ID A0A0V0S150_9BILA Unreviewed; 624 AA.
AC A0A0V0S150;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
GN Name=plcd3a {ECO:0000313|EMBL:KRX20367.1};
GN ORFNames=T07_13795 {ECO:0000313|EMBL:KRX20367.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX20367.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX20367.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX20367.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX20367.1}.
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DR EMBL; JYDL01000049; KRX20367.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0S150; -.
DR Proteomes; UP000054630; 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; 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; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
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:SF210; PHOSPHOINOSITIDE PHOSPHOLIPASE C; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 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; 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; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361133};
KW Reference proteome {ECO:0000313|Proteomes:UP000054630}.
FT DOMAIN 139..165
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 458..554
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT COILED 119..146
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 624 AA; 71286 MW; 4F26E598BF42DB12 CRC64;
MDRQTNTDLV NVETTMRRVK NNGLVASSPL ILKLAADQRH IIYFDNACFK TSKTASLSKA
LEVRSGWNTD VFHKAMKSKT FVTQVNESAC FSIIFRHPIR HFKSLNLICE DAQTRHNWVH
FLTEAIEKLK EEHADLRQFK KADKNRNGYL TFEETWNLLL SLNLELDKQI ARKTFEKSDF
RKEGPSADAL DFDEFHHFFR FLTDRPDLRD IIRQLSEFHE EFFTVEDLKN FLTNIQQLSA
VTLSHCRQLI RRYEPEPENQ KSLKLSFHGL RRLLLSEAGN IVKPEHRVIY QNMEKPLTDY
YIYSTHNTYL CGHQLMGDAT IEGYILALKK GARLLELDIW PGENDLQVTH GHTLVKPVSL
SVVLKAINNY GFSTTPYPII LSLEIHCDIR KQAILADMLV KTFGKKLHKN VAHLKTLPSP
EELKNKILLK GKGGLAKELA ALIAIVSAKL VNPLVDLERH PVNSMASKSE DQLIAMVEEN
QPAMVKYTSQ HLVKCYPRGT RTSSTNMNPV VYWLAGIQSV CLNVQTADLA NDLNTAMFSI
NGNCGYVLKP DCLQNKESST EQQVKKMIVR VWIIILSANF LPKPSTTTSK EDVIDPYVKV
ETFGMPSDRV KYRTAVIRNN GNVK
//
