ID A0A0V0XH18_TRIPS Unreviewed; 1065 AA.
AC A0A0V0XH18;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
GN Name=Plcg1 {ECO:0000313|EMBL:KRX87277.1};
GN ORFNames=T4E_6509 {ECO:0000313|EMBL:KRX87277.1};
OS Trichinella pseudospiralis (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX87277.1, ECO:0000313|Proteomes:UP000054815};
RN [1] {ECO:0000313|EMBL:KRX87277.1, ECO:0000313|Proteomes:UP000054815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS141 {ECO:0000313|EMBL:KRX87277.1};
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|RuleBase:RU361133};
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:KRX87277.1}.
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DR EMBL; JYDU01000296; KRX87277.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0XH18; -.
DR STRING; 6337.A0A0V0XH18; -.
DR Proteomes; UP000054815; Unassembled WGS sequence.
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; cd09932; SH2_C-SH2_PLC_gamma_like; 1.
DR CDD; cd00174; SH3; 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; 2.
DR Gene3D; 3.30.505.10; SH2 domain; 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR035023; PLC-gamma_C-SH2.
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 InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR10336:SF159; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA; 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 Pfam; PF00017; SH2; 2.
DR Pfam; PF07653; SH3_2; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00239; C2; 1.
DR SMART; SM00148; PLCXc; 1.
DR SMART; SM00149; PLCYc; 1.
DR SMART; SM00252; SH2; 2.
DR SMART; SM00326; SH3; 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 SUPFAM; SSF55550; SH2 domain; 2.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
DR PROSITE; PS50001; SH2; 2.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000256|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU361133};
KW Reference proteome {ECO:0000313|Proteomes:UP000054815};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Signal {ECO:0000256|SAM:SignalP};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1065
FT /note="Phosphoinositide phospholipase C"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006872546"
FT DOMAIN 386..451
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 484..573
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 599..662
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 682..738
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 739..839
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 833..968
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1007..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1010..1032
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1065 AA; 122598 MW; 73437B5D84FDC52B CRC64;
MRFEVNFILS LILVPLKLMK PFIQQRLQCR IPSKSFLEIV NGNSNFEAFV LAYRRLVYRH
SLFSCSFFSY SVDGEKVFLD GFRRFLLREQ NDKMAECKEK CRLFMCQYLR GIYPPRDEDN
PYLTIQEFVD FLFSKQNSIF DPVHENITQS MWHPLCDYWI ASSHNTYLTG DQLKSESSLE
AYARALMMNC RCVELDCWDG QKRGLSELDI VIYHGYTMTT KLSLRDVLRT IKEYAFVQSE
YPVILSVEDN CTLPYQRQLH KKLPVEQDDV VNGLNSNCFL DDPFRDTDAL SNPDILKKGI
LYIKEKDLEE WHPHIFLLFP DRIYFTRNVD TTLGQRYNKT ATAEEDADKI EELKDISSPS
SSCEQDDTEE GKINFNADEL HLTEEWFHGR ISRDQAVEIL KEHSHLGKGL FLVRESSTFV
GDHSLSLLYN DTVHHCRIKS TQIAGTKHYY LVEAKKQNYL VTPKFRAKLK IPCPQPCPHI
GEPWFHAELD RQKAEEMLNA YPLDGAFLIR TSSSGDRSFI LSFRVDGHIK HCRLKQEGRL
FVVCDHQFEN FNWLVDYYGK NELYHGISLK YPVNAETIEK YASEVSHAPS GSYMDLNSDG
KTIARARCDY VASNESELSF PMNAWITVQR IEDEQWYGRM LRGIYKGKVG LVPRDQVELI
PSSLTKPLLP NDSNYNLQEF DSINLSTCSI EELDVSRPFV FNVRENTSND TTAREIIVAA
NSRDDQIDWI NSILEVSRSL TEKANSVKTK EKCLRIAREL SDIMVYCQAI PFNRHQLSRV
YPNACRLTSS NFNPIPMWNA GCQMVALNYQ TPDKFMQLNQ ARFLANGKCG YVLKPEFMRN
ESYDPNLPES VLGSRAILLT IEVIAGRHLY RKDRCKGIVS PVVEVEIVGL PFDCQAYRTS
RLFLACDGLH PIWNEHFEFN VKCPEAALLR FYVEDGDLVY PSGEPVIAQA TFPLNCIRTG
YRSVNLKNEY SEELELSALL LHIDIQEQEE VQLSEIPEHI LEAIEKTKNK GTLTKSPPAD
SSSSSMANRL ESIANPSAVP KKKLSANSIK RMFKMSLSKN ASDRV
//
