PLDA1_RICCO
ID PLDA1_RICCO Reviewed; 808 AA.
AC Q41142; P93507;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 104.
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 Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 30-55.
RC STRAIN=cv. Hale; TISSUE=Endosperm;
RX PubMed=8051126; DOI=10.1016/s0021-9258(17)31993-2;
RA Wang X., Xu L., Zheng L.;
RT "Cloning and expression of phosphatidylcholine-hydrolyzing phospholipase D
RT from Ricinus communis L.";
RL J. Biol. Chem. 269:20312-20317(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Leaf;
RX PubMed=8980529; DOI=10.1007/bf00020218;
RA Xu L., Zheng L., Coughlan S.J., Wang X.;
RT "Structure and analysis of phospholipase D gene from Ricinus communis L.";
RL Plant Mol. Biol. 32:767-771(1996).
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}. Vacuole. Endoplasmic
CC reticulum. Plastid. Cell membrane.
CC -!- TISSUE SPECIFICITY: Expression is higher in radicle than in endosperm.
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; L33686; AAB04095.1; -; mRNA.
DR EMBL; U72693; AAB37305.1; -; Genomic_DNA.
DR PIR; T10171; T10171.
DR RefSeq; NP_001310687.1; NM_001323758.1.
DR AlphaFoldDB; Q41142; -.
DR SMR; Q41142; -.
DR STRING; 3988.XP_002517625.1; -.
DR PRIDE; Q41142; -.
DR GeneID; 8282326; -.
DR KEGG; rcu:8282326; -.
DR eggNOG; KOG1329; Eukaryota.
DR InParanoid; Q41142; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; 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; 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; 2.
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; Cell membrane; Cytoplasm; Direct protein sequencing;
KW Endoplasmic reticulum; Hydrolase; Lipid degradation; Lipid metabolism;
KW Membrane; Metal-binding; Plastid; Repeat; Vacuole.
FT PROPEP 1..30
FT /id="PRO_0000024653"
FT CHAIN 31..808
FT /note="Phospholipase D alpha 1"
FT /id="PRO_0000024654"
FT DOMAIN 1..125
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 326..364
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT DOMAIN 654..681
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 331
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 333
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 338
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 659
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 661
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 666
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT BINDING 186
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 331
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 370
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 404
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 520
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 659
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 720
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT CONFLICT 268
FT /note="L -> I (in Ref. 2; AAB37305)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 808 AA; 91992 MW; E75F6CFFB9ADF3CB CRC64;
MAQISLHGTL HVTIYEVDKL HSGGGPHFFR KLVENIEETV GFGKGVSKLY ATIDLEKARV
GRTRILENEQ SNPRWYESFH VYCAHQASNV IFTVKDDNPI GATLIGRAYV PVEELLDGEE
IDRWVEILDE DKNPVHSGSK IHVKLQYFEV TKDRNWGQGI RSSKYPGVPY TYFSQRQGCK
VSLYQDAHIP DKFVPQIPLA GGNYYEPHRC WEDVFDAITN AKHLIYITGW SVYTEISLIR
DSRRPKPGGD ITLGELLKKK ASEGVRVLML VWDDRTSVGL LKKDGLMATH DEETEHFFQN
TDVHCVLCPR NPDDGGSFVQ DLQISTMFTH HQKIVVVDSA MPNGDSQRRR IVSFVGGLDL
CDGRYDSPFH SLFRTLDSAH HDDFHQPNFA GASIEKGGPR EPWHDIHSRL EGPIAWDVLF
NFEQRWRKQG GKDLLIQLRE LEDVIIPPSP VMYPDDFEAW NVQLFRSIDG GAAFGFPETP
EDAPEAGLVS GKDNIIDRSI QDAYIHAIRR AKNFIYIENQ YFLGSSFGWS PDGIKPEDIN
ALHLIPKELS LKILSKIAAG ERFTVYIVVP MWPEGIPESA SVQAILDWQK RTMEMMYKDI
VQALKANGII EDPRNYLTFF CLGNREVKKS GEYEPAEKPE PDTDYIRAQE ARRFMIYVHT
KMMIVDDEYI IIGSANINQR SMDGARDSEI AMGAYQPHHL STRQPARGQI HGFRMSLWYE
HLGMLDESFL NPESEECVRK VNQMAEKYWD LYSSETLEHD LPGHLLRYPI GVASEGDVTE
LPGTEFFPDT KARVLGAKSD YLPPILTT
