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Conserved domains on  [gi|767905576|ref|XP_011540258|]
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group IIF secretory phospholipase A2 isoform X2 [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 ...
 64-181 7.99e-33

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: 114.27  E-value: 7.99e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905576  64 SLLNLKAMVEAVTGRSAiLSFVGYGCYCGLGGRGQPKDEVDWCCHAHDCCYQELFDQGCHPYVDHYDHTIENNTeIVCSD 143
Cdd:cd00125    1 NLLQFGKMIKCTTGRSA-LDYNGYGCYCGLGGSGTPVDDTDRCCQVHDCCYDRAEKGGCSPYFTSYSYTCSDGQ-ITCSD 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767905576 144 LNkTECDKQTCMCDKNMVLCLMNQTYREEYRGFLNVYC 181
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 ...
 64-181 7.99e-33

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: 114.27  E-value: 7.99e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905576  64 SLLNLKAMVEAVTGRSAiLSFVGYGCYCGLGGRGQPKDEVDWCCHAHDCCYQELFDQGCHPYVDHYDHTIENNTeIVCSD 143
Cdd:cd00125    1 NLLQFGKMIKCTTGRSA-LDYNGYGCYCGLGGSGTPVDDTDRCCQVHDCCYDRAEKGGCSPYFTSYSYTCSDGQ-ITCSD 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767905576 144 LNkTECDKQTCMCDKNMVLCLMNQTYREEYRGFLNVYC 181
Cdd:cd00125   79 AN-DKCARALCECDRAAALCFARAPYNPKYRNYDKKRC 115
Phospholip_A2_1 pfam00068
Phospholipase A2; Phospholipase A2 releases fatty acids from the second carbon group of ...
 65-174 3.44e-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: 110.00  E-value: 3.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905576   65 LLNLKAMVEAVTGRSAILSFVGYGCYCGLGGRGQPKDEVDWCCHAHDCCYQELFDQGC-HPYVDHYDHTIENNTeIVCSd 143
Cdd:pfam00068   1 LWQFGEMIKCTTGRNPPLDYNDYGCYCGLGGSGTPVDATDRCCQAHDCCYERLKKLGCgNPYLLSYNYSCSDGT-ITCS- 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 767905576  144 lNKTECDKQTCMCDKNMVLCLMNQTYREEYR 174
Cdd:pfam00068  79 -GNSSCEKQLCECDKAAAECFARATYNKKYK 108
PA2c smart00085
Phospholipase A2;
64-176 1.11e-19

Phospholipase A2;


Pssm-ID: 214508  Cd Length: 117  Bit Score: 80.33  E-value: 1.11e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905576    64 SLLNLKAMVEAVTGRSAILSFVGYGCYCGLGGRGQPKDEVDWCCHAHDCCYQELFDQGCHPYVDHYDHTIENNTeIVCSD 143
Cdd:smart00085   1 NLWQFGNMIQCATGKRAWLSYGDYGCYCGWGGSGTPVDATDRCCFVHDCCYGKAEKEGCNPKTTTYSYSCDNGF-ITCGG 79

                           90       100       110
                   ....*....|....*....|....*....|...
gi 767905576   144 lNKTECDKQTCMCDKNMVLCLMNQTYREEYRGF 176
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 ...
 64-181 7.99e-33

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: 114.27  E-value: 7.99e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905576  64 SLLNLKAMVEAVTGRSAiLSFVGYGCYCGLGGRGQPKDEVDWCCHAHDCCYQELFDQGCHPYVDHYDHTIENNTeIVCSD 143
Cdd:cd00125    1 NLLQFGKMIKCTTGRSA-LDYNGYGCYCGLGGSGTPVDDTDRCCQVHDCCYDRAEKGGCSPYFTSYSYTCSDGQ-ITCSD 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767905576 144 LNkTECDKQTCMCDKNMVLCLMNQTYREEYRGFLNVYC 181
Cdd:cd00125   79 AN-DKCARALCECDRAAALCFARAPYNPKYRNYDKKRC 115
Phospholip_A2_1 pfam00068
Phospholipase A2; Phospholipase A2 releases fatty acids from the second carbon group of ...
 65-174 3.44e-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: 110.00  E-value: 3.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905576   65 LLNLKAMVEAVTGRSAILSFVGYGCYCGLGGRGQPKDEVDWCCHAHDCCYQELFDQGC-HPYVDHYDHTIENNTeIVCSd 143
Cdd:pfam00068   1 LWQFGEMIKCTTGRNPPLDYNDYGCYCGLGGSGTPVDATDRCCQAHDCCYERLKKLGCgNPYLLSYNYSCSDGT-ITCS- 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 767905576  144 lNKTECDKQTCMCDKNMVLCLMNQTYREEYR 174
Cdd:pfam00068  79 -GNSSCEKQLCECDKAAAECFARATYNKKYK 108
PA2c smart00085
Phospholipase A2;
64-176 1.11e-19

Phospholipase A2;


Pssm-ID: 214508  Cd Length: 117  Bit Score: 80.33  E-value: 1.11e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905576    64 SLLNLKAMVEAVTGRSAILSFVGYGCYCGLGGRGQPKDEVDWCCHAHDCCYQELFDQGCHPYVDHYDHTIENNTeIVCSD 143
Cdd:smart00085   1 NLWQFGNMIQCATGKRAWLSYGDYGCYCGWGGSGTPVDATDRCCFVHDCCYGKAEKEGCNPKTTTYSYSCDNGF-ITCGG 79

                           90       100       110
                   ....*....|....*....|....*....|...
gi 767905576   144 lNKTECDKQTCMCDKNMVLCLMNQTYREEYRGF 176
Cdd:smart00085  80 -KNTACLVFVCECDRAAAICFAKNPYNKKNYNI 111
PLA2_like cd00618
PLA2_like: Phospholipase A2, a super-family of secretory and cytosolic enzymes; the latter are ...
 97-166 6.03e-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: 67.20  E-value: 6.03e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905576  97 GQPKDEVDWCCHAHDCCYQELFDQGCHPYVDHYDHtienNTEIVCSDLNKTECDKQTCMCDKNMVLCLMN 166
Cdd:cd00618   17 GQPVDETDRCCRKHDCCYDQISDGGCCDGCLSYSF----SEGGVTCLTNSDLCTRSHCDCDRRLAICLAR 82
otoconin_90 cd04707
otoconin_90: Phospholipase A2-like domains present in otoconin-90 and otoconin-95, mammal ...
 93-186 1.04e-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: 48.63  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767905576  93 LGGRGQPKDEVDWCCHAHDCCYQELFDQGChpyvdHYDHTIenNTEIVCSD-----LNKTECDKQTCMCDKNMVLCLMNQ 167
Cdd:cd04707   26 QEGEGLPVDELDRCCFQHRCCLEQASEMGC-----LQDRKL--STEVTCVDhkpkcEGVSVCEKLLCTCDKTAAECMAAA 98

                         90
                 ....*....|....*....
gi 767905576 168 TYREEYRGFLNVYCQGPTP 186
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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