ID F6GUR2_VITVI Unreviewed; 588 AA.
AC F6GUR2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
GN OrderedLocusNames=VIT_06s0004g06660 {ECO:0000313|EMBL:CCB43475.1};
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760 {ECO:0000313|EMBL:CCB43475.1, ECO:0000313|Proteomes:UP000009183};
RN [1] {ECO:0000313|Proteomes:UP000009183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX PubMed=17721507; DOI=10.1038/nature06148;
RG The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA Wincker P.;
RT "The grapevine genome sequence suggests ancestral hexaploidization in major
RT angiosperm phyla.";
RL Nature 449:463-467(2007).
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; FN594951; CCB43475.1; -; Genomic_DNA.
DR RefSeq; XP_002278527.1; XM_002278491.4.
DR AlphaFoldDB; F6GUR2; -.
DR STRING; 29760.F6GUR2; -.
DR PaxDb; 29760-VIT_06s0004g06660-t01; -.
DR EnsemblPlants; Vitvi06g00648_t001; Vitvi06g00648_P001; Vitvi06g00648.
DR GeneID; 100255373; -.
DR Gramene; Vitvi06g00648_t001; Vitvi06g00648_P001; Vitvi06g00648.
DR KEGG; vvi:100255373; -.
DR eggNOG; KOG0169; Eukaryota.
DR HOGENOM; CLU_002738_3_2_1; -.
DR InParanoid; F6GUR2; -.
DR OrthoDB; 882863at2759; -.
DR Proteomes; UP000009183; Chromosome 6.
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:UP000009183};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 353..439
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 434..570
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 259..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 588 AA; 66978 MW; 625CF032350D4DC7 CRC64;
MGSYRVCMCF RRKFRVVEAE PPEDVKEAFK KYAEGGTHMT AEQLRRFLLE SQSDGSVTLS
DAERIVEQVL QKRHHIAKFT RHNLTLDDFH HFLFSTDLNA PIGSQVHQDM NAPLSHYFIY
TGHNSYLTGN QLSSDCSDVP VIKALKRGVR VIELDIWPDS TKADVHVLHG RTLTTPVELI
KCLRSIKEHA FSASPYPVII TLEDHLTPDL QAKVAQMVTQ TFQDILFYPK SECLQEFPSP
EELKYRIIIS TKPPKEYLEA KGSEDKENNI QKGKDSDDDV WGEEPSNITA DHENNDKSDS
EGSEVDEDGE ENNDCRPIGA PAYKHLISIH AGKPKGGFKD ALKVEPNKVR RLSLSEQALE
KATASHGTDV VRFTQKNFLR IYPKGTRFNS SNYKPLIGWT HGAQMVAFNM QGYGRYLWLM
HGMFRANGGC GYVKKPDFLM NVGPNNQVFN PRVKLPVKKT LKVKVYMGDG WHLDFKQTHF
DLYSPPDFYA RVGIAGVPGD EVMKKTKTKE DKWTPVWNEE FQFPLTVPEL ALLRVEVHEY
DLSEKDDFAG QTCLPISELK PGIRAVPLFN RKGEMFCSAR LLMRFEFV
//
