ID A0A267FHQ5_9PLAT Unreviewed; 1277 AA.
AC A0A267FHQ5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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};
DE Flags: Fragment;
GN ORFNames=BOX15_Mlig033595g1 {ECO:0000313|EMBL:PAA73320.1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA73320.1, ECO:0000313|Proteomes:UP000215902};
RN [1] {ECO:0000313|EMBL:PAA73320.1, ECO:0000313|Proteomes:UP000215902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DV1 {ECO:0000313|EMBL:PAA73320.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:PAA73320.1};
RA Berezikov E.;
RT "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT model organism for stem cell research.";
RL Submitted (JUN-2017) 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:PAA73320.1}.
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DR EMBL; NIVC01001019; PAA73320.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A267FHQ5; -.
DR STRING; 282301.A0A267FHQ5; -.
DR Proteomes; UP000215902; 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; 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:SF149; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE CLASSES I AND II; 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; 1.
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; 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:UP000215902};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 577..693
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT REGION 1246..1277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1082..1126
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1154..1184
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 356
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT ACT_SITE 403
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT BINDING 357
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 386
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 388
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 437
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PAA73320.1"
SQ SEQUENCE 1277 AA; 141970 MW; 15B86024680FD0D4 CRC64;
LASRYGGLGL LQLPAPMADA RPALYASQLK QVAVSKLLID GSKFICWTED STGPQAVTLK
VDPKGHVLYW RDGSGEIECL EIAWIRDTRT GRSARIPKET KIREACGFFG SSEALIEDRT
VTISYGLDLV NIQWINFVAA SKNVAQEWSS QLFRYATNSF VNNPSFYDML ERSWTKLSVS
RDADNLIALK TIYKLFAHHK DDKKRVEKAL ETCCLLTAKK DSVDAKEFTF DAFLRFYTCL
CPRTDIDQIC IDLNPACKTQ PVPYITKSQV IWLLNEKQRD PRLNEIIYPY ANEAKARELI
AKFEPDNAFV EKDQLSSRGL HAYLISTDNN VVPLEKLDLS QDMEQPLAHY FINSSHNTYL
SGHQLTGKSS VELYRQVLLT GCRCVELDCW DGKGAEEEPI ITHGYTMCSE VPFRETMEAI
AESAFKVSDY PVILSFENHC SPKQQAKMVK LIKDYLGDRL LSQPLDSHPL KPGVPLPSPQ
SLRGKFLIKN KKRDFKKSAK QSEPSVEYPI SHQVNVDMED LPVARDAATA ALSGQAAEEF
PYEDEEDPEL RKLREEAGEV KEEKPMMAKE PVMLSEISAL VNYIEPAPFY SFEYALKKNV
SYECCSIAET NATNLLKESP EDFVNFNKRQ LSRIYPKGTR VDSSNYMPQL FWNAGCQMVA
LNFQTPDLGL QLNMGIFQYQ KSCGYLLKPE FMRRSDRRFD PFSESTVDGI VANSLSLRVI
SGYFLSERRV GTFVELEMFG LPADTVRRRF RTRTVPGNGI NPAYSQEPFV FKKVVLPQLA
AIRIAACEES GRVIGQRILP VDSLRPGYRH IPLFSDFMQP LSLATLFVCI SVNDYVSNAF
AELAAALANP IHYLSQKDKH QQQLMVLTDD FDAESHQEHW SEAPMSLATS IPATVAPELP
DSGVGSSASA GDQQLLSAVE APGQQGGPTT PRSAARGILA AQRFCAAEAA AAAAVSSATP
TGPSTPTSSP GALFAAFAFA TGGCAGAGGG SKPTATLQET ATLKKPSLED LLADKKYKKL
LHRCEKELQA LVKKHQKETM LLQAKHRLSQ PRRYSSDENL RSGRMAVTAA TAAASRPPRT
VEQAAEARLQ AEQQRAAELE LRTKQLESLR AQLERSLAAA VAASEKQLEA LRQHELATLK
KSQERQRNLE GRELTRLYKD KAELKEVRKE FQQKQISAAV LERQAMDSLH RRRDRELSEH
NDRLKSEVQR FIAELAGNLE AGRSAHQLEN QMPANSTSTS ALMAASAAAA AGPSPRLGRS
GATAGKSLPC TPHHRRV
//
