. The PROSITE pattern PA2_HIS, specific to the first core helix, recognizes both families.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774966  30 FWQFQRMVKHITGRSAFFSYYGYGCYCGLGGRGIPVDATDRCCWAHDCCYHKLKEYGC-QPILNAYQFAIVNGTVTCgct 108
Cdd:pfam00068   1 LWQFGEMIKCTTGRNPPLDYNDYGCYCGLGGSGTPVDATDRCCQAHDCCYERLKKLGCgNPYLLSYNYSCSDGTITC--- 77

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958774966 109 mGGGCLCGQKACECDKLSVYCFKEnlATYEKTFK 142
Cdd:pfam00068  78 -SGNSSCEKQLCECDKAAAECFAR--ATYNKKYK 108

PLA2c: Phospholipase A2, a family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. PLA2 cleaves the sn-2 position of the glycerol backbone of phospholipids (PC or phosphatidylethanolamine), usually in a metal-dependent reaction, to generate lysophospholipid (LysoPL) and a free fatty acid (FA). The resulting products are either dietary or used in synthetic pathways for leukotrienes and prostaglandins. Often, arachidonic acid is released as a free fatty acid and acts as second messenger in signaling networks. Secreted PLA2s have also been found to specifically bind to a variety of soluble and membrane proteins in mammals, including receptors. As a toxin, PLA2 is a potent presynaptic neurotoxin which blocks nerve terminals by binding to the nerve membrane and hydrolyzing stable membrane lipids. The products of the hydrolysis (LysoPL and FA) cannot form bilayers leading to a change in membrane conformation and ultimately to a block in the release of neurotransmitters. PLA2 may form dimers or oligomers.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774966  29 SFWQFQRMVKHITGRSAFfSYYGYGCYCGLGGRGIPVDATDRCCWAHDCCYHKLKEYGCQPILNAYQFAIVNGTVTCGCT 108
Cdd:cd00125     1 NLLQFGKMIKCTTGRSAL-DYNGYGCYCGLGGSGTPVDDTDRCCQVHDCCYDRAEKGGCSPYFTSYSYTCSDGQITCSDA 79

                          90       100
                  ....*....|....*....|....*.
gi 1958774966 109 MGGgclCGQKACECDKLSVYCFKENL 134
Cdd:cd00125    80 NDK---CARALCECDRAAALCFARAP 102

Phospholipase A2; Phospholipase A2 releases fatty acids from the second carbon group of glycerol. Perhaps the best known members are secreted snake venoms, but also found in secreted pancreatic and membrane-associated forms. Structure is all-alpha, with two core disulfide-linked helices and a calcium-binding loop. This alignment represents the major family of PLA2s. A second minor family, defined by the honeybee venom PLA2 PDB:1POC and related sequences from Gila monsters (Heloderma), is not recognized. This minor family conserves the core helix pair but is substantially different elsewhere. The PROSITE pattern PA2_HIS, specific to the first core helix, recognizes both families.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774966  30 FWQFQRMVKHITGRSAFFSYYGYGCYCGLGGRGIPVDATDRCCWAHDCCYHKLKEYGC-QPILNAYQFAIVNGTVTCgct 108
Cdd:pfam00068   1 LWQFGEMIKCTTGRNPPLDYNDYGCYCGLGGSGTPVDATDRCCQAHDCCYERLKKLGCgNPYLLSYNYSCSDGTITC--- 77

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958774966 109 mGGGCLCGQKACECDKLSVYCFKEnlATYEKTFK 142
Cdd:pfam00068  78 -SGNSSCEKQLCECDKAAAECFAR--ATYNKKYK 108

PLA2c: Phospholipase A2, a family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. PLA2 cleaves the sn-2 position of the glycerol backbone of phospholipids (PC or phosphatidylethanolamine), usually in a metal-dependent reaction, to generate lysophospholipid (LysoPL) and a free fatty acid (FA). The resulting products are either dietary or used in synthetic pathways for leukotrienes and prostaglandins. Often, arachidonic acid is released as a free fatty acid and acts as second messenger in signaling networks. Secreted PLA2s have also been found to specifically bind to a variety of soluble and membrane proteins in mammals, including receptors. As a toxin, PLA2 is a potent presynaptic neurotoxin which blocks nerve terminals by binding to the nerve membrane and hydrolyzing stable membrane lipids. The products of the hydrolysis (LysoPL and FA) cannot form bilayers leading to a change in membrane conformation and ultimately to a block in the release of neurotransmitters. PLA2 may form dimers or oligomers.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774966  29 SFWQFQRMVKHITGRSAFfSYYGYGCYCGLGGRGIPVDATDRCCWAHDCCYHKLKEYGCQPILNAYQFAIVNGTVTCGCT 108
Cdd:cd00125     1 NLLQFGKMIKCTTGRSAL-DYNGYGCYCGLGGSGTPVDDTDRCCQVHDCCYDRAEKGGCSPYFTSYSYTCSDGQITCSDA 79

                          90       100
                  ....*....|....*....|....*.
gi 1958774966 109 MGGgclCGQKACECDKLSVYCFKENL 134
Cdd:cd00125    80 NDK---CARALCECDRAAALCFARAP 102

otoconin_90: Phospholipase A2-like domains present in otoconin-90 and otoconin-95, mammal proteins that are principal matrix proteins of calcitic otoconia. Interactions involving otoconin-90 may trigger or constitute key events in otoconia formation. The PLA2-like domains in otoconins may have lost their metal-binding sites.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958774966  61 RGIPVDATDRCCWAHDCCYHKLKEYGCQpilnayQFAIVNGTVTCGCTM---GGGCLCGQKACECDKLSVYCF 130
Cdd:cd04707    29 EGLPVDELDRCCFQHRCCLEQASEMGCL------QDRKLSTEVTCVDHKpkcEGVSVCEKLLCTCDKTAAECM 95