ID   PLDA1_ORYSJ             Reviewed;         812 AA.
AC   Q43007;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 2.
DT   16-JUN-2009, entry version 60.
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;
DE   Flags: Precursor;
GN   Name=PLD1; OrderedLocusNames=Os01g0172400, LOC_Os01g07760;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade;
OC   Ehrhartoideae; Oryzeae; Oryza.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=cv. Koshihikari;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Koshihikari; TISSUE=Leaf;
RA   Morioka S., Ueki J., Komari T.;
RT   "Characterization of two Distinctive genomic clones for phospholipase
RT   D from rice.";
RL   (er) Plant Gene Register PGR97-076.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   MEDLINE=22337376; PubMed=12447438; DOI=10.1038/nature01184;
RA   Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA   Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA   Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M.,
RA   Okamoto M., Ando T., Aoki H., Arita K., Hamada M., Harada C.,
RA   Hijishita S., Honda M., Ichikawa Y., Idonuma A., Iijima M., Ikeda M.,
RA   Ikeno M., Ito S., Ito T., Ito Y., Ito Y., Iwabuchi A., Kamiya K.,
RA   Karasawa W., Katagiri S., Kikuta A., Kobayashi N., Kono I.,
RA   Machita K., Maehara T., Mizuno H., Mizubayashi T., Mukai Y.,
RA   Nagasaki H., Nakashima M., Nakama Y., Nakamichi Y., Nakamura M.,
RA   Namiki N., Negishi M., Ohta I., Ono N., Saji S., Sakai K., Shibata M.,
RA   Shimokawa T., Shomura A., Song J., Takazaki Y., Terasawa K., Tsuji K.,
RA   Waki K., Yamagata H., Yamane H., Yoshiki S., Yoshihara R., Yukawa K.,
RA   Zhong H., Iwama H., Endo T., Ito H., Hahn J.H., Kim H.-I., Eun M.-Y.,
RA   Yano M., Jiang J., Gojobori T.;
RT   "The genome sequence and structure of rice chromosome 1.";
RL   Nature 420:312-316(2002).
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.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.0;
CC       Temperature dependence:
CC         Stable from 4 to 37 degrees Celsius. Activity is reduced to one
CC         third of the original level after incubation at 50 degrees
CC         Celsius for 30 minutes;
CC   -!- SUBUNIT: Monomer.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves, roots, developing seeds
CC       and cultured cells.
CC   -!- DEVELOPMENTAL STAGE: The transcript begins to emerged in seeds as
CC       early as the second day after imbibition and increased after
CC       radicle emergence on the third day. Strongly expressed in the
CC       leaves, roots and residual grain of seedling eight days after
CC       imbibition. Undetectable in mature dry seeds.
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; D73411; BAA11136.1; -; mRNA.
DR   EMBL; AB001920; BAA19467.1; -; Genomic_DNA.
DR   EMBL; AP003215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP003282; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; T03402; T03402.
DR   RefSeq; NP_001042153.1; -.
DR   UniGene; Os.155; -.
DR   GeneID; 4327647; -.
DR   KEGG; osa:4327647; -.
DR   Gramene; Q43007; -.
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   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Hydrolase; Lipid degradation;
KW   Repeat.
FT   PROPEP        1     46
FT                                /FTId=PRO_0000024655.
FT   CHAIN        47    812       Phospholipase D alpha 1.
FT                                /FTId=PRO_0000024656.
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.
FT   CONFLICT    139    139       P -> S (in Ref. 1 and 2).
SQ   SEQUENCE   812 AA;  92219 MW;  6AE267E6C8B1DC5E CRC64;
     MAQMLLHGTL HATIFEAASL SNPHRASGSA PKFIRKFVEG IEDTVGVGKG ATKVYSTIDL
     EKARVGRTRM ITNEPINPRW YESFHIYCAH MASNVIFTVK IDNPIGATNI GRAYLPVQEL
     LNGEEIDRWL DICDNNREPV GESKIHVKLQ YFDVSKDRNW ARGVRSTKYP GVPYTFFSQR
     QGCKVTLYQD AHVPDNFIPK IPLADGKNYE PHRCWEDIFD AISNAQHLIY ITGWSVYTEI
     TLVRDSNRPK PGGDVTLGEL LKKKASEGVR VLMLVWDDRT SVGLLKRDGL MATHDEETEN
     YFHGSDVNCV LCPRNPDDSG SIVQDLSIST MFTHHQKIVV VDHELPNQGS QQRRIVSFVG
     GLDLCDGRYD TQYHSLFRTL DSTHHDDFHQ PNFATASIKK GGPREPWHDI HSRLEGPIAW
     DVLYNFEQRW RKQGGKDLLL QLRDLSDTII PPSPVMFPED RETWNVQLFR SIDGGAAFGF
     PDTPEEAAKA GLVSGKDQII DRSIQDAYIH AIRRAKNFIY IENQYFLGSS YAWKPEGIKP
     EDIGALHLIP KELALKVVSK IEAGERFTVY VVVPMWPEGV PESGSVQAIL DWQRRTMEMM
     YTDITEALQA KGIEANPKDY LTFFCLGNRE VKQAGEYQPE EQPEADTDYS RAQEARRFMI
     YVHTKMMIVD DEYIIIGSAN INQRSMDGAR DSEIAMGGYQ PYHLATRQPA RGQIHGFRMA
     LWYEHLGMLD DVFQRPESLE CVQKVNRIAE KYWDMYSSDD LQQDLPGHLL SYPIGVASDG
     VVTELPGMEY FPDTRARVLG AKSDYMPPIL TS
//