NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|142976884|ref|NP_056530|]
View 

group 3 secretory phospholipase A2 precursor [Homo sapiens]

Protein Classification

PLA2_bee_venom_like and PLA2_group_III_like domain-containing protein( domain architecture ID 10140434)

PLA2_bee_venom_like and PLA2_group_III_like domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PLA2_bee_venom_like cd04704
PLA2_bee_venom_like: A sub-family of Phospholipase A2, similar to bee venom PLA2. PLA2 is a ...
 151-247 4.48e-54

PLA2_bee_venom_like: A sub-family of Phospholipase A2, similar to bee venom PLA2. PLA2 is a super-family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. Enzymatically active PLA2 cleaves the sn-2 position of the glycerol backbone of phospholipids; 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 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. Bee venom PLA2 has fewer conserved disulfide bridges than most canonical PLA2s.


:

Pssm-ID: 153093  Cd Length: 97  Bit Score: 177.11  E-value: 4.48e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142976884 151 WTMPGTLWCGVGDSAGNSSELGVFQGPDLCCREHDRCPQNISPLQYNYGIRNYRFHTISHCDCDTRFQQCLQNQHDSISD 230
Cdd:cd04704    1 FIVPGTKWCGPGNIATNYSDLGAFRETDKCCREHDHCPDIISAGEYKYGLTNTRLFTRSHCDCDNRFRQCLKNVNDSTSN 80

                         90
                 ....*....|....*..
gi 142976884 231 IVGVAFFNVLEIPCFVL 247
Cdd:cd04704   81 QVGKIYFNVLQVPCFEL 97
PLA2_group_III_like cd04705
PLA2_group_III_like: A sub-family of Phospholipase A2, similar to human group III PLA2. PLA2 ...
 314-427 1.37e-32

PLA2_group_III_like: A sub-family of Phospholipase A2, similar to human group III PLA2. PLA2 is a super-family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. Enzymatically active PLA2 cleaves the sn-2 position of the glycerol backbone of phospholipids; 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 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: 153094  Cd Length: 100  Bit Score: 119.94  E-value: 1.37e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142976884 314 HQKGSKRPSKANTTA-LQDPMVSPRLdvaptglqgpqgglKPQGARWVCRSFRRHlDQCEHQIGPREIEFQLLNSAQEPL 392
Cdd:cd04705    1 TRLTSERRGLEKTGAiASSPDVSPFL--------------SEGEFKEPDRCCWKH-KQCPGHIIPPFSSDGHHNFHLHSV 65

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 142976884 393 FHCNCTRRLARFLRLHSPPEVTNMLWELLGTTCFK 427
Cdd:cd04705   66 SHCDCDSRLKDCLRLSSSSRVGPTCSHLLGTTCFN 100
 
Name Accession Description Interval E-value
PLA2_bee_venom_like cd04704
PLA2_bee_venom_like: A sub-family of Phospholipase A2, similar to bee venom PLA2. PLA2 is a ...
 151-247 4.48e-54

PLA2_bee_venom_like: A sub-family of Phospholipase A2, similar to bee venom PLA2. PLA2 is a super-family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. Enzymatically active PLA2 cleaves the sn-2 position of the glycerol backbone of phospholipids; 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 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. Bee venom PLA2 has fewer conserved disulfide bridges than most canonical PLA2s.


Pssm-ID: 153093  Cd Length: 97  Bit Score: 177.11  E-value: 4.48e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142976884 151 WTMPGTLWCGVGDSAGNSSELGVFQGPDLCCREHDRCPQNISPLQYNYGIRNYRFHTISHCDCDTRFQQCLQNQHDSISD 230
Cdd:cd04704    1 FIVPGTKWCGPGNIATNYSDLGAFRETDKCCREHDHCPDIISAGEYKYGLTNTRLFTRSHCDCDNRFRQCLKNVNDSTSN 80

                         90
                 ....*....|....*..
gi 142976884 231 IVGVAFFNVLEIPCFVL 247
Cdd:cd04704   81 QVGKIYFNVLQVPCFEL 97
Phospholip_A2_2 pfam05826
Phospholipase A2; This family consists of several phospholipase A2 like proteins mostly from ...
 152-248 2.97e-47

Phospholipase A2; This family consists of several phospholipase A2 like proteins mostly from insects.


Pssm-ID: 461751  Cd Length: 97  Bit Score: 158.84  E-value: 2.97e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142976884  152 TMPGTLWCGVGDSAGNSSELGVFQGPDLCCREHDRCPQNISPLQYNYGIRNYRFHTISHCDCDTRFQQCLQNQHDSISDI 231
Cdd:pfam05826   1 IYPGTKWCGTGNIAENYDDLGEFDETDRCCREHDHCPDTIESFQTKYGLTNFRPFTRSHCDCDQRFRRCLKNTNSSVSNA 80

                          90
                  ....*....|....*..
gi 142976884  232 VGVAFFNVLEIPCFVLE 248
Cdd:pfam05826  81 VGFIYFNVLQVKCFRLI 97
PLA2_group_III_like cd04705
PLA2_group_III_like: A sub-family of Phospholipase A2, similar to human group III PLA2. PLA2 ...
 314-427 1.37e-32

PLA2_group_III_like: A sub-family of Phospholipase A2, similar to human group III PLA2. PLA2 is a super-family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. Enzymatically active PLA2 cleaves the sn-2 position of the glycerol backbone of phospholipids; 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 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: 153094  Cd Length: 100  Bit Score: 119.94  E-value: 1.37e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142976884 314 HQKGSKRPSKANTTA-LQDPMVSPRLdvaptglqgpqgglKPQGARWVCRSFRRHlDQCEHQIGPREIEFQLLNSAQEPL 392
Cdd:cd04705    1 TRLTSERRGLEKTGAiASSPDVSPFL--------------SEGEFKEPDRCCWKH-KQCPGHIIPPFSSDGHHNFHLHSV 65

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 142976884 393 FHCNCTRRLARFLRLHSPPEVTNMLWELLGTTCFK 427
Cdd:cd04705   66 SHCDCDSRLKDCLRLSSSSRVGPTCSHLLGTTCFN 100
PA2c smart00085
Phospholipase A2;
148-262 1.74e-06

Phospholipase A2;


Pssm-ID: 214508  Cd Length: 117  Bit Score: 46.81  E-value: 1.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142976884   148 KRGWTMPGTLWCGVGdsAGNSselgvfqGP-----DLCCREHDRCPQNISPLQYNygirnyRFHTISHCDCDTRFQQCLq 222
Cdd:smart00085  15 KRAWLSYGDYGCYCG--WGGS-------GTpvdatDRCCFVHDCCYGKAEKEGCN------PKTTTYSYSCDNGFITCG- 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 142976884   223 nqHDSISDIVGVAFFNVLEIPCFVLE-EQEACVAWYWWGGC 262
Cdd:smart00085  79 --GKNTACLVFVCECDRAAAICFAKNpYNKKNYNIDTKKRC 117
 
Name Accession Description Interval E-value
PLA2_bee_venom_like cd04704
PLA2_bee_venom_like: A sub-family of Phospholipase A2, similar to bee venom PLA2. PLA2 is a ...
 151-247 4.48e-54

PLA2_bee_venom_like: A sub-family of Phospholipase A2, similar to bee venom PLA2. PLA2 is a super-family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. Enzymatically active PLA2 cleaves the sn-2 position of the glycerol backbone of phospholipids; 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 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. Bee venom PLA2 has fewer conserved disulfide bridges than most canonical PLA2s.


Pssm-ID: 153093  Cd Length: 97  Bit Score: 177.11  E-value: 4.48e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142976884 151 WTMPGTLWCGVGDSAGNSSELGVFQGPDLCCREHDRCPQNISPLQYNYGIRNYRFHTISHCDCDTRFQQCLQNQHDSISD 230
Cdd:cd04704    1 FIVPGTKWCGPGNIATNYSDLGAFRETDKCCREHDHCPDIISAGEYKYGLTNTRLFTRSHCDCDNRFRQCLKNVNDSTSN 80

                         90
                 ....*....|....*..
gi 142976884 231 IVGVAFFNVLEIPCFVL 247
Cdd:cd04704   81 QVGKIYFNVLQVPCFEL 97
Phospholip_A2_2 pfam05826
Phospholipase A2; This family consists of several phospholipase A2 like proteins mostly from ...
 152-248 2.97e-47

Phospholipase A2; This family consists of several phospholipase A2 like proteins mostly from insects.


Pssm-ID: 461751  Cd Length: 97  Bit Score: 158.84  E-value: 2.97e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142976884  152 TMPGTLWCGVGDSAGNSSELGVFQGPDLCCREHDRCPQNISPLQYNYGIRNYRFHTISHCDCDTRFQQCLQNQHDSISDI 231
Cdd:pfam05826   1 IYPGTKWCGTGNIAENYDDLGEFDETDRCCREHDHCPDTIESFQTKYGLTNFRPFTRSHCDCDQRFRRCLKNTNSSVSNA 80

                          90
                  ....*....|....*..
gi 142976884  232 VGVAFFNVLEIPCFVLE 248
Cdd:pfam05826  81 VGFIYFNVLQVKCFRLI 97
PLA2_group_III_like cd04705
PLA2_group_III_like: A sub-family of Phospholipase A2, similar to human group III PLA2. PLA2 ...
 314-427 1.37e-32

PLA2_group_III_like: A sub-family of Phospholipase A2, similar to human group III PLA2. PLA2 is a super-family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. Enzymatically active PLA2 cleaves the sn-2 position of the glycerol backbone of phospholipids; 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 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: 153094  Cd Length: 100  Bit Score: 119.94  E-value: 1.37e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142976884 314 HQKGSKRPSKANTTA-LQDPMVSPRLdvaptglqgpqgglKPQGARWVCRSFRRHlDQCEHQIGPREIEFQLLNSAQEPL 392
Cdd:cd04705    1 TRLTSERRGLEKTGAiASSPDVSPFL--------------SEGEFKEPDRCCWKH-KQCPGHIIPPFSSDGHHNFHLHSV 65

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 142976884 393 FHCNCTRRLARFLRLHSPPEVTNMLWELLGTTCFK 427
Cdd:cd04705   66 SHCDCDSRLKDCLRLSSSSRVGPTCSHLLGTTCFN 100
PLA2_group_III_like cd04705
PLA2_group_III_like: A sub-family of Phospholipase A2, similar to human group III PLA2. PLA2 ...
 172-238 8.77e-18

PLA2_group_III_like: A sub-family of Phospholipase A2, similar to human group III PLA2. PLA2 is a super-family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. Enzymatically active PLA2 cleaves the sn-2 position of the glycerol backbone of phospholipids; 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 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: 153094  Cd Length: 100  Bit Score: 78.72  E-value: 8.77e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 142976884 172 GVFQGPDLCCREHDRCPQNISPLQYNYGIRNYRFHTISHCDCDTRFQQCLQ-----NQHDSISDIVGVAFFN 238
Cdd:cd04705   29 GEFKEPDRCCWKHKQCPGHIIPPFSSDGHHNFHLHSVSHCDCDSRLKDCLRlssssRVGPTCSHLLGTTCFN 100
PLA2_like cd00618
PLA2_like: Phospholipase A2, a super-family of secretory and cytosolic enzymes; the latter are ...
 153-223 1.96e-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: 71.44  E-value: 1.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142976884 153 MPGTLWCGVGDSAGNSSELGvfQGPDLCCREHDRCPQNISPLQYNYGI-------------RNYRFHTISHCDCDTRFQQ 219
Cdd:cd00618    1 LPYGCYCGPGGSACPSGQPV--DETDRCCRKHDCCYDQISDGGCCDGClsysfseggvtclTNSDLCTRSHCDCDRRLAI 78


                 ....
gi 142976884 220 CLQN 223
Cdd:cd00618   79 CLAR 82
PA2c smart00085
Phospholipase A2;
148-262 1.74e-06

Phospholipase A2;


Pssm-ID: 214508  Cd Length: 117  Bit Score: 46.81  E-value: 1.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142976884   148 KRGWTMPGTLWCGVGdsAGNSselgvfqGP-----DLCCREHDRCPQNISPLQYNygirnyRFHTISHCDCDTRFQQCLq 222
Cdd:smart00085  15 KRAWLSYGDYGCYCG--WGGS-------GTpvdatDRCCFVHDCCYGKAEKEGCN------PKTTTYSYSCDNGFITCG- 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 142976884   223 nqHDSISDIVGVAFFNVLEIPCFVLE-EQEACVAWYWWGGC 262
Cdd:smart00085  79 --GKNTACLVFVCECDRAAAICFAKNpYNKKNYNIDTKKRC 117
PLA2_like cd00618
PLA2_like: Phospholipase A2, a super-family of secretory and cytosolic enzymes; the latter are ...
 346-408 1.69e-05

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: 43.32  E-value: 1.69e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 142976884 346 QGPQGGLKPQGARWVCRSFRRHlDQCEHQIGPRE-------------IEFQLLNSAQEPLFHCNCTRRLARFLRLH 408
Cdd:cd00618    9 PGGSACPSGQPVDETDRCCRKH-DCCYDQISDGGccdgclsysfsegGVTCLTNSDLCTRSHCDCDRRLAICLARA 83
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH