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   16-JUN-2009, entry version 60.
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; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids I; Malpighiales; Euphorbiaceae; Acalyphoideae;
OC   Acalypheae; Ricinus.
OX   NCBI_TaxID=3988;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 30-55.
RC   STRAIN=cv. Hale; TISSUE=Endosperm;
RX   MEDLINE=94327597; PubMed=8051126;
RA   Wang X., Xu L., Zheng L.;
RT   "Cloning and expression of phosphatidylcholine-hydrolyzing
RT   phospholipase D from Ricinus communis L.";
RL   J. Biol. Chem. 269:20312-20317(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Leaf;
RX   MEDLINE=97134969; 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
RT   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: A phosphatidylcholine + H(2)O = choline + a
CC       phosphatidate.
CC   -!- COFACTOR: Calcium. Calcium requirement for activity depends on pH.
CC       Active either under acidic conditions with micromolar levels of
CC       calcium (PIP2-dependent) or at neutral pH with millimolar levels
CC       of calcium (PIP2-independent).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane;
CC       Peripheral membrane protein (By similarity). Vacuole. Endoplasmic
CC       reticulum. Plastid. Cell membrane.
CC   -!- TISSUE SPECIFICITY: Expression is higher in radicle than in
CC       endosperm.
CC   -!- DOMAIN: C2 domain is a calcium-binding fold, and the binding
CC       promotes the protein association with membranes. A lower affinity
CC       toward calcium can be anticipated for PLD alpha due to the absence
CC       of two potential calcium ligands.
CC   -!- MISCELLANEOUS: The propeptide appears to play a key role in the
CC       proper folding and activation of the enzyme.
CC   -!- SIMILARITY: Belongs to the phospholipase D family. C2-PLD
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 2 PLD phosphodiesterase domains.
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DR   EMBL; L33686; AAB04095.1; -; mRNA.
DR   EMBL; U72693; AAB37305.1; -; Genomic_DNA.
DR   PIR; T10171; T10171.
DR   BRENDA; 3.1.4.4; 816.
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:UniProtKB-KW.
DR   GO; GO:0070290; F:NAPE-specific phospholipase D activity; IEA:EC.
DR   GO; GO:0004630; F:phospholipase D activity; IEA:EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR015679; Phospholipase_D.
DR   InterPro; IPR011402; PLD_pln.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   PANTHER; PTHR18896; Phospholipase_D; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00614; PLDc; 2.
DR   PIRSF; PIRSF036470; PLD_plant; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00155; PLDc; 2.
DR   PROSITE; PS50004; C2; FALSE_NEG.
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; Membrane;
KW   Plastid; Repeat; Vacuole.
FT   PROPEP        1     30
FT                                /FTId=PRO_0000024653.
FT   CHAIN        31    808       Phospholipase D alpha 1.
FT                                /FTId=PRO_0000024654.
FT   DOMAIN        1    109       C2.
FT   DOMAIN      326    364       PLD phosphodiesterase 1.
FT   DOMAIN      654    681       PLD phosphodiesterase 2.
FT   ACT_SITE    331    331       Potential.
FT   ACT_SITE    333    333       Potential.
FT   ACT_SITE    338    338       Potential.
FT   ACT_SITE    659    659       Potential.
FT   ACT_SITE    661    661       Potential.
FT   ACT_SITE    666    666       Potential.
FT   CONFLICT    268    268       L -> I (in Ref. 2; AAB37305).
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
//