ID A0A0B2V3G2_TOXCA Unreviewed; 1471 AA.
AC A0A0B2V3G2;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=PLCB4 {ECO:0000313|EMBL:KHN75550.1};
GN ORFNames=Tcan_11690 {ECO:0000313|EMBL:KHN75550.1};
OS Toxocara canis (Canine roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN75550.1, ECO:0000313|Proteomes:UP000031036};
RN [1] {ECO:0000313|EMBL:KHN75550.1, ECO:0000313|Proteomes:UP000031036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN75550.1};
RA Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA Gasser R.B.;
RT "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL Submitted (NOV-2014) 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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR000956-2};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR000956-2};
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:KHN75550.1}.
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DR EMBL; JPKZ01002673; KHN75550.1; -; Genomic_DNA.
DR STRING; 6265.A0A0B2V3G2; -.
DR OMA; DTINLEQ; -.
DR Proteomes; UP000031036; 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; cd13361; PH_PLC_beta; 1.
DR CDD; cd08591; PI-PLCc_beta; 1.
DR Gene3D; 2.30.29.240; -; 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; 1.20.1230.10; Phospholipase C beta, distal C-terminal domain; 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; IPR016280; PLC-beta.
DR InterPro; IPR042531; PLC-beta_C_sf.
DR InterPro; IPR009535; PLC-beta_CS.
DR InterPro; IPR037862; PLC-beta_PH.
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:SF211; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE BETA-4; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR Pfam; PF06631; DUF1154; 1.
DR Pfam; PF09279; EF-hand_like; 1.
DR Pfam; PF17787; PH_14; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR PIRSF; PIRSF000956; PLC-beta; 3.
DR PRINTS; PR00390; PHPHLIPASEC.
DR SMART; SM00239; C2; 1.
DR SMART; SM00148; PLCXc; 1.
DR SMART; SM00149; PLCYc; 1.
DR SUPFAM; SSF69989; C-terminal domain of PLC-beta; 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; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR000956-2};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361133};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000956-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000031036};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 816..932
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 935..1060
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 537..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1124..1191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1240..1306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1336..1378
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1426..1453
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 590..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..688
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1275..1306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 381
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT ACT_SITE 429
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT BINDING 382
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 411
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 413
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 463
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
SQ SEQUENCE 1471 AA; 168892 MW; 73129F05BDE0FDAE CRC64;
MAPISQMCEP RWSAGDARGT LAAYLAMAKE YQFNWRSNIP DTLLQGSYFD RYDDESTCLD
LNAHFRVDEY GFFLYWACEG RDTIVLDLGQ VWEARPAGLP KDGRVLFELE QRGPRETLEE
RTVWITHGVD LVNITSFYIV AQDVETAKIW RNGLNELLKN TKVRHISYST CLMKNWRFLC
LSLNDRRKIP LRNIVKMFAS GKTDKMVQKC LSDLGLSGDK YTIPHVIHRS FGRKVRHFYR
CNARRKRKER EELDVELFTF DKFLRLYHKI CPRSDVQELF VKLSGQKEYL TKDRLINFLN
EEQRDPRLNE ILFPFFDNNR VQQLIAKYET DETYVNNGKM SGDAFLRFLM SDENAPVFLD
RVEHYQDMDQ PLCHYYINSS HNTYLTGRQY GGKSSTEIYR QVLLTGCRCI ELDCWDGTGE
NKGEPIITHG KAMCTDVFFK DVLYQIRDTA FARSDYPVIL SFENHCSKSN QHKMAKYCME
IFGDMLLSRP LDDHPLEAGV PLPSPNHLKR KILIKNKRLK ADIEKLQMEQ FLREGKLDEE
DELTETPEVV IGEDAGSPQG DDDTSEDDDP SVQNSLNVAR DPLEVLPPSS SPSPSRRGSH
SPRNSLAEHT SAELLLPTDR LRLDRSSSAR TPLTHLARNA KFSFRNTIAS SVKHRTSSPL
SLRRRHIASG DQRAHPEAEQ RDDQSSPSRS EVAGDTLQLK EVDEAHPELK QSNFMAKLKP
LGFTKKPQFA METSSEHLLP VATATSFRNK RSFRRNTRTS EMEGASLSAA LLDPQPQRSS
SARHKNKKPF LTKEEEERIF AEYHYTGATT NIHPLLSSLV NYTHPVKFSG FDVAEMNNLH
FHMSSFSEST GLGYLKQSAP EFVNYNKRQL SRIYPKGARV DSSNFLPQIF WNAGCQMVAL
NFQTPDVYMQ LNMGKFEYNG SCGYLLKPDF MRRPDRTFDP FSESPVDGVI AAHCSVKVIS
GHFLCDRKVG TYVEVEMYGL PTDTIRKEHR TRTVPANGLN PVYNSDPFVF RKVVLPELAV
LRFAVYDENG KQLGQRILPL DGLQAGYRHI TLRTESNLTM ILPALFVHIV IKTYVPDELS
GLVDALADPR AYLSAQEKRK EALHNMGVDD ADILEVPANK SSASKSNLLR INGSTANHSG
DQTKSPLAPQ KDLLSAAKQP TDSNDNKQKW YLAPRSPSCR SLSPPLHTPD GMDHVSLHNA
SMRRTPTMEP LAEVEMINVA ELKKDKCFVK LTKKLQKDMD ELKKRHQKQR DSIQKQQQSN
VEKLMCDSHK QSKKRTVVNS LNQSRHPSLS DRQSDPSNLN PDMANSHRMR SLVMTQTDEW
SAMVRRHETE CYELRRAHIR EEFDLLNKLL VEAQKQQMAA LKLRLETENK ELKQTQTKKS
MDDARAIQQD KSIKTKAEKD RRVKEMNEKN LKMFFEERKR LAIKSQKHEE QLSKRHQEQC
ESLEKDALKA LEQEEMNYRE AQLASRPESV C
//
