Literature summary for 3.1.4.4 extracted from

Rahier, R.; Noiriel, A.; Abousalham, A.
Functional characterization of the N-terminal C2 domain from Arabidopsis thaliana phospholipase Dalpha and Dbeta (2016), BioMed Res. Int., 2016, 2721719 .

Search for more literature for 3.1.4.4

Cloned(Commentary)

Cloned (Comment)	Organism
expression of mature-like form of the C2 domain in Escherichia coli	Arabidopsis thaliana
expression of protein in Pichia pastoris, expression of mature-like form of the C2 domain in Escherichia coli	Arabidopsis thaliana

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	the C2 domain binds phosphatidylglycerol in a Ca2+-independent manner while phosphatidic acid and phosphatidylserine binding are enhanced in the presence of Ca2+	Arabidopsis thaliana

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	P93733	isoform PLDbeta1	-
Arabidopsis thaliana	Q38882	isoform PLDalpha1	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	sequence contains one potential N-glycosylation site	Arabidopsis thaliana

Purification (Commentary)

Purification (Comment)	Organism
partial, recombinant protein	Arabidopsis thaliana

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine + H2O	-	Arabidopsis thaliana	1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidate + choline	-	?

Subunits

Subunits	Comment	Organism
?	x * 14300, isolated C2 domain, SDS-PAGE	Arabidopsis thaliana
?	x * 90000, SDS-PAGE, x * 88100, calculated from sequence. X * 14800, isolated C2 domain, SDS-PAGE	Arabidopsis thaliana

Synonyms

Synonyms	Comment	Organism
PLDalpha	-	Arabidopsis thaliana
PLDbeta	-	Arabidopsis thaliana

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Release 2023.1 (January 2023)