ID A0A9R1VX19_LACSA Unreviewed; 861 AA.
AC A0A9R1VX19;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 18-JUN-2025, entry version 11.
DE RecName: Full=Phospholipase D {ECO:0000256|PIRNR:PIRNR036470};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR036470};
GN ORFNames=LSAT_V11C400192390 {ECO:0000313|EMBL:KAJ0212063.1};
OS Lactuca sativa (Garden lettuce).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Cichorioideae; Cichorieae;
OC Lactucinae; Lactuca.
OX NCBI_TaxID=4236 {ECO:0000313|EMBL:KAJ0212063.1, ECO:0000313|Proteomes:UP000235145};
RN [1] {ECO:0000313|EMBL:KAJ0212063.1, ECO:0000313|Proteomes:UP000235145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Seedlings {ECO:0000313|EMBL:KAJ0212063.1};
RX PubMed=28401891; DOI=10.1038/ncomms14953;
RA Reyes-Chin-Wo S., Wang Z., Yang X., Kozik A., Arikit S., Song C., Xia L.,
RA Froenicke L., Lavelle D.O., Truco M.J., Xia R., Zhu S., Xu C., Xu H.,
RA Xu X., Cox K., Korf I., Meyers B.C., Michelmore R.W.;
RT "Genome assembly with in vitro proximity ligation data and whole-genome
RT triplication in lettuce.";
RL Nat. Commun. 8:14953-14953(2017).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAJ0212063.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NBSK02000004; KAJ0212063.1; -; Genomic_DNA.
DR Proteomes; UP000235145; Chromosome 4.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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 FunFam; 3.30.870.10:FF:000027; Phospholipase D; 1.
DR FunFam; 3.30.870.10:FF:000025; Phospholipase D delta; 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:SF162; PHOSPHOLIPASE D; 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; 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|ARBA:ARBA00022837, 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:ARBA00023098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000235145};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 41..177
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 378..416
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 706..733
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 861 AA; 97842 MW; E09A63901255600C CRC64;
MGFPAGGSDG NLRCRSVFRD EFERMKIATK RNYKDDITAK KILRTKRCAG YKMSKVLLHG
TLHVTIYEVD KLHEGGGPNV FGKLMANIQE TVGFGEGTPK IYATIDLEKC RVGRTRMIEN
EPQNPRWYES FHIYCAHSAS DVIFTVKDNN PIGATLIGRA HMPVRELMDG DEVDKWIEIM
DENNNPVPAG SKIHVKLQFF DVTQDRNWAH GIKNAKYPGV PYTFFAQRTG CRVSLYQDAH
VPENFMPKIA LAGGKYYETH RCWEDIFEAI TNAKHFIYIT GWSVYTEIAL IRDPKRQKDG
GDVMLGQILK RKAEEGVRVA MLVWDDRTSV NVFKEDGLMA THDEETENFF QNTDVHCILC
PRDPDDGGSV FQDLQVSTMF THHQKIVVVD AEMPTGGSEK RRVVSFVGGI DLCDGRYDYA
FHPLFKTLNA AHHDDFHQPN YTGASIAKGG PREPWHDIHS RVEGPIAWDV LFNFEQRWRK
QGGKNILVDL RQLRDILIPP SPVTFPNDQE TWNVQLFRSI DGGAAFGFPD TPEEAGKAGL
VSGKDNIIDR SIQDAYINAI RRAKNFIYIE NQYFLGSSFA WKSDDINVNE IGALHLIPKE
LSLKIVSKIE AGQKFIVYVV VPMWPEGIPE SGSVQAILDW QKRTMEMMYK DIVKALQDKG
RDDDPREYLT FFCLGNREMK QDDEHEPTEA PEPDSGYLHA QENRRFMIYV HSKMMIVDDE
YIIVGSANIN QRSMDGARDS EIAMGAYQPN HLASARSPAR GQIHGFRMAL WYEHLGMIDQ
TFEHPENVEC VRKVNDVADK CWELYASENL ERDLPGHLLR YPVGIARDGD ITELPGTECF
PDTSAKILGT KSDFLPPILT T
//
