ID A0A3Q3BKZ8_HAPBU Unreviewed; 1009 AA.
AC A0A3Q3BKZ8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 Name=PLCH2 {ECO:0000313|Ensembl:ENSHBUP00000001676.1};
OS Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000001676.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000001676.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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|ARBA:ARBA00001913};
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DR AlphaFoldDB; A0A3Q3BKZ8; -.
DR Ensembl; ENSHBUT00000013393.1; ENSHBUP00000001676.1; ENSHBUG00000003062.1.
DR GeneTree; ENSGT00940000158374; -.
DR Proteomes; UP000264840; Unplaced.
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; cd16205; EFh_PI-PLCeta; 1.
DR CDD; cd13364; PH_PLC_eta; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001192; PI-PLC_fam.
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 PANTHER; PTHR10336:SF146; PHOSPHOINOSITIDE PHOSPHOLIPASE C; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF16457; PH_12; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR SMART; SM00239; C2; 1.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00148; PLCXc; 1.
DR SMART; SM00149; PLCYc; 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; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU361133};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000264840};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 19..127
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 147..177
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 178..214
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 492..582
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 583..712
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 760..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 937..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..803
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..860
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..908
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..966
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1009 AA; 115035 MW; 8E63731BC7EA3067 CRC64;
QIWLKQHENI DPFYLRCMCT MQTGTQLTKM KGKKKGLVRF FYLDEHKSCI RWRPSRKHDK
AKITIDSIHE VCEGKKSEVF RRYADNRFDP NCCFSIYYGD RVKSLDLVST NAEETRTWIT
GLKYLMAGIS DEDSLARRQR TRDQYPLSQT FSEADKNGDG TLSIGEVHQL LHKLNVNLPK
QKVREMFQEA DTDENQGSLG FDEFCSFYKM ISTRRDLYLI LISYSNQKEV LDLHDLARFL
ENEQKVHLVD IVAKFEPCPE NLQRMVLGID GFTNYMRSPA GDIFNPEHNQ VNQDMTQPLT
NYFIATSHNT YLTGDQLLSQ SRVEMYAYVL QAGCRCVEVD CWDGPDGEPI VHHGYTLTSK
ILFKDVIETI DKYAFTKSQY PVILSIENHC TVPQQKKMAK YLREVLQDKL DLSNVSVHEC
KKLPSPEILK GKILVKVQLF LPTHKITITH KHTRARTHVR AHTHTYIKRK TMRLSRALSD
LVKYTKSVRV SWQVSSLDET VMNQILQLKP GELVRFNQRQ LLRVYPSNYR VDSSNFNPQS
YWNSGCHMVA MNYQTEGRML ELNQAKFSSN GNCGYILKPK CMCKGAFNPV LEEPLPGHRK
TQLVLKIISG QQLPKPKDSM FGDRGEIIDP FVEVEIIGLP VDCSKQQTRV VHDNGFNPMW
EETLVFNIQM PQIALVRFQV WDHDPIGRDF IGQRTVAFTS MMPGYRHVYL EEMAESSIFV
HVAIIDMAGK TKRGIFSRMS STDSQHTGVA PCVIAESFDL ETSSQTSSPD SPAPDSQNPV
IQEELENDPS ELQQSNCAGQ QIESEQPEPP EELPPESKPG NDIATEPEPL PEAQSQTDTV
PQPPLVPQPE AKPSPLVPPS SPARVRRTLE APVTPWPSTP IRTKGRSRSC PRKQTTSAQT
PMLNRKPTFH CQTRGAQNYS SYGNPVRRIP NGLCLLDTTS SSSSDSSTDS LDFVPPPSST
GSEQHEGTLQ REMKALFDQK MREIRCKSPL FLDGESHLQK NEKKFDYKS
//
