ID A0A3Q7FU23_SOLLC Unreviewed; 768 AA.
AC A0A3Q7FU23;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
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:Solyc03g121470.3.1};
RN [1] {ECO:0000313|EnsemblPlants:Solyc03g121470.3.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc03g121470.3.1};
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:Solyc03g121470.3.1}
RP IDENTIFICATION.
RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc03g121470.3.1};
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 AlphaFoldDB; A0A3Q7FU23; -.
DR STRING; 4081.A0A3Q7FU23; -.
DR EnsemblPlants; Solyc03g121470.3.1; Solyc03g121470.3.1; Solyc03g121470.3.
DR Gramene; Solyc03g121470.3.1; Solyc03g121470.3.1; Solyc03g121470.3.
DR InParanoid; A0A3Q7FU23; -.
DR OMA; EFEPSWG; -.
DR Proteomes; UP000004994; Chromosome 3.
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; cd00030; C2; 1.
DR CDD; cd09142; PLDc_pPLD_like_2; 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; IPR025202; PLD-like_dom.
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:SF137; PHOSPHOLIPASE D ALPHA 4; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF12357; PLD_C; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR PIRSF; PIRSF036470; PLD_plant; 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..123
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 308..345
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 615..642
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 768 AA; 88596 MW; DFD94E61646141B4 CRC64;
MEGKHKFFHG TLEVSIFRAT SRKSSLPFKC ISSNGKPAFV TIKIDNKTVA KTTQESDRVW
NQTFQILCAH SPDTTVTITL KTKCSILGKF TIQANKLLNE TSLIEGFFPL SIENKKPKKK
LKLQFIVWFK PAENEPSWGR ILENGAFTGL KNSTFPQRSN CSVTLYQDAH HQHTFQPPFQ
TRPKNLWEDI YRAIEDAKHL VYIAGWSFSP KMVLVKLDLR PNVDFLDMVR DPSAEITHAK
GVKLGELLKR KAEEGVAVMI MLWDDETSLP IIKNKGVMRT HDEDSLAYFR DTKVVCKLVP
RLHHKLPSFF AHHQKMIAVD SRSHLSSTSR EITSFLGGLD LCDGRYDTEE HSLFRTLNTE
SHCYDFYQTS LSGASLHKGG PREPWHDAHA RVTGQAAMDV LNNFEQRWNK QIGPSLLIPI
RSIPELSNQP NMASTDRDWN VQVFRSIDHV SACPLPRNMT VERSIHEAYV EAIRRADRFI
YIENQYFIGG CHLWEQDQHC GCRNLIPIEI ALKIVNKIRA KERFSVYIVI PMWPEGLPES
DSVQDILYWT RETMKMMYKF IGEAIKESGE QGHPRDYLNF FCLANREEKI KGEFAPPYSP
HPESQYWRAQ KNRRFMVYVH SKIMIVDDTY LLIGSANINQ RSMDGKRDTE IAIGCYQSKT
EEDIDQRDIH AYRMSLWYEH TGQAEQEFQH PQSLECVNRI RSIGDKMWKI YDQDKLEDMK
GVHLVTYPVN VTAEGHVEDL MERNGHFPDT EAPIKGKRSK VLAPTITT
//
