PLDA1_BRAOC
ID PLDA1_BRAOC Reviewed; 810 AA.
AC O82549;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Phospholipase D alpha 1;
DE Short=PLD 1;
DE EC=3.1.4.4;
DE AltName: Full=Choline phosphatase 1;
DE AltName: Full=Phosphatidylcholine-hydrolyzing phospholipase D 1;
DE Flags: Precursor;
GN Name=PLD1;
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 [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).
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 due to the absence of two potential
CC calcium ligands.
CC -!- MISCELLANEOUS: The propeptide appears to play a key role in the proper
CC 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; AF090445; AAC78487.1; -; mRNA.
DR EMBL; AF113918; AAD17208.1; -; Genomic_DNA.
DR AlphaFoldDB; O82549; -.
DR SMR; O82549; -.
DR PRIDE; O82549; -.
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 2: Evidence at transcript level;
KW Calcium; Cytoplasm; Hydrolase; Lipid degradation; Lipid metabolism;
KW Membrane; Metal-binding; Repeat.
FT PROPEP 1..36
FT /evidence="ECO:0000250"
FT /id="PRO_0000024649"
FT CHAIN 37..810
FT /note="Phospholipase D alpha 1"
FT /id="PRO_0000024650"
FT DOMAIN 1..126
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 327..366
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT DOMAIN 656..683
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 332
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 339
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 661
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 663
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 668
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 332
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 372
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 406
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 522
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 661
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 722
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
SQ SEQUENCE 810 AA; 91838 MW; CBC5B3D7E1F0DAAB CRC64;
MAQHLLHGTL HATIYEVDDL HTGGLRSGFF GKILANVEET IGVGKGETQL YATIDLQRAR
VGRTRKIKDE AKNPKWYESF HIYCAHLASD IIFTVKDDNP IGATLIGRAY VPVDQVIHGE
EVDQWVEILD NDRNPIHGGS KIHVKLQYFG VEADRNWNQG IKSAKFPGVP YTFFSQRQGC
KVSLYQDAHI PDNFVPRIPL AGGKNYEPQR CWEDIFDAIS NAQHMIYITG WSVYTEIALV
RDSRRPKPGG DVTVGELLKK KASEGVRVLL LVWDDRTSVD VLKKDGLMAT HDEETENFFR
GSDVHCILCP RNPDDGGSIV QNLQVSAMFT HHQKIVVVDS EMPSRGGSQM RRIVSFVGGI
DLCDGRYDTP FHSLFRTLDT VHHDDFHQPN FTGAAITKGG PREPWHDIHS RLEGPIAWDV
LYNFEQRWSK QGGKDILVKL RELSDIIITP SPVMFQEDHD VWNVQLFRSI DGGAAAGFPE
SPEAAAEAGL VSGKDNIIDR SIQDAYIHAI RRAKDFIYIE NQYFLGSSFA WAADGITPED
INALHLIPKE LSLKIVSKIE KGEKFRVYVV VPMWPEGLPE SASVQAILDW QRRTMQMMYK
DIVQALRAQG LEEDPRNYLT FFCLGNREVK KEGEYEPAER PDADSSYMKA QEARRFMIYV
HTKMMIVDDE YIIIGSANIN QRSMDGARDS EIAMGGYQPH HLSHRQPARG QIHGFRMSLW
YEHLGMLDET FLDPSSVECI EKVNRISDKY WDLYSSESLE HDLPGHLLRY PVDVDGEGDV
TEFPGFEFFP DTKARILGTK SDYLPPILTT
