PLDA2_BRAOC
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 03-AUG-2022, entry version 102.
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}.
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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 PRIDE; P55939; -.
DR BRENDA; 3.1.4.4; 947.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR024632; PLipase_D_C.
DR InterPro; IPR015679; PLipase_D_fam.
DR InterPro; IPR011402; PLipase_D_pln.
DR PANTHER; PTHR18896; PTHR18896; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF12357; PLD_C; 1.
DR Pfam; PF00614; PLDc; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR PIRSF; PIRSF036470; PLD_plant; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF49562; SSF49562; 1.
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
