ID M5WLT0_PRUPE Unreviewed; 587 AA.
AC M5WLT0;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
GN ORFNames=PRUPE_6G056800 {ECO:0000313|EMBL:ONH99903.1};
OS Prunus persica (Peach) (Amygdalus persica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=3760 {ECO:0000313|EMBL:ONH99903.1, ECO:0000313|Proteomes:UP000006882};
RN [1] {ECO:0000313|EMBL:ONH99903.1, ECO:0000313|Proteomes:UP000006882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX PubMed=23525075; DOI=10.1038/ng.2586;
RA Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F.,
RA Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A.,
RA Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V.,
RA Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G., Dondini L.,
RA Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C., Aramini V., Copetti D.,
RA Gonzalez S., Horner D.S., Falchi R., Lucas S., Mica E., Maldonado J.,
RA Lazzari B., Bielenberg D., Pirona R., Miculan M., Barakat A., Testolin R.,
RA Stella A., Tartarini S., Tonutti P., Arus P., Orellana A., Wells C.,
RA Main D., Vizzotto G., Silva H., Salamini F., Schmutz J., Morgante M.,
RA Rokhsar D.S.;
RT "The high-quality draft genome of peach (Prunus persica) identifies unique
RT patterns of genetic diversity, domestication and genome evolution.";
RL Nat. Genet. 45:487-494(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-
CC diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456,
CC ChEBI:CHEBI:203600; EC=3.1.4.11;
CC Evidence={ECO:0000256|ARBA:ARBA00001195,
CC ECO:0000256|RuleBase:RU361133};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
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DR EMBL; CM007656; ONH99903.1; -; Genomic_DNA.
DR RefSeq; XP_007206576.1; XM_007206514.1.
DR AlphaFoldDB; M5WLT0; -.
DR STRING; 3760.M5WLT0; -.
DR EnsemblPlants; ONH99903; ONH99903; PRUPE_6G056800.
DR GeneID; 18772015; -.
DR Gramene; ONH99903; ONH99903; PRUPE_6G056800.
DR KEGG; pper:18772015; -.
DR eggNOG; KOG0169; Eukaryota.
DR HOGENOM; CLU_002738_3_2_1; -.
DR OMA; LAVYCHA; -.
DR OrthoDB; 882863at2759; -.
DR Proteomes; UP000006882; Chromosome g6.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IBA:GO_Central.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IBA:GO_Central.
DR CDD; cd00275; C2_PLC_like; 1.
DR CDD; cd08599; PI-PLCc_plant; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR015359; PLC_EF-hand-like.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336:SF204; PHOSPHOINOSITIDE PHOSPHOLIPASE C 4-RELATED; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF09279; EF-hand_like; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR SMART; SM00239; C2; 1.
DR SMART; SM00148; PLCXc; 1.
DR SMART; SM00149; PLCYc; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000256|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361133};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Reference proteome {ECO:0000313|Proteomes:UP000006882};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
SQ SEQUENCE 587 AA; 67199 MW; 5BBC14995089C3ED CRC64;
MGSYRMCMCF TRKFRVTEAE PPLDVKEAFN KYAEGGTHMT AEQLQNFLLE FQADGGVGGG
AEASDAERIV EQVLQKRHHI AKLISRRTLT LDDFHHYLFS PDLNPPIRDQ VHQDMTAPLS
HYYIYTGHNS YLTGNQLSSD CSDVPIIKAL KRGVRVVELD IWPNSTKDNV HVLHGRTLTT
PVELIKCLKS IQEHAFSESP YPVIITLEDH LTPDLQAKVA QMLIETFGEM LFYPESDCLK
ELPSPEELKY RIIISTKPPE EYRKAKTANE KEHDSHKSEE DLWGKEPSEL TEEHEDDDMS
DSDSSEDNSH SNRGSFSSAE HEYKRLITIH AGKPKGGLKE ALKVELDKVR RLSLSEQALE
KAAESHGTDV VRFTQKNILR VYPKGTRFNS SNYKPLIGWM HGAQMVAFNM QGYGRSLWLM
HGMFRANGGC GYVKKPDFIM NESDNQIFDP KAKLPVKKTL KVKVYMGDGW HLDFKQTHFD
LYSPPDFYTR VGIAGVPADE IMKKTKKKED DWTPVWEEEF TFPLRVPELA LLRVEVHEYD
MSEKDDFGGQ TCLPVSELRQ GIRAVPLFDR KGTKYNSVRL LMQFEFI
//
