ID PLDA2_BRAOC Reviewed; 812 AA. AC P55939; O49981; O82548; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 21-FEB-2001, sequence version 2. DT 02-SEP-2026, entry version 111. DE RecName: Full=Phospholipase D alpha 2; DE Short=PLD 2; DE EC=3.1.4.4; DE AltName: Full=Choline phosphatase 2; DE AltName: Full=Phosphatidylcholine-hydrolyzing phospholipase D 2; DE Flags: Precursor; GN Name=PLD2; OS Brassica oleracea var. capitata (Cabbage). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica. OX NCBI_TaxID=3716; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=10101274; DOI=10.1016/s1388-1981(99)00020-7; RA Kim D.-U., Roh T.-Y., Lee J., Noh J.-Y., Jang Y.-J., Hoe K.-L., Yoo H.-S., RA Choi M.-U.; RT "Molecular cloning and functional expression of a phospholipase D from RT cabbage (Brassica oleracea var. capitata)."; RL Biochim. Biophys. Acta 1437:409-414(1999). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RA Pannenberg I., Mansfeld J., Ulbrich-Hofmann R.; RT "Identification of two isoenzymes of phospholipase D from cabbage (Brassica RT oleracea var. capitata)."; RL (er) Plant Gene Register PGR98-188(1998). RN [3] RP PROTEIN SEQUENCE OF 37-68. RC TISSUE=Leaf; RX PubMed=8353126; DOI=10.1016/0304-4165(93)90088-p; RA Abousalham A., Riviere M., Teissere M., Verger R.; RT "Improved purification and biochemical characterization of phospholipase D RT from cabbage."; RL Biochim. Biophys. Acta 1158:1-7(1993). RN [4] RP CHARACTERIZATION OF SULFHYDRYL GROUPS. RX PubMed=11180538; RX DOI=10.1002/1097-0231(20010130)15:2<110::aid-rcm200>3.0.co;2-r; RA Hwang I.S., Park S.J., Roh T.-Y., Choi M.-U., Kim H.J.; RT "Investigation of sulfhydryl groups in cabbage phospholipase D by RT combination of derivatization methods and matrix-assisted laser RT desorption/ionization time-of-flight mass spectrometry."; RL Rapid Commun. Mass Spectrom. 15:110-115(2001). CC -!- FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal CC phosphodiesteric bond. Plays an important role in various cellular CC processes, including phytohormone action, vesicular trafficking, CC secretion, cytoskeletal arrangement, meiosis, tumor promotion, CC pathogenesis, membrane deterioration and senescence. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl- CC sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:14445, CC ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58608; EC=3.1.4.4; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Note=Ca(2+) requirement for activity depends on pH. Active either under CC acidic conditions with micromolar levels of calcium (PIP2-dependent) or CC at neutral pH with millimolar levels of calcium (PIP2-independent).; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; CC Peripheral membrane protein {ECO:0000250}. CC -!- DOMAIN: C2 domain is a calcium-binding fold, and the binding promotes CC the protein association with membranes. A lower affinity toward calcium CC can be anticipated for PLD alpha C2 due to the absence of two potential CC calcium ligands. CC -!- MISCELLANEOUS: All eight cysteine residues were shown to have free CC sulfhydryl groups by mass spectrometry. The propeptide appears to play CC a key role in the proper folding and activation of the enzyme. CC -!- SIMILARITY: Belongs to the phospholipase D family. C2-PLD subfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U85482; AAC79125.1; -; mRNA. DR EMBL; AF090444; AAC78486.1; -; mRNA. DR EMBL; AF113919; AAD17209.1; -; Genomic_DNA. DR AlphaFoldDB; P55939; -. DR SMR; P55939; -. DR BRENDA; 3.1.4.4; 946. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0004630; F:D-type glycerophospholipase activity; IEA:UniProtKB-EC. DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro. DR GO; GO:0009395; P:phospholipid catabolic process; IEA:TreeGrafter. DR CDD; cd04015; C2_plant_PLD; 1. DR CDD; cd09199; PLDc_pPLDalpha_2; 1. DR FunFam; 3.30.870.10:FF:000027; Phospholipase D; 1. DR FunFam; 2.60.40.150:FF:000266; Phospholipase D alpha 1; 1. DR FunFam; 3.30.870.10:FF:000025; Phospholipase D delta; 1. DR Gene3D; 2.60.40.150; C2 domain; 1. DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2. DR InterPro; IPR000008; C2_dom. DR InterPro; IPR035892; C2_domain_sf. DR InterPro; IPR001736; PLipase_D/transphosphatidylase. DR InterPro; IPR015679; PLipase_D_fam. DR InterPro; IPR011402; PLipase_D_pln. DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1. DR PANTHER; PTHR18896:SF163; PHOSPHOLIPASE D; 1. DR Pfam; PF00168; C2; 1. DR Pfam; PF00614; PLDc; 1. DR PIRSF; PIRSF036470; PLD_plant; 1. DR SMART; SM00239; C2; 1. DR SMART; SM00155; PLDc; 2. DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1. DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2. DR PROSITE; PS50004; C2; 1. DR PROSITE; PS50035; PLD; 2. PE 1: Evidence at protein level; KW Calcium; Cytoplasm; Direct protein sequencing; Hydrolase; KW Lipid degradation; Lipid metabolism; Membrane; Metal-binding; Repeat. FT PROPEP 1..36 FT /evidence="ECO:0000269|PubMed:8353126" FT /id="PRO_0000024651" FT CHAIN 37..812 FT /note="Phospholipase D alpha 2" FT /id="PRO_0000024652" FT DOMAIN 1..127 FT /note="C2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT DOMAIN 328..368 FT /note="PLD phosphodiesterase 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153" FT DOMAIN 658..685 FT /note="PLD phosphodiesterase 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153" FT ACT_SITE 333 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153" FT ACT_SITE 335 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153" FT ACT_SITE 340 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153" FT ACT_SITE 663 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153" FT ACT_SITE 665 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153" FT ACT_SITE 670 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153" FT BINDING 333 FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate" FT /ligand_id="ChEBI:CHEBI:58608" FT /evidence="ECO:0000250|UniProtKB:Q38882" FT BINDING 374 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q38882" FT BINDING 524 FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate" FT /ligand_id="ChEBI:CHEBI:58608" FT /evidence="ECO:0000250|UniProtKB:Q38882" FT BINDING 663 FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate" FT /ligand_id="ChEBI:CHEBI:58608" FT /evidence="ECO:0000250|UniProtKB:Q38882" FT BINDING 724 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q38882" FT CONFLICT 50 FT /note="Q -> E (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" SQ SEQUENCE 812 AA; 92062 MW; F771FC53734E7A2B CRC64; MAQHLLHGTL HATIYEVDAL HTGGLRSAGF LGKIISNVEE TIGFGKGETQ LYATIDLQKA RVGRTRKITD EPKNPKWYES FHIYCAHMAS DIIFTVKDDN PIGATLIGRA YVPVDEVING EEVEKWVEIL DDDRNPIHGE SKIHVKLQYF AVEADRNWNM GVKSAKFPGV PYTFFSQRQG CKVSLYQGAH VPDNFVPKIP LAGGKNYEPH RCWEDIFDAI TNAKHLIYIT GWSVYTEITL VRDSRRPKPG GDMTLGELLK KKATEGVRVL LLVWDDRTSV DVLKKDGLMA THDEDTENYF NGSEVHCVLC PRNPDDGGSI VQNLQVSAMF THHQKIVVVD SEVPSQGGGS EMRRIMSFVG GIDLCDGRYD TPFHSLFRTL DTVHHDDFHQ PNFTGASITK GGPREPWQDI HSRLEGPIAW DVLYNFEQRW SKQGGKDILV KLRELSDIII TPSPVMFQED HDVWNVQLFR SIDGGAAAGF PDSPEVAAEA GLVSGKDNVI DRSIQDAYIH AIRRAKDFIY IENQYFLGSS FAWAADGITP EDINALHLIP KELSLKIVDK IEKGEKFRVY VVVPMWPEGI PESASVQAIL DWQRRTLEMM YKDVTQALRA QGLEEDPRNY LTFFCLGNRE VKKEGEYEPA ERPDPDTDYM RAQEARRFMI YVHSKMMIVD DEYIIVGSAN INQRSMDGAR DSEIAMGGYQ PHHLSHRQPA RGQVHGFRMS LWYEHLGMLD ETFLDPSSLE CIEKVNRIAD KYWDFYSSES LEHDLPGHLL RYPISVDNEG NITELPGFEF FPDSKARILG NKVDYLPPIL TT //