ID A0A3P9QNB2_VIGRR Unreviewed; 591 AA.
AC A0A3P9QNB2;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|ARBA:ARBA00012368, ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|ARBA:ARBA00012368, ECO:0000256|RuleBase:RU361133};
GN Name=LOC106757831 {ECO:0000313|RefSeq:NP_001304243.1};
GN Synonyms=PLC {ECO:0000313|RefSeq:NP_001304243.1}, plc3
GN {ECO:0000313|RefSeq:NP_001304243.1}, plc4
GN {ECO:0000313|RefSeq:NP_001304243.1};
OS Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:NP_001304243.1};
RN [1] {ECO:0000313|RefSeq:NP_001304243.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; NP_001304243.1; NM_001317314.1.
DR AlphaFoldDB; A0A3P9QNB2; -.
DR STRING; 3916.A0A3P9QNB2; -.
DR KEGG; vra:106757831; -.
DR OrthoDB; 882863at2759; -.
DR Proteomes; UP000087766; Chromosome 3.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:UniProtKB-EC.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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:SF36; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA PLC-3; 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:UP000087766};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 356..442
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 444..573
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 258..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 591 AA; 67306 MW; 9DFA9EE222C6BB73 CRC64;
MSKQTYSLCF CLRRRFSLPV SEAPPEIRTL FDRYSDENGI MTASHVRGFL VEVQKEESVT
EEEAQAIIDG HKHLSIFHRR GLNLESFFNY LFSSNNNPPL SPSLGVHQDM SSPLSHYFIY
TGHNSYLTGN QLSSDCSDVP IIKALQKGVR VIELDIWPNE SKDDVDVLHG RTLTSPVALI
KCLRSIKQYA FVASEYPVVI TLEDHLTPDL QAKVAEMITQ TFGDILFSPG SESLKEFPSP
KSLKRRIIIS TKPPKEYIEA KEVQEKGEGS QKEKPVDDEE AWGKEVPSLR GGTISDHKNI
EDEDDLDNED DTDEAEYSRQ NASDEYRRLI AIHAGKPKGG LTECLKVDPD TVKRLSLSEL
QLEKAAETHG KEIIRFTQRN ILRVYPKGTR IASTNYNPLI GWMHGAQMVA FNMQGYGRSL
WLMQGMFKAN GGCGYVKKPD FLLKTGLNNE VFDPKARLPV KKTLKVTIYM GEGWFHDFKH
THFDQYSPPD FYARVGIAGV PYDTVMKKTK SVEDNWSPSW NEEFKFPLSV PELALLRVEV
HEYDMSEKDD FGGQTCLPVW ELRSGIRAVP LYSRKGEKYH NVKLLMRFEF I
//
