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Database: UniProt
Entry: A0A2A2LYQ2_9BILA
LinkDB: A0A2A2LYQ2_9BILA
Original site: A0A2A2LYQ2_9BILA 
ID   A0A2A2LYQ2_9BILA        Unreviewed;       971 AA.
AC   A0A2A2LYQ2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
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=WR25_12629 {ECO:0000313|EMBL:PAV91381.1};
OS   Diploscapter pachys.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX   NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV91381.1, ECO:0000313|Proteomes:UP000218231};
RN   [1] {ECO:0000313|EMBL:PAV91381.1, ECO:0000313|Proteomes:UP000218231}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PF1309 {ECO:0000313|EMBL:PAV91381.1};
RA   Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA   Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT   "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL   Curr. Biol. 0:0-0(2017).
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:PAV91381.1}.
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DR   EMBL; LIAE01006322; PAV91381.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A2LYQ2; -.
DR   Proteomes; UP000218231; 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; cd10341; SH2_N-SH2_PLC_gamma_like; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 2.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
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; 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; PF00388; PI-PLC-X; 1.
DR   Pfam; PF00017; SH2; 2.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00390; PHPHLIPASEC.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   SMART; SM00148; PLCXc; 1.
DR   SMART; SM00252; SH2; 2.
DR   SMART; SM00326; SH3; 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; PS50007; PIPLC_X_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:UP000218231};
KW   SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          612..711
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          722..811
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          839..897
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   971 AA;  112426 MW;  7D9C1E4BAB673B95 CRC64;
     MSSSSGSNRS KSNSTVSPST LPHTNSLTSV HHASASPKTR VYNKIHEMDF TKMFMAMEKG
     HKVCKLNVNK RWDPAYKHLM LHKESRQLFL TKLEQTAVRS RPNVLDIRHV REVQTLDYKL
     NTIKIQDKWK KDKEIQNFEP LKILVISYGV GFTLNNWILL FETVEACRLW SQGVHNLMLE
     TRDRDTSSHP QRVDRFIHKQ FMAIAGPNDT VARKHMKPFV QTSLQFKVQS KQLQEVTEDD
     MTLSQFSKAT RQLIHIPQLF TTLFSDLMKE DTKNDENKND PNGKITFDKF VLFLKNKQCD
     EMATNKHRVS EFLQRYLPQE ISHIDPEPSM SIMEFCDFLF SRENSLWDIM NEKVTHDMTR
     PLSHYWIASS HNTYLTGDQL RSESSLDSYA QALLMGCRCI ELDCWDGQKK PNSNEFYDIV
     IYHGYTMTSK LLLRDVLYTI KHYAFITSEY PVILSIEDNC SVPAQRLLAQ EMREILGEYL
     LITPVSRDET QLPSPAAMKK KIILKHKKLP IESDNLAVVV TSNDDFQDTD ILARDCIRKG
     ILQLKDSTSH EWMSHVFVLF PDRLCYLLEP CTTDEASLKD DSLSMLGEDD KEEESPTGFG
     VRPEEMHITE EWFHGKCGRE DAKKRIEEHK DKGDGLFMIR DSNLFIGDYS LSILHNGRVH
     HVRIRSKIID KEKKYYFLDN KVCDTLYELV SYYTRHYLST SDFKMVLTTP CPQPQPHLNQ
     PWFSATADKK KAEELLNRVT EDGAFLVRTS SSDTSVFVLS LRVDGEFWHY RLKRDGRIFV
     VNQTVFENLN QIVDYYSSRE FVRGISLRFP VNERDVNQYT SGEMSEAAPG CYMDLKDLDK
     EVQARAIRPY RGTADDDLSF PANAIITVLR KEEGLWRGRY GSATGWFPSA YVQEVLPEKS
     TNSGDDNNGY NTIELAGTLI ERTTDGDKPF AIKISQSGQH WTGQQWILAA NCRNMLIPKV
     VKRFIFSYRR S
//
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