ID A0A0L8GXQ7_OCTBM Unreviewed; 944 AA.
AC A0A0L8GXQ7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
GN ORFNames=OCBIM_22026044mg {ECO:0000313|EMBL:KOF81841.1};
OS Octopus bimaculoides (California two-spotted octopus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF81841.1};
RN [1] {ECO:0000313|EMBL:KOF81841.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF81841.1};
RC TISSUE=Gonad {ECO:0000313|EMBL:KOF81841.1};
RA Tran T., Druce J.;
RT "MeaNS - Measles Nucleotide Surveillance Program.";
RL Submitted (JUL-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};
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DR EMBL; KQ419973; KOF81841.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L8GXQ7; -.
DR STRING; 37653.A0A0L8GXQ7; -.
DR EnsemblMetazoa; Ocbimv22026044m; Ocbimv22026044m.p; Ocbimv22026044m.g.
DR OMA; AISFRWY; -.
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; 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; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
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; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR035023; PLC-gamma_C-SH2.
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: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; PF00018; SH3_1; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00452; SH3DOMAIN.
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; 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}; Repeat {ECO:0000256|ARBA:ARBA00022737};
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 265..366
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 377..466
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 495..555
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 657..726
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 727..849
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 918..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 944 AA; 109390 MW; 325DA6259112D220 CRC64;
MSPENFQLFL LQEQRDSSAN DINVVKDIMK THLDDAVRAA AEPYFTEQEF EDYLFSKPNQ
VWDTKYDKVT QDMNHPLSHY WIASSHNTYL TGCQLRSDSS VEAYARCLRM GCRCIELDCW
DGPEGYPHIT HGLTLTSKIK FLDVLKTIAE HAWVTTDYPL ILSIENHCTL PQQRKMAMAF
KDMFRDDLLV DFIDKDETQL PSPNQLRKKI LLKVWHPHIF VLTTTKLLYA EDPSAAEQDE
DQEDEENSLC AENCSSDELH FGEKWFHGKL EGGRHRAEWL LHQYKSLGDG TFLVRESETF
IGDFSLSFLR KSNVNHCRIK SKQDRGQLKY YLIDTLLFDS LYSLITYYRQ NPLRSSDFEL
TLKEPIPQPQ CHEGKEWFYG DIDRATAEDK LKRIPRDGAF LVRRSETDQY AFVISFRCEG
KIKHCRIKQE GRLFTIGTAQ FESLLNLIKY HEKNPLYKKM RLRYPVTDQL IMRMGIEPDD
GNIHGDEIYY MPKYTSKVKV KAIQDYQAKR PDELSFRRGS IVNNVHKQEG GWWRGDYGTD
KQHWFPANYV EEIDGADDAG DTSDLGSLQK GSIDLKNSII ENVTGPTNLF VFRIYNCYQN
SPLEIGCETS NDFVEWFSAI SKCIASANER VNHGLQLERT KHIAQEFSDL IVYCQAVPYS
QNQLSRIYPG RHRVDSSNFY PVPMWCCGSQ MLALNYQTGD RSMHLHHSRF AMNGQCGYIL
QPECMRAEDY DPFNVETMKG IEPMMLTMTI IGARHLVKQG RGIASPLVEV EVCGLDCDTH
KWHSSTKVDS GLNPVWNEVC HFDIECPDLA LLRIVVQVED MVGDPSFLGQ AGFPVHTLRY
GYRVVPLLNA YSEELELASL LIHFDIRNTR DSEDQETYSS IQELQKQADE LKEKLEDEED
VMQRDIVEQQ LNEAMEKLQA KREERKQKKQ SSRSQIVYRR TANN
//
