Protein Family Models

This family consists of several phospholipase A2 like proteins mostly from insects [1]. [1][1]. 1216762712167627. Bee venom phospholipase inhibits malaria parasite development inBee venom phospholipase inhibits malaria parasite development in transgenic mosquitoes.transgenic mosquitoes. Moreira LA, Ito J, Ghosh A, Devenport M, Zieler H, Abraham EG,Moreira LA, Ito J, Ghosh A, Devenport M, Zieler H, Abraham EG, Crisanti A, Nolan T, Catteruccia F, Jacobs-Lorena M;Crisanti A, Nolan T, Catteruccia F, Jacobs-Lorena M;. J Biol Chem 2002;277:40839-40843.J Biol Chem 2002;277:40839-40843. (from Pfam)

Date:

2025-02-20

This family consists of Lysophospholipase / phospholipase B EC:3.1.1.5 and cytosolic phospholipase A2 EC:3.1.4 which also has a C2 domain Pfam:PF00168. Phospholipase B enzymes catalyse the release of fatty acids from lysophsopholipids and are capable in vitro of hydrolysing all phospholipids extractable form yeast cells [1]. Cytosolic phospholipase A2 associates with natural membranes in response to physiological increases in Ca2+ and selectively hydrolyses arachidonyl phospholipids [2], the aligned region corresponds the the carboxy-terminal Ca2+-independent catalytic domain of the protein as discussed in [2]. [1][1]. 80270858027085. Delineation of two functionally distinct domains of cytosolicDelineation of two functionally distinct domains of cytosolic phospholipase A2, a regulatory Ca(2+)-dependent lipid-bindingphospholipase A2, a regulatory Ca(2+)-dependent lipid-binding domain and a Ca(2+)-independent catalytic domain.domain and a Ca(2+)-independent catalytic domain. Nalefski EA, Sultzman LA, Martin DM, Kriz RW, Towler PS, KnopfNalefski EA, Sultzman LA, Martin DM, Kriz RW, Towler PS, Knopf JL, Clark JD;JL, Clark JD;. J Biol Chem 1994;269:18239-18249.J Biol Chem 1994;269:18239-18249. [2][2]. 80510528051052. The Saccharomyces cerevisiae PLB1 gene encodes a proteinThe Saccharomyces cerevisiae PLB1 gene encodes a protein required for lysophospholipase and phospholipase B activity.required for lysophospholipase and phospholipase B activity. Lee KS, Patton JL, Fido M, Hines LK, Kohlwein SD, Paltauf F,Lee KS, Patton JL, Fido M, Hines LK, Kohlwein SD, Paltauf F, Henry SA, Levin DE;Henry SA, Levin DE;. J Biol Chem 1994;26. TRUNCATED at 1650 bytes (from Pfam)

Date:

2025-02-20

This family is has been called MAPEG (Membrane Associated Proteins in Eicosanoid and Glutathione metabolism). It includes proteins such as Prostaglandin E synthase. This enzyme catalyses the synthesis of PGE2 from PGH2 (produced by cyclooxygenase from arachidonic acid). Because of structural similarities in the active sites of FLAP, LTC4 synthase and PGE synthase, substrates for each enzyme can compete with one another and modulate synthetic activity. [1][1]. 1009167210091672. Common structural features of MAPEG -- a widespread superfamilyCommon structural features of MAPEG -- a widespread superfamily of membrane associated proteins with highly divergent functionsof membrane associated proteins with highly divergent functions in eicosanoid and glutathione metabolism.in eicosanoid and glutathione metabolism. Jakobsson PJ, Morgenstern R, Mancini J, Ford-Hutchinson A,Jakobsson PJ, Morgenstern R, Mancini J, Ford-Hutchinson A, Persson B;Persson B;. Protein Sci 1999;8:689-692.Protein Sci 1999;8:689-692. (from Pfam)

Date:

2025-02-20

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 recognised. This minor family conserves the core helix pair but is substantially different elsewhere. The PROSITE pattern PA2_HIS, specific to the first core helix, recognises both families. (from Pfam)

Date:

2025-02-20

patatin-like phospholipase domain-containing protein may function as a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids

Date:

2021-12-17

MAPEG (Membrane Associated Proteins in Eicosanoid and Glutathione metabolism) family protein is a membrane associated protein; similar to mammalian prostaglandin E synthase, leukotriene C4 synthase, arachidonate 5-lipoxygenase-activating protein, microsomal glutathione S-transferases, and mitochondrial glutathione S-transferase 3

Date:

2017-03-02

serine/threonine-protein kinase N (PKN) catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates, and can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids

Date:

2017-03-02

serine/threonine-protein kinase N catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates, and can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids

Date:

2021-07-29

serine/threonine-protein kinase N (PKN) catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates, and can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids| Sck1 family serine/threonine-protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates; similar to Schizosaccharomyces pombe Sck1 that plays a role in trehalase activation

Date:

2017-03-02

serine/threonine-protein kinase N (PKN) catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates, and can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids

Date:

2017-03-02

serine/threonine-protein kinase N (PKN) catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates, and can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids| Sck1 family serine/threonine-protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates; similar to Schizosaccharomyces pombe Sck1 that plays a role in trehalase activation

Date:

2017-03-02

serine/threonine-protein kinase N (PKN) catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates, and can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids| Sck1 family serine/threonine-protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates; similar to Schizosaccharomyces pombe Sck1 that plays a role in trehalase activation

Date:

2017-03-02

serine/threonine-protein kinase N (PKN) catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates, and can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids

Date:

2017-03-02

serine/threonine-protein kinase N (PKN) catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates, and can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids| Sck1 family serine/threonine-protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates; similar to Schizosaccharomyces pombe Sck1 that plays a role in trehalase activation

Date:

2017-03-02

MAPEG (Membrane Associated Proteins in Eicosanoid and Glutathione metabolism) family protein is a membrane associated protein; similar to mammalian prostaglandin E synthase, leukotriene C4 synthase, arachidonate 5-lipoxygenase-activating protein, microsomal glutathione S-transferases, and mitochondrial glutathione S-transferase 3

Date:

2024-05-29

serine/threonine-protein kinase N (PKN) catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates, and can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids| Sck1 family serine/threonine-protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates; similar to Schizosaccharomyces pombe Sck1 that plays a role in trehalase activation

Date:

2017-03-02

serine/threonine-protein kinase N (PKN) catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates, and can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids

Date:

2023-11-13

serine/threonine-protein kinase N (PKN) catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates, and can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids

Date:

2023-04-18

serine/threonine-protein kinase N (PKN) catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates, and can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids

Date:

2017-03-02

serine/threonine-protein kinase N (PKN) catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates, and can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids

Date:

2019-03-21