PLDA1_MAIZE
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 03-AUG-2022, entry version 111.
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; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Missouri 17;
RX PubMed=7551587; DOI=10.1093/oxfordjournals.pcp.a078837;
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 mays
RT 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:
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; Evidence={ECO:0000250};
CC -!- SUBUNIT: Monomer. {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 -!- SIMILARITY: Belongs to the phospholipase D family. C2-PLD subfamily.
CC {ECO:0000305}.
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DR EMBL; D73410; BAA11135.1; -; mRNA.
DR PIR; T03659; T03659.
DR RefSeq; NP_001105686.1; NM_001112216.1.
DR AlphaFoldDB; Q43270; -.
DR SMR; Q43270; -.
DR STRING; 4577.GRMZM2G054559_P01; -.
DR PaxDb; Q43270; -.
DR PRIDE; Q43270; -.
DR GeneID; 542702; -.
DR KEGG; zma:542702; -.
DR MaizeGDB; 113853; -.
DR eggNOG; KOG1329; Eukaryota.
DR OrthoDB; 128697at2759; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; Q43270; baseline and differential.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
DR GO; GO:0009395; P:phospholipid catabolic process; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Calcium; Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding;
KW Reference proteome; Repeat.
FT CHAIN 1..812
FT /note="Phospholipase D alpha 1"
FT /id="PRO_0000218820"
FT DOMAIN 1..130
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 330..368
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT DOMAIN 658..685
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 335
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 337
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 342
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 663
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 665
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 670
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 335
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 374
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 408
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 524
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 663
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 724
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
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
