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Database: UniProt
Entry: A0A158PSX9_9BILA
LinkDB: A0A158PSX9_9BILA
Original site: A0A158PSX9_9BILA 
ID   A0A158PSX9_9BILA        Unreviewed;      1358 AA.
AC   A0A158PSX9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
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   ORFNames=BTMF_LOCUS6079 {ECO:0000313|EMBL:VDO20803.1};
OS   Brugia timori.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX   NCBI_TaxID=42155 {ECO:0000313|Proteomes:UP000050602, ECO:0000313|WBParaSite:BTMF_0000798001-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:BTMF_0000798001-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDO20803.1, ECO:0000313|Proteomes:UP000280834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) 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};
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DR   EMBL; UZAG01015489; VDO20803.1; -; Genomic_DNA.
DR   STRING; 42155.A0A158PSX9; -.
DR   WBParaSite; BTMF_0000798001-mRNA-1; BTMF_0000798001-mRNA-1; BTMF_0000798001.
DR   Proteomes; UP000050602; Unplaced.
DR   Proteomes; UP000280834; 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; cd10341; SH2_N-SH2_PLC_gamma_like; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 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; IPR035024; PLC-gamma_N-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:SF36; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA PLC-3; 1.
DR   PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00169; PH; 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:UP000280834};
KW   SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW   ProRule:PRU00191};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT   DOMAIN          610..709
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          720..809
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          838..896
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          931..967
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          989..1111
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50008"
FT   DOMAIN          1114..1247
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
SQ   SEQUENCE   1358 AA;  157093 MW;  59EA28AECCFF6AD9 CRC64;
     MYPQSSADSV LLFQRPFVFT SNSLMTSSSV EFEMEKVFHA MEMGHNVYKL LLMKRRDPAQ
     KRLTYNRETR QLFLSKLDNY DKSGGKTLRL DLRIVKEVHT LDFKLKKIKI GDKWEKDKEI
     KQFDATRILV LSYATTFNLR YWILLFDTED LCRMWCQGVH YLMLDTISAC HALLVERWLR
     KEFYNIAGYA LENPCVAMKH MKPFVQTSLQ YKVQSKQLQE VCEETMHYDS FANAYRKLLH
     ANSLFAEHFA AYSDDAAVVS FNNFLRFHKD KQNDEIGMMR EKASDFLRHF LRQWDPYRDV
     REPALSVTEF CDFLFSRENS LWDSVNENVI HDMNRPLSHY WIASSHNTLI LYLTGDQLKS
     ESSLDTYARA LLMGCRCVER MLLFVLIDTI DCWDGQKRNS GEIQDIVIYH GYTMTSKINL
     RDVLYTIRHY AFINSEFPVI LSIEDNCSVP VQRLLAREIR EILGDYLLTA PVSREETCLP
     SPEALKRKII LKHKKLPTES ENIILQQADE DQEQDLLLLN FTRQGILSLK SGISDEWTTH
     LFILFPDRLC YMLEQCENNI DNQGILRRQD SLGNAHDDEN QVMCLVYIDV LTNLTGFGVP
     PEEMHITEEW FHGKTDRDTA RIRLLEHKDK GNGLFLVRDS TIFIGDYSLS FLHNEKVHHC
     RIRTRMVNGE KKYYFLENKQ MDTLYELISH YTKERLRTPN FSTTLITPCP QPCPHLGMIW
     FCEKTDRNRA EELLNTVQQD GAFLLRFSST DKNVFVLSLR VDGEIWHYHL KRDGRIFVVN
     QTIFENLNQI VEYYSTREFV RGICLKYPVG EDTIIGSAGI CCSTDRALGC YMELKDIDKE
     VLVRAIESYN GSLPCELSFP VNAVINVFRK DGDRWRGKYR GRSGFFPSRC VIELETSDNQ
     PSELGPYAAI DLADSLIEEV PFEIAGRPFA FKIRRVSTHW NPSEYVLAAN SSEEREDWLN
     ILHELMRTVT DRNTLIRTRE KNLRIASELS DLVVYCQAVP FNSQFATLLE KANSENIVAQ
     GNFYEMCSFS ETKFEKLVER GLVQFNARQL SRVYPQGSRV TSANYDPVPM WNAACHMVAL
     NYQTGDRSMQ LNQGKFMANG QCGYVLKPSY MIDEMFSPDA AEVVSTSCPI ILTVHVNIYS
     LFNWKGGQHL SRKDRNRGIC SPTVTVEVVG LPADSTSVRT RAIASNGLNP VWNEKFIFKV
     YCPEIALLRL YVEDGDFMGP KMDPFIGQAV YPLDCIRTGF RSVPLRNQYS EELELSSLLV
     YLDMRRRSNE AEVLNPHVDL QSDRYVAGGL HKTLTSSGVF SARLNSTDQS SFTVPLTPNL
     SVAKQVQVLM DSTSVEYFFF XXXXXXXXXX XXXWIRRP
//
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