ID W6UW42_ECHGR Unreviewed; 1310 AA.
AC W6UW42;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase {ECO:0000256|PIRNR:PIRNR000956};
DE EC=3.1.4.11 {ECO:0000256|PIRNR:PIRNR000956};
GN ORFNames=EGR_00105 {ECO:0000313|EMBL:EUB64836.1};
OS Echinococcus granulosus (Hydatid tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus;
OC Echinococcus granulosus group.
OX NCBI_TaxID=6210 {ECO:0000313|EMBL:EUB64836.1, ECO:0000313|Proteomes:UP000019149};
RN [1] {ECO:0000313|EMBL:EUB64836.1, ECO:0000313|Proteomes:UP000019149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24013640; DOI=10.1038/ng.2757;
RA Zheng H., Zhang W., Zhang L., Zhang Z., Li J., Lu G., Zhu Y., Wang Y.,
RA Huang Y., Liu J., Kang H., Chen J., Wang L., Chen A., Yu S., Gao Z.,
RA Jin L., Gu W., Wang Z., Zhao L., Shi B., Wen H., Lin R., Jones M.K.,
RA Brejova B., Vinar T., Zhao G., McManus D.P., Chen Z., Zhou Y., Wang S.;
RT "The genome of the hydatid tapeworm Echinococcus granulosus.";
RL Nat. Genet. 45:1168-1175(2013).
CC -!- FUNCTION: The production of the second messenger molecules
CC diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated
CC by activated phosphatidylinositol-specific phospholipase C enzymes.
CC {ECO:0000256|PIRNR:PIRNR000956}.
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|PIRNR:PIRNR000956,
CC 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:EUB64836.1}.
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DR EMBL; APAU02000001; EUB64836.1; -; Genomic_DNA.
DR STRING; 6210.W6UW42; -.
DR EnsemblMetazoa; XM_024489354.1; XP_024356032.1; GeneID_36335820.
DR OMA; DTINLEQ; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000019149; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:UniProtKB-UniRule.
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; 1.
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; PF00168; C2; 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; 2.
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|PIRNR:PIRNR000956};
KW Lipid degradation {ECO:0000256|PIRNR:PIRNR000956,
KW ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|PIRNR:PIRNR000956,
KW ECO:0000256|RuleBase:RU361133};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000956-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000019149};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PIRNR:PIRNR000956}.
FT DOMAIN 615..734
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 734..863
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 497..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1048..1079
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 341
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT ACT_SITE 388
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT BINDING 342
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 371
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 373
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 422
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
SQ SEQUENCE 1310 AA; 147297 MW; 0AC55848202D5B41 CRC64;
MSSDIAKRQR TVPSTKAYDF VWRRPVPTAL REGSYFDRYE EETGALELGC FLRVDEDGFF
LFWKSETNEG QVLELSQVSD VRQGTKPKDE KLLGVLMERM PSGGKNLDER IVTVCSGLDL
VNISYTNFVA ASAEVASLWI QSVRGLTHNT KAQNVCPMTQ LRKHWLRITL TVNPRGKIPV
RVVTKTFASG RNERIIFQSL KDLGLPSGKN DEVEPSDFTF ERFYELYHKI CPRTDIEELF
KSLSHGRDTI TADKMIEFLN EVQRDPRLNE ILYPYANRHT IRYIQETYDS RDKSNSSDTV
SLKGFYRYLM SDDNAPVFLD RLDIYQDMDQ PLCHYYINSS HNTYLIGRQF GGKSSVEIYR
QVLLAGCRCI ELDCWDGKGE DQEPIITHGK AMCSDILFKD VIYAVRDTAF VTSEYPLIMS
FENHCSKHQQ YKLAKYCEDI LGDMLLTKPL DKHPLEPGVP LPSPEKLKRK ILIKNKRLDP
DVEKHQLELF IKGQADPVQE EDDVAEDPDP LGSTDCDVSP INGDIDPHPE TKIRPGSGQI
NALSTSSAFS SSLMGKLSET EMKRLIMKKV ALVILFLPLI ESQTLLKGTL TAEEEQAMLA
QYHYTGATKT IHPLLSSMVN YAQPVKFQGF DIAEDENIHY HMSSFSETVA LGLMKNEAIE
FVKYPFLLRG LRENACEACS PPQRLGLMLN IFWNAGCQMV ALNFQTPDLA MQLNQGKFEY
NGNCGYLLKP EFMRRPERQF DPFSESPMDG VIAATCEVRI ISGQFLSDRK VGTYVEVDMY
GLPTDTIRKE FRTRVVPNNG LNPVYGEDAV FVFRKVVLPD LAVLRFAVYE DTGKLIGQRV
LPLDGLQSGY RHISLRTEGN FPLSLPTLFC RVSLTTYVPE GLNDLVDALS DPRAFLSKEE
QRMKQLASMG IDSSEIDEVS SSSTKLTSML KQRPVGSGPT LSSTTSGVPT GSAGCASAGG
GGGGGSSSSG AGVGSASGLC LSCLGPSGDP HRLTPASVTG VAASTAYGSG TACIAVSTPG
PSGNSTKKED KKEDPKFPSI SLAMLRSDKN YRRLVKKQAK ELESLQRRHE KEAAAMLRAH
SLLTDKLNAS HAKAIASSTS SLRSTPQKVN GVGTPLKEAH IAQMNDLVRQ QTDEWSKLKC
TQMSEIHTLV LTFIDSRKDL LLKSQFRDCK KFLNVTFLCH RRQDSSQILR DTHDEQKRLL
KQIQERENKD MKAQQIKISL DSNRNVMNDP KLKNKAERDR RIRELKDYNT KRFIDQRKAQ
AQRNDRQAQD LLRRHEEEEQ GVIAGVNRER DELIRNYREE LLASKRATMI
//
