ID A0A3Q7JSX4_SOLLC Unreviewed; 820 AA.
AC A0A3Q7JSX4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 23.
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};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081 {ECO:0000313|EnsemblPlants:Solyc12g011170.2.1};
RN [1] {ECO:0000313|EnsemblPlants:Solyc12g011170.2.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc12g011170.2.1};
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
RN [2] {ECO:0000313|EnsemblPlants:Solyc12g011170.2.1}
RP IDENTIFICATION.
RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc12g011170.2.1};
RG EnsemblPlants;
RL Submitted (JAN-2019) 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 RefSeq; XP_004251821.1; XM_004251773.2.
DR AlphaFoldDB; A0A3Q7JSX4; -.
DR STRING; 4081.A0A3Q7JSX4; -.
DR PaxDb; 4081-Solyc12g011170-1-1; -.
DR EnsemblPlants; Solyc12g011170.2.1; Solyc12g011170.2.1; Solyc12g011170.2.
DR GeneID; 101264185; -.
DR Gramene; Solyc12g011170.2.1; Solyc12g011170.2.1; Solyc12g011170.2.
DR KEGG; sly:101264185; -.
DR InParanoid; A0A3Q7JSX4; -.
DR OMA; RIYCAHT; -.
DR OrthoDB; 3014064at2759; -.
DR Proteomes; UP000004994; Chromosome 12.
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:SF169; 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:UP000004994}.
FT DOMAIN 1..135
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 335..373
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 665..692
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 820 AA; 93433 MW; 6924C08B6FAAC65C CRC64;
MVPRLLHGTL HATIYEIDKI RTGCADCCGP TSPQKLTKRV LNNVKKLFFC APKISATKLY
ATIDLDKARV GRTRIAENEP SNPHWNDTFR LYCAHEVSNI IFTVKDENPV SATLIGRAYL
PVEEVLNRYI VDRWVPIVDE ERHPISGHSK IHVRLQFYSV KQDSNWSRGI TSLAFGGLPY
TFFKERQGCQ VTLYPDADIS DDDITNYLKS QGLFEPQRCW EDIFDAISNA KHMIYIAGWS
VYTKITLIRN PRRPKVGGEL TLGELLKKKA SEGVNVLLLV WDDITSDEVL KRDGLMSTHD
QETADYFKNT DVHCCLCPRN ADSGKTVIQG FQVGTMFTHH QKTIVVDTEI PGGMSHKRMI
VSFLGGIDLC DGRYDTRDHS LFRTLDTVHK QDFYQPAFPG SSIAKGGPRE PWHDIHCRLE
GPVAWDVLYN FEQRWRKQIG NRFIYSINEL DKFIIRPTEV TASRDRETWN VQIFRSIDGG
AVTDFPVKPD EASEVGLVTG KNNVIDQSIH DAYISAIRRA KNFIYIENQY FIGSCYGWKP
TTDIKLEDIG ALHLIPKEIS LKIVSKIQAG ERFTVYVVLP MWPEGIPESD SVQAILDWQK
RTMEMMYTDI CNALKAKGNT NADPREYLTF FCLGNREVEK PGEYKPPQKP VPDTNYARAQ
EFRRFMIYVH SKMMIVDDEY IIIGSANINQ RSMDGARDSE IAMGGYQPYH LASNQPPRGK
IYGFRMSLWC EHLNYADDSF ADPSSLECVR KVNGMADESW KLYSNDTFDI DLPGHLLRYP
IDINSNTGQI TTLPGFKFFP DTKAAILGNK SQFLPPILTT
//
