ID   PLDA1_MAIZE             Reviewed;         812 AA.
AC   Q43270;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   16-JUN-2009, entry version 57.
DE   RecName: Full=Phospholipase D alpha 1;
DE            Short=PLD alpha 1;
DE            EC=3.1.4.4;
DE   AltName: Full=Choline phosphatase 1;
DE   AltName: Full=Phosphatidylcholine-hydrolyzing phospholipase D 1;
GN   Name=PLD1;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae;
OC   PACCAD clade; Panicoideae; Andropogoneae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Missouri 17;
RX   MEDLINE=96012933; PubMed=7551587;
RA   Ueki J., Morioka S., Komari T., Kumashiro T.;
RT   "Purification and characterization of phospholipase D (PLD) from rice
RT   (Oryza sativa L.) and cloning of cDNA for PLD from rice and maize (Zea
RT   mays L.).";
RL   Plant Cell Physiol. 36:903-914(1995).
CC   -!- FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal
CC       phosphodiesteric bond. Plays an important role in various cellular
CC       processes.
CC   -!- CATALYTIC ACTIVITY: A phosphatidylcholine + H(2)O = choline + a
CC       phosphatidate.
CC   -!- COFACTOR: Calcium (By similarity).
CC   -!- SUBUNIT: Monomer (By similarity).
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   -!- 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; D73410; BAA11135.1; -; mRNA.
DR   PIR; T03659; T03659.
DR   RefSeq; NP_001105686.1; -.
DR   UniGene; Zm.95980; -.
DR   GeneID; 542702; -.
DR   Gramene; Q43270; -.
DR   MaizeGDB; 113853; -.
DR   BRENDA; 3.1.4.4; 289.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Calcium; Hydrolase; Lipid degradation; Repeat.
FT   CHAIN         1    812       Phospholipase D alpha 1.
FT                                /FTId=PRO_0000218820.
FT   DOMAIN        1    114       C2.
FT   DOMAIN      330    368       PLD phosphodiesterase 1.
FT   DOMAIN      658    685       PLD phosphodiesterase 2.
FT   ACT_SITE    335    335       Potential.
FT   ACT_SITE    337    337       Potential.
FT   ACT_SITE    342    342       Potential.
FT   ACT_SITE    663    663       Potential.
FT   ACT_SITE    665    665       Potential.
FT   ACT_SITE    670    670       Potential.
SQ   SEQUENCE   812 AA;  92242 MW;  D05CB351655BCC61 CRC64;
     MAQILLHGTL HATIFEAESL SNPHRATGGA PKFIRKLVEG IEDTVGVGKG ATKIYATVDL
     EKARVGRTRM ISNEPVNPRW YESFHIYCAH MAADVIFTVK IDNSIGASLI GRAYLAVQDL
     LGGEEIDKWL EISDENREPV GDSKIHVKLQ YFDVGKDRNW ARGVRSTKYP GVPYTFFSQR
     QGCKVTLYQD AHVPDNFVPR IQLADGKNYE PHRCWEDIFD AISKAQHLIY ITGWSVYTEI
     TLVRDTNRPK PGGDVTLGEL LKRKASEGVR VLMLVWDDRT SVGLLKKDGL MATHDEETAN
     YFHGTDVNCV LCPRNPDDSG SFVQDLQIST MFTHHQKIVV VDHEMPNQGS QQRRIVSFIG
     GIDLCDGRYD TQYHSLFRTL DTVHHDDFHQ PNFEGGSIKK GGPREPWHDI HSRLEGPIAW
     DVLYNFEQRW RKQGGKDLLV RLRDLPDIII PPSPVMFPED RETWNVQLFR SIDGGAAFGF
     PETPEEAARA GLVSGKDQII DRSIQDAYVN AIRRAKNFIY IENQYFLGSS YGWKPEGIKP
     EEIGALHLIP KELSLKIVSK IEAGERFTVY VVVPMWPEGV PESASVQAIL DWQRRTMEMM
     YTDIAQALEA NGIEANPKDY LTFFCLGNRE VKQEGEYEPE EHPEPDTDYI RAQEARRFMI
     YVHTKMMIVD DEYIIIGSAN INQRSMDGAR DSEIAMGAYQ PYHLATRQPA RGQIHGFRMS
     LWYEHLGMLE DVFQRPESVE CVQKVNEVAE KYWDLYSSDD LEQDLPGHLL SYPIGVTADG
     SVTELPGMEN FPDTRARVLG NKSDYLPPIL TT
//