ID A0A1U8AIC0_NELNU Unreviewed; 861 AA.
AC A0A1U8AIC0;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Phospholipase D {ECO:0000256|ARBA:ARBA00012027, ECO:0000256|PIRNR:PIRNR036470};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027, ECO:0000256|PIRNR:PIRNR036470};
GN Name=LOC104604314 {ECO:0000313|RefSeq:XP_010266912.1};
GN ORFNames=HUJ06_016631 {ECO:0000313|EMBL:DAD46694.1};
OS Nelumbo nucifera (Sacred lotus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Proteales; Nelumbonaceae; Nelumbo.
OX NCBI_TaxID=4432 {ECO:0000313|Proteomes:UP000189703, ECO:0000313|RefSeq:XP_010266912.1};
RN [1] {ECO:0000313|EMBL:DAD46694.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:DAD46694.1};
RX PubMed=32343808;
RA Shi T., Rahmani R.S., Gugger P.F., Wang M., Li H., Zhang Y., Li Z.,
RA Wang Q., Van de Peer Y., Marchal K., Chen J.;
RT "Distinct Expression and Methylation Patterns for Genes with Different
RT Fates following a Single Whole-Genome Duplication in Flowering Plants.";
RL Mol. Biol. Evol. 37:2394-2413(2020).
RN [2] {ECO:0000313|RefSeq:XP_010266912.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal
CC phosphodiesteric bond. {ECO:0000256|PIRNR:PIRNR036470}.
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 Evidence={ECO:0000256|ARBA:ARBA00000798,
CC ECO:0000256|PIRNR:PIRNR036470};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913,
CC ECO:0000256|PIRNR:PIRNR036470};
CC -!- SIMILARITY: Belongs to the phospholipase D family. C2-PLD subfamily.
CC {ECO:0000256|ARBA:ARBA00010683, ECO:0000256|PIRNR:PIRNR036470}.
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DR EMBL; DUZY01000008; DAD46694.1; -; Genomic_DNA.
DR RefSeq; XP_010266912.1; XM_010268610.2.
DR STRING; 4432.A0A1U8AIC0; -.
DR GeneID; 104604314; -.
DR KEGG; nnu:104604314; -.
DR eggNOG; KOG1329; Eukaryota.
DR OrthoDB; 3014064at2759; -.
DR Proteomes; UP000189703; Unplaced.
DR Proteomes; UP000607653; Unassembled WGS sequence.
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 CDD; cd04015; C2_plant_PLD; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
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; PHOSPHOLIPASE D; 1.
DR PANTHER; PTHR18896:SF60; PHOSPHOLIPASE D; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF12357; PLD_C; 1.
DR Pfam; PF00614; PLDc; 1.
DR PIRSF; PIRSF036470; PLD_plant; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50035; PLD; 2.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRNR:PIRNR036470};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR036470};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR036470};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR036470};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000189703}.
FT DOMAIN 12..158
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 363..398
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 707..734
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 861 AA; 97059 MW; BFB8E43A95E1D41A CRC64;
MASNSDGNLQ VPASMANNNP SDQIIYLHGD LDLKILGARS LPNMDLLFER CRRCFTVCGT
CLHPAAPKQP RDQEHRKMIT SDSYVTVSLS GATVARTRVI PNSENPQWNE EFNIPLAHPA
AHVEFHVKDN DMFGAQVIGV VSIPAQRIKS GELISEWFSV IGPSGKPPKP NSALNLEMKF
TPIESNPLYR HGIAADPKHL GVRDTYFPVR KGGSVTLYQD AHVPDGMLPE IKLENGEVFR
HNKCWGDICH AILEAHHLVY IVGWSVYHKV KLVRESTRPL PSGGDLTLGE LLKYKSQEGV
RVLLLLWDDK TSHSNILINT AGVMETHDEE TRKFFKHSSV ICVLAPRYAS SKLSIVKQQV
VGTLFTHHQK CVLVDTQASG NNRKITAFIG GLDLCVGRYD TPEHRLFSDL DTVFRDDYHN
PTFPAETKGP RQPWHDLHCK IEGPAAYDVL KNFEQRWRKA TKWTEFGKRF KRVSRWDDDA
LIKLERISWI LSPSPYIAND DPILWVSKEG DAENWHVQVF RSIDSGSVKG FPTKDVQLAH
DQKLICEKNL VIDKSIQTGY VQAIRSAQHF IYIENQYFLG SSYGWPSYKN AGADNLIPME
LALKIASKIR VKERFAVYIV IPMWPEGFPT DASVQEILYW QGQTMQMMYE VVAKELKSMQ
LENSYPQDYL NFYCLGNREQ IPKDIPESIS SSTNGGAASA AQKNRRFMIY VHAKGMIVDD
EYVILGSANI NERSMSGARD TEIAMGAYQP HHTWAVKKKH PHGQVYGYRM SLWAEHLGVV
NESFLEPQRL ECVRTVNGIA EDNWKKFTAE EVTPLCGHLL KYPILVEADG KVSPLPGHEN
FPDVGGKVLG SYTSLPDALT T
//