ID A0A3B3Q9B9_9TELE Unreviewed; 1044 AA.
AC A0A3B3Q9B9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000001986.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000001986.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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|RuleBase:RU361133};
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DR AlphaFoldDB; A0A3B3Q9B9; -.
DR Ensembl; ENSPKIT00000025922.1; ENSPKIP00000001986.1; ENSPKIG00000020037.1.
DR GeneTree; ENSGT00940000164828; -.
DR Proteomes; UP000261540; Unplaced.
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; cd16206; EFh_PRIP; 1.
DR CDD; cd13364; PH_PLC_eta; 1.
DR CDD; cd08597; PI-PLCc_PRIP_metazoa; 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; 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; 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; 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:SF85; PHOSPHOINOSITIDE PHOSPHOLIPASE C; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF09279; EF-hand_like; 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; 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; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361133};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 56..166
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 533..649
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 649..778
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 20..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1002..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1022
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1044 AA; 117796 MW; 2CD7034E75F1C3E6 CRC64;
YSVGSLSFYS VKKAFQVPPR SIKNDGSKQK QVRKKTVSFS SMPNDRKINS TAACISFMME
GCEMKKVRSN SRMYNRYFLL DSDMHWLRWE PSKKDSEKAK LEIKSIKEVR LGKKTPVLRS
NGLSEQFPEE CAFSIIYGEN YESLDLVAST ADVVSTWVMG LRYLVSYGRH TVGVIEPSQP
SLRTSWIGSV FELADIAKEG QIDIFRATQI IKGLNPGMKA SRIELKFKEL QKAKDQYGEK
INVEIFTEAY CELCTRPEIF FLLVQFSSNK EYLDCKDLML FVEVEQGVEG VSEEMCRNIV
QKYEPSTEGR ERGYLSIDGF THYLLSSECH IFDPQHKQVC QDMTQPLSHY YINSSHNASL
LEDHFWGSSD IGNYIRALKM GCRSLEVVVW DGPDNEPLVY VGSSVASQLA FSKILDVINQ
FAFESSEYPL ILCLVTHCSL PQQKVMAQHM KKILGDKLYI EPPKADEHYL PSPEKLKGKI
LLKGKRLPSN YPDSEGEVTD EEEGMEMCRR VGSDENYHIN GVGIKRLKLC KDLSDLVSLC
KSVQFRDFET SKRDQKYWEI CSFNEVIANR FANEFPEDFV CYNKRFLSRV YPTPMRIDAS
NMNPQDFWKC GCQIVAMNYQ TPGLMMDLNQ GWFRQNGNSG YVLRPAIMRE EVSYFSANAR
DSLPGVSAQL LHIKVISGQN LPKPRGSAAK GDVVEPYIYV EIHGIPADCA EQRTKTISKN
GDNPIFDESF EFQINLPELA VLRFVVLDDD YIGDEFIGQY TIPFECLQPG YRHVPLQSLT
GEFLSNTLLF VHIAITNRRG GGKGHKKGLS VRKSKKAREY TSTKSTGIKV VDELFRASTQ
PLREATDLRE NVQNAMVSFK ELCGLTPAAN MKQCILTVSS WLLNSERVLQ VSVDLSGVYP
SIEAHGPIPE LLRKVLSAYD MMIQTSRTLI ESADVVYAKL MQAQRAGLDF HEDLHKIGAK
EGLKGRKLQK AMESFAWNIT VLKGQADLLK HAKGEALDTR RQMHNAAQSC GLSKNGATSP
EVPHTHAGQD PVPEAEAGGD IGPT
//
