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Database: UniProt
Entry: A0A1U8AIC0_NELNU
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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
//
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