ID E3M7D9_CAERE Unreviewed; 751 AA.
AC E3M7D9;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 88.
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=Cre-plc-4 {ECO:0000313|EMBL:EFO93863.1};
GN ORFNames=CRE_12711 {ECO:0000313|EMBL:EFO93863.1}, FL82_04079
GN {ECO:0000313|EMBL:OZF97814.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|EMBL:EFO93863.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|EMBL:EFO93863.1};
RG The Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:OZF97814.1, ECO:0000313|Proteomes:UP000216624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX439 {ECO:0000313|EMBL:OZF97814.1,
RC ECO:0000313|Proteomes:UP000216624};
RA de Groot N.N.;
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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:ARBA00023674};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC Evidence={ECO:0000256|ARBA:ARBA00023674};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR EMBL; DS268427; EFO93863.1; -; Genomic_DNA.
DR EMBL; NMWX01000006; OZF97814.1; -; Genomic_DNA.
DR RefSeq; XP_003107964.1; XM_003107916.1.
DR AlphaFoldDB; E3M7D9; -.
DR STRING; 31234.E3M7D9; -.
DR EnsemblMetazoa; CRE12711.1; CRE12711.1; WBGene00071958.
DR eggNOG; KOG0169; Eukaryota.
DR HOGENOM; CLU_002738_0_2_1; -.
DR InParanoid; E3M7D9; -.
DR OMA; YLTCTLV; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000008281; Unassembled WGS sequence.
DR Proteomes; UP000216624; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; cd16202; EFh_PI-PLCdelta; 1.
DR CDD; cd08558; PI-PLCc_eukaryota; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR039504; PLC-delta3_EF-hand.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336:SF210; PHOSPHOINOSITIDE PHOSPHOLIPASE C; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF14788; EF-hand_10; 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; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU361133};
KW Reference proteome {ECO:0000313|Proteomes:UP000008281};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 26..146
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 156..191
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 523..608
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 604..729
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 751 AA; 86020 MW; CD5806F775F348C8 CRC64;
MAKNVSPEEQ AAAQAADEEK TKEELEWAEK GSLLCRIKNQ KVKEMSLVTI KSKQFLNYYS
SYWFNFVPNA LKSVALSELL EVRSGYQTDN LQRASKKYEF QELAPESRCF SVIFSHAKFL
HKSVDFCADS RETRDKWVSV LNHLISVAKH QRVVFNETAW LIDKFQQGDT NKNGLLTFDE
VWNLLKRMNL QISERYAKAI FRESELENSR DNKLNEKEFL NFFERLTDRP DLRFVMTQAS
SDNVETLTVA DLQRFLTVEQ GFENVDMKKA EQILDTFEQT VQDKQKEKLM GLMGMRRLMQ
SRWGNVFKPG NESIFQDMDQ PLTHYFVNSS HNTYLTGLQV KGEATVEGYI SALRKGARLL
ELDLFDGEHG EPVITHKRTF IESITLRNSL EAIKRTAFET SPYPVILTLE NHVGFVQQAV
MAELFKEILG DSLYIPPKDS HRHPLPSPNK LKRKFLLRGK KIILEEEIEE PDEDDSPIDK
DKHHVHPHPV APELSALIGL PSVKLSHNIY QDVNKHPFDG SPSLSENKVY TMFEAAVPIF
TYTAERLVKS YPKGLRQDSS NMHPIVSWLC GIQSVAMNFQ TAGEELDLNA GLFRINGNCG
YVLKPGCLLE GIDPRTMTKP KLKLGIGLFS AQYLPKSEPG KEIIDPYVSV QIFGIPRDET
KAKTRIIKDN GFNPEWRDNF YFTLCCPELA IIRFCVKDFD STSSNDFVGE FSIPVMSLRT
GYSQIQLNTG YQHTLDPSAS LFVRIAMEEE Y
//
