ID A0A3B3XE97_9TELE Unreviewed; 1164 AA.
AC A0A3B3XE97;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
OS Poecilia mexicana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000013304.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000013304.1}
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 RefSeq; XP_014845233.1; XM_014989747.1.
DR AlphaFoldDB; A0A3B3XE97; -.
DR STRING; 48701.ENSPMEP00000013304; -.
DR Ensembl; ENSPMET00000020960.1; ENSPMEP00000013304.1; ENSPMEG00000015584.1.
DR GeneID; 106919416; -.
DR KEGG; pmei:106919416; -.
DR CTD; 5334; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000261480; 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; cd16222; EFh_PRIP1; 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; 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:SF102; INACTIVE PHOSPHOLIPASE C-LIKE PROTEIN 1; 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; 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; 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 673..765
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 765..894
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1164 AA; 126559 MW; 9861C5C2B0E3B982 CRC64;
MSERDGCGDG LYGDGAPDFI PPRVSRGRRS GVILPGGGGG GGGGGGGPDS DTILLESVKA
APRRSSIIKD PSVQKVGGGR KKTVSFSSMP SEKKVSSAAD CLAFMQGGCE LKKIRPNSRV
YCRFYTLDTD LSCLRWEPSK KDSERARLDV SSIKEVRTGK STETFLHNGP LSEHLAEEAA
FSIIHGDEYQ SLDLVALSAD VANIWVTGLR YLLAHPSIIG GAGGGCGVVG GGQGDGGVAV
EGSLGSKIRS EWLAAEFALV DEDGYGIVSE DVAVTTVCKL CPGIKEAKVR LRFKEIQRSK
EKLTSHVTRE EFQEAFCELC TRPDVYFLLV QLSQDRECLD PQDLRLFLET EQGLSLATTE
GCWELLKRYE PSAQGRERGL LGLDGFARYL QSPECQLLDP EHLGVCQDMN LPLAHYYIST
SYRSYLLDDQ VHGRADLGGL IKALQSGCRC LELGVTDGPE GEPLLGVDYG PDISRHHHHH
HHHSPVTIRS ALEVVNKYAF LTSQYPLLLY LCHRCSPGQQ RTMAHHLKKV FGSRLYTPDA
QHVSLGGRAT TLPSPEQLKG RILLVGKKLP PEEEGSDGEV SEEDEEIGGG GPLAGRRMTI
PGEEELGVVL VVPPPSQPRK LSLHRELSDL VAIARTSSRS FYAQRGSYKQ TQQQSPPSSP
SSPGSPVPPE LPYWTMCSLG EGEAGRLTSE SPEDLVVFTK RTLTRVRPSS VRLDSSNPNP
QGYWKGGVQL VALNQQTPGA MLDLHRGRFT QNGGSGYVLR PAVMRDEVSY FSAHTHGCVP
GVPPQTLRIK VISAHNLPKP QGSGAKGEVI DPYVVLELHG VPADCAEQRT RTAAQNQDEP
MFDETFEFQV NMPELALLRF VVLDDDYIGD DFIGQYSVAF ECLQPGYRNV PLLGLAGDPL
PHTSLFVHVA ITNRRGGGKA QRRGLSVRRV GRRGREYVSL RHTGIKALDE VFKQAGGPLK
EATDLREDAQ CSTAGFKDQC GLPTVAKLKQ CIQSLATRLQ SPEGAMGAAM VLREGYPCLE
PQVSLSEATR KLLSAYDTMI SAQKQLIENA DGVQERIDQV HREGMDLHED LSRLCEKEGL
KGRKLNKAVE SFTWNITVLK GQSDLLRGAK MDSLDALRQL ALACEACGLT SSSSSSNSFS
TAELHYSSHP ASGRRSSTHG NGRV
//
