ID A0A1I8HQA2_9PLAT Unreviewed; 597 AA.
AC A0A1I8HQA2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 22-FEB-2023, entry version 25.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0007295-snap-gene-0.8-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0007295-snap-gene-0.8-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) 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|RuleBase:RU361133};
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DR AlphaFoldDB; A0A1I8HQA2; -.
DR WBParaSite; maker-uti_cns_0007295-snap-gene-0.8-mRNA-1; maker-uti_cns_0007295-snap-gene-0.8-mRNA-1; maker-uti_cns_0007295-snap-gene-0.8.
DR Proteomes; UP000095280; Unplaced.
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; cd08558; PI-PLCc_eukaryota; 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; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336:SF6; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE EPSILON-1; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR Pfam; PF00168; C2; 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 Hydrolase {ECO:0000256|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361133};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 380..470
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 476..597
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 295..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..321
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 597 AA; 66048 MW; A4375DA10C826106 CRC64;
SKLTVAKAKA SLSPLAQRAQ ICNAVAVSSI TANSAGLDLG HGAATVMGQK EIASFLELQQ
EDVSPLTPAE VVDRFEQSAD FKLKGFLSFE GFCAFLQDTR NFAAPVEQNK WKEEIMDHPL
SHYFIASSHN TYLCGHQLKG ESSVDMYRQV LLTGCRCIEL DCHDGENGSP VIYHGMTLTS
KIAFESAVEA INQFAFVKSP LPLVLSIENH CSLPQQQKMA AIFLRIFGDR LVKNFLFESD
HDDDPYLPSP NQLKEKILIK NKKLSTGIVS GVVSAGSGIS SVTRTVGGRA WVLKNQNSDS
GVPEDDEQFD EEDDEFDFEE EKKDSPDTPH PPGTKKPTIR RSILQSVHTN ERLSDAVVQA
QAAAKARAAV GPNATTPLAH QVTSMKETSA KQVFRRFPTA NVPCSEKQLQ RVYPGGMRID
SSNPNPISFW CFGSQMVALN YQTEDVSLII NQALFESTGN CGYVLKPEVM WNKLHPLHSR
FNPLDKDFDN IPAAIVSLQI ISGQFLCLSN PTAGLMVELE VQGLPHDCAK FKTPISNRNS
LNPIWYETFR FQLHFSELAF LRFTVIEVSS YHTVAQRTIL LSELRKGSLS CCNNSPQ
//
