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Conserved domains on  [gi|139947887|ref|NP_001038981|]
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protein PROCA1 isoform 2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLA2_like super family cl05417
PLA2_like: Phospholipase A2, a super-family of secretory and cytosolic enzymes; the latter are ...
1-36 1.95e-04

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.


The actual alignment was detected with superfamily member cd04705:

Pssm-ID: 471240  Cd Length: 100  Bit Score: 39.43  E-value: 1.95e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 139947887   1 MHAVSQCDCESRCRSHRPVSVAIIYHPT-HHMYMTDD 36
Cdd:cd04705   62 LHSVSHCDCDSRLKDCLRLSSSSRVGPTcSHLLGTTC 98
 
Name Accession Description Interval E-value
PLA2_group_III_like cd04705
PLA2_group_III_like: A sub-family of Phospholipase A2, similar to human group III PLA2. PLA2 ...
1-36 1.95e-04

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: 39.43  E-value: 1.95e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 139947887   1 MHAVSQCDCESRCRSHRPVSVAIIYHPT-HHMYMTDD 36
Cdd:cd04705   62 LHSVSHCDCDSRLKDCLRLSSSSRVGPTcSHLLGTTC 98
 
Name Accession Description Interval E-value
PLA2_group_III_like cd04705
PLA2_group_III_like: A sub-family of Phospholipase A2, similar to human group III PLA2. PLA2 ...
1-36 1.95e-04

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: 39.43  E-value: 1.95e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 139947887   1 MHAVSQCDCESRCRSHRPVSVAIIYHPT-HHMYMTDD 36
Cdd:cd04705   62 LHSVSHCDCDSRLKDCLRLSSSSRVGPTcSHLLGTTC 98
 
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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