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Conserved domains on  [gi|1344169088|ref|NP_001347798|]
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group IIF secretory phospholipase A2 isoform 2 precursor [Homo sapiens]

Protein Classification

phospholipase A2 family protein( domain architecture ID 10062756)

phospholipase A2 (PLA2) family protein such as PLA2 that catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLA2c cd00125
PLA2c: Phospholipase A2, a family of secretory and cytosolic enzymes; the latter are either Ca ...
 21-138 1.79e-32

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.


:

Pssm-ID: 153091  Cd Length: 115  Bit Score: 111.96  E-value: 1.79e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344169088  21 SLLNLKAMVEAVTGRSAiLSFVGYGCYCGLGGRGQPKDEVDWCCHAHDCCYQELFDQGCHPYVDHYDHTIENNTeIVCSD 100
Cdd:cd00125     1 NLLQFGKMIKCTTGRSA-LDYNGYGCYCGLGGSGTPVDDTDRCCQVHDCCYDRAEKGGCSPYFTSYSYTCSDGQ-ITCSD 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1344169088 101 LNkTECDKQTCMCDKNMVLCLMNQTYREEYRGFLNVYC 138
Cdd:cd00125    79 AN-DKCARALCECDRAAALCFARAPYNPKYRNYDKKRC 115
 
Name Accession Description Interval E-value
PLA2c cd00125
PLA2c: Phospholipase A2, a family of secretory and cytosolic enzymes; the latter are either Ca ...
 21-138 1.79e-32

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.


Pssm-ID: 153091  Cd Length: 115  Bit Score: 111.96  E-value: 1.79e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344169088  21 SLLNLKAMVEAVTGRSAiLSFVGYGCYCGLGGRGQPKDEVDWCCHAHDCCYQELFDQGCHPYVDHYDHTIENNTeIVCSD 100
Cdd:cd00125     1 NLLQFGKMIKCTTGRSA-LDYNGYGCYCGLGGSGTPVDDTDRCCQVHDCCYDRAEKGGCSPYFTSYSYTCSDGQ-ITCSD 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1344169088 101 LNkTECDKQTCMCDKNMVLCLMNQTYREEYRGFLNVYC 138
Cdd:cd00125    79 AN-DKCARALCECDRAAALCFARAPYNPKYRNYDKKRC 115
Phospholip_A2_1 pfam00068
Phospholipase A2; Phospholipase A2 releases fatty acids from the second carbon group of ...
 22-131 6.02e-31

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.


Pssm-ID: 459659  Cd Length: 108  Bit Score: 107.69  E-value: 6.02e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344169088  22 LLNLKAMVEAVTGRSAILSFVGYGCYCGLGGRGQPKDEVDWCCHAHDCCYQELFDQGC-HPYVDHYDHTIENNTeIVCSd 100
Cdd:pfam00068   1 LWQFGEMIKCTTGRNPPLDYNDYGCYCGLGGSGTPVDATDRCCQAHDCCYERLKKLGCgNPYLLSYNYSCSDGT-ITCS- 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1344169088 101 lNKTECDKQTCMCDKNMVLCLMNQTYREEYR 131
Cdd:pfam00068  79 -GNSSCEKQLCECDKAAAECFARATYNKKYK 108
PA2c smart00085
Phospholipase A2;
21-133 1.28e-19

Phospholipase A2;


Pssm-ID: 214508  Cd Length: 117  Bit Score: 79.17  E-value: 1.28e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344169088   21 SLLNLKAMVEAVTGRSAILSFVGYGCYCGLGGRGQPKDEVDWCCHAHDCCYQELFDQGCHPYVDHYDHTIENNTeIVCSD 100
Cdd:smart00085   1 NLWQFGNMIQCATGKRAWLSYGDYGCYCGWGGSGTPVDATDRCCFVHDCCYGKAEKEGCNPKTTTYSYSCDNGF-ITCGG 79

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1344169088  101 lNKTECDKQTCMCDKNMVLCLMNQTYREEYRGF 133
Cdd:smart00085  80 -KNTACLVFVCECDRAAAICFAKNPYNKKNYNI 111
 
Name Accession Description Interval E-value
PLA2c cd00125
PLA2c: Phospholipase A2, a family of secretory and cytosolic enzymes; the latter are either Ca ...
 21-138 1.79e-32

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.


Pssm-ID: 153091  Cd Length: 115  Bit Score: 111.96  E-value: 1.79e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344169088  21 SLLNLKAMVEAVTGRSAiLSFVGYGCYCGLGGRGQPKDEVDWCCHAHDCCYQELFDQGCHPYVDHYDHTIENNTeIVCSD 100
Cdd:cd00125     1 NLLQFGKMIKCTTGRSA-LDYNGYGCYCGLGGSGTPVDDTDRCCQVHDCCYDRAEKGGCSPYFTSYSYTCSDGQ-ITCSD 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1344169088 101 LNkTECDKQTCMCDKNMVLCLMNQTYREEYRGFLNVYC 138
Cdd:cd00125    79 AN-DKCARALCECDRAAALCFARAPYNPKYRNYDKKRC 115
Phospholip_A2_1 pfam00068
Phospholipase A2; Phospholipase A2 releases fatty acids from the second carbon group of ...
 22-131 6.02e-31

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.


Pssm-ID: 459659  Cd Length: 108  Bit Score: 107.69  E-value: 6.02e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344169088  22 LLNLKAMVEAVTGRSAILSFVGYGCYCGLGGRGQPKDEVDWCCHAHDCCYQELFDQGC-HPYVDHYDHTIENNTeIVCSd 100
Cdd:pfam00068   1 LWQFGEMIKCTTGRNPPLDYNDYGCYCGLGGSGTPVDATDRCCQAHDCCYERLKKLGCgNPYLLSYNYSCSDGT-ITCS- 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1344169088 101 lNKTECDKQTCMCDKNMVLCLMNQTYREEYR 131
Cdd:pfam00068  79 -GNSSCEKQLCECDKAAAECFARATYNKKYK 108
PA2c smart00085
Phospholipase A2;
21-133 1.28e-19

Phospholipase A2;


Pssm-ID: 214508  Cd Length: 117  Bit Score: 79.17  E-value: 1.28e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344169088   21 SLLNLKAMVEAVTGRSAILSFVGYGCYCGLGGRGQPKDEVDWCCHAHDCCYQELFDQGCHPYVDHYDHTIENNTeIVCSD 100
Cdd:smart00085   1 NLWQFGNMIQCATGKRAWLSYGDYGCYCGWGGSGTPVDATDRCCFVHDCCYGKAEKEGCNPKTTTYSYSCDNGF-ITCGG 79

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1344169088  101 lNKTECDKQTCMCDKNMVLCLMNQTYREEYRGF 133
Cdd:smart00085  80 -KNTACLVFVCECDRAAAICFAKNPYNKKNYNI 111
PLA2_like cd00618
PLA2_like: Phospholipase A2, a super-family of secretory and cytosolic enzymes; the latter are ...
 54-123 7.20e-15

PLA2_like: Phospholipase A2, a super-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.


Pssm-ID: 153092  Cd Length: 83  Bit Score: 66.05  E-value: 7.20e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344169088  54 GQPKDEVDWCCHAHDCCYQELFDQGCHPYVDHYDHtienNTEIVCSDLNKTECDKQTCMCDKNMVLCLMN 123
Cdd:cd00618    17 GQPVDETDRCCRKHDCCYDQISDGGCCDGCLSYSF----SEGGVTCLTNSDLCTRSHCDCDRRLAICLAR 82
otoconin_90 cd04707
otoconin_90: Phospholipase A2-like domains present in otoconin-90 and otoconin-95, mammal ...
 50-143 1.60e-07

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.


Pssm-ID: 153096  Cd Length: 117  Bit Score: 47.47  E-value: 1.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1344169088  50 LGGRGQPKDEVDWCCHAHDCCYQELFDQGChpyvdHYDHTIenNTEIVCSD-----LNKTECDKQTCMCDKNMVLCLMNQ 124
Cdd:cd04707    26 QEGEGLPVDELDRCCFQHRCCLEQASEMGC-----LQDRKL--STEVTCVDhkpkcEGVSVCEKLLCTCDKTAAECMAAA 98

                          90
                  ....*....|....*....
gi 1344169088 125 TYREEYRGFLNVYCQGPTP 143
Cdd:cd04707    99 HFNSSLNSLDVSSCPGQVP 117
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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