ID A0A3B3VG07_9TELE Unreviewed; 1275 AA.
AC A0A3B3VG07;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase {ECO:0000256|PIRNR:PIRNR000956};
DE EC=3.1.4.11 {ECO:0000256|PIRNR:PIRNR000956};
GN Name=PLCB2 {ECO:0000313|Ensembl:ENSPLAP00000024690.1};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000024690.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000024690.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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) + H2O =
CC 1D-myo-inositol 1-phosphate + a 1,2-diacyl-sn-glycerol + H(+);
CC Xref=Rhea:RHEA:43484, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:57880, ChEBI:CHEBI:58433;
CC Evidence={ECO:0000256|ARBA:ARBA00023726};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43485;
CC Evidence={ECO:0000256|ARBA:ARBA00023726};
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|ARBA:ARBA00023674};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC Evidence={ECO:0000256|ARBA:ARBA00023674};
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};
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DR AlphaFoldDB; A0A3B3VG07; -.
DR STRING; 48699.ENSPLAP00000024690; -.
DR Ensembl; ENSPLAT00000002810.1; ENSPLAP00000024690.1; ENSPLAG00000011117.1.
DR GeneTree; ENSGT00940000159326; -.
DR Proteomes; UP000261500; Unplaced.
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 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; 2.
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; IPR014815; PLC-beta_C.
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:SF10; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE BETA-2; 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 Pfam; PF08703; PLC-beta_C; 2.
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 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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PIRNR:PIRNR000956}.
FT DOMAIN 559..675
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 675..802
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 462..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..1033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1071..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..539
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..851
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..882
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..900
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..983
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1030
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 325
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT ACT_SITE 372
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT BINDING 326
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 355
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 357
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 406
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
SQ SEQUENCE 1275 AA; 143260 MW; 78C71ADB4A5E4528 CRC64;
MNKKRYFLDP PEVKDYLVKG ERFTKWSEDT TKTVPVTMKM DPKGFYVYWT NQSKETTFLD
VATIRDTRTG KYAKLPKHPK VRNVFNLDFP DSNHLAKTLT IVSGPDMVNL TYHNFFASKE
KVTQNWADDI LGIAYNAART NACRQVFLEK IYIRISLQTN KDGKIPVKNI YKMFPADKKR
VESALASAHL PKGKYDTIKP DVFTEAAFKT FLTNLCPRPE IFEIFTSYST KPTMTKENFT
KFLNEKQRDS RFNEELFPRL RQDQIKALID KYEPLTTNSN RGLISPEGFL FFLMGPETSV
VMQDKLAKCQ DMTQPIPHYF IKSSHNTYLT AGQFSGVSSP EMYRQCLLSG CRCLELDCWK
GKPPDEEPII THGFTMCTEI LFKDVIEAIA ESAFKTSKYP VVLSFENHVD SVKQQEKMAN
YCKTLFGDAL LSEPLEKYPL KPGQQIPSPS ELMGKILIKN KKGSHEKPAQ AKKTSAAATD
QTAVAVTEQT VAAEPTQDPN ASSQDASNPA APTQENQAEG EAATEDNEEQ EDTEEQDEEK
MKTSDEGTAG QEVTAYEAMS SIVNYIQPNK FISFENAKKK NKSYVISSFV ETRGEAMISK
TAVEFVEYNK RQMSRIYPKG TRMDSSNYSP QPFWNVGCQM VALNYQTMDF PMQLNMALFE
FNGRTGYLLK HDVMRRSDKK FDPFCDRIDT VVASTLTIKI YSGQFLSEKS VKTGVEVEVI
GLPGDPKKKY RTKWSTTPNA INPVWNEEPF VFEKILLPEM ASLRIVVHEE NGKFVGHRII
PIDAIQSGFH HICLRSESNM PLTLPALFVY IEVKDYIPAA FADFTEDLFN PTKGADKTSK
TPKTSSSDYI SPYELPLGDQ PPAGKAKENE APAEEKAASE PKPNTDESTS QSQSPSETGA
EETKEQPEQS QTPDAAPTKD DEPDAGKLES QSPPEAPAAN KEVEAEKEVD PKSAAAPEAK
EEEGTDPDAN PKNEDKEDSE APAPASGEDA PAEDASVSLS SLPSESAGSS DSSQSPSKPC
TVTVEQLTQH KNYLKVIKRQ EKELKDAEKK YQKKAEDLIQ KYSDSIKAIK KKGSLKKKEG
GDNSSDNSVK KERVQDQKDK MQTELQALWT EQCDQTKKKK EQCATERLAK LLEMAMERHT
VELKTLERYD KLLTDKTTNL YIPHTSYTDI LKPLYENHKS MEDVLCFAVL QSADFSPQQE
ALMKKQAATL EEVKGMTNQL IQEALKEHAQ KTRSLSAEVR NAVNVCVGAH FPEYVDEDGD
KKPPCESFYG NVFVG
//
