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Database: UniProt
Entry: A0A3B3YDP5_9TELE
LinkDB: A0A3B3YDP5_9TELE
Original site: A0A3B3YDP5_9TELE 
ID   A0A3B3YDP5_9TELE        Unreviewed;      1109 AA.
AC   A0A3B3YDP5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
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:ENSPMEP00000025283.1, ECO:0000313|Proteomes:UP000261480};
RN   [1] {ECO:0000313|Ensembl:ENSPMEP00000025283.1}
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_014860870.1; XM_015005384.1.
DR   RefSeq; XP_014860871.1; XM_015005385.1.
DR   RefSeq; XP_014860872.1; XM_015005386.1.
DR   RefSeq; XP_014860873.1; XM_015005387.1.
DR   AlphaFoldDB; A0A3B3YDP5; -.
DR   STRING; 48701.ENSPMEP00000025283; -.
DR   Ensembl; ENSPMET00000005490.1; ENSPMEP00000025283.1; ENSPMEG00000008165.1.
DR   GeneID; 106928849; -.
DR   KEGG; pmei:106928849; -.
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; 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:SF84; INACTIVE PHOSPHOLIPASE C-LIKE PROTEIN 2; 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          115..225
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          591..707
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50008"
FT   DOMAIN          707..836
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          51..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1072..1109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..70
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..99
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1072..1088
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1109 AA;  124503 MW;  00729ED3D8224DB0 CRC64;
     MAELGEDGRL PPVHFGHTAV PSDEAAGKTH CEVSVLNGDC GISENMMCSG SPLTPGSQTG
     VETANTSVGP DAKSDIPRRS SIIKDGRQRK ERKKTVSFSS MPTEKKISRV SDCINAMVDG
     SELKKVRSNS RIYHRYFLLD ADMQSLRWEP TKKESEKAKI DVKSIKEVRT GKNTETFRTN
     GTYDQISEDC AFSIVFGENY ESLDLVANTA DVANIWVTGL RYLISYGKHT LNMIESSQNN
     LRSSWLSDLF DEEDVNHNKQ IAICAAVQLI KKLNPGLKNV KIELKFKELH KAQDKSGSDV
     TKEEFAEVFH DLCTRPEIYF LFVQFSSNKE FLDTKDLMIF LEAEQGMAQV SEDTSLNVIH
     KYEPSKEGQL KGWLSLDGFS NYLMSAECHI FDPEHKSVCQ DMNQPLSHYY INASHNTYLI
     EDQFRGPSDV TGYIRALKMG CRCVELDVWD GSDNEPVIYT GHTMTSQIVF RSVIDVINKY
     AFVASEFPLI LCLENHCSVK QQKVMFQHLK KILGDRIHVD SPKLEDCYLP SPSELKGKIL
     LKGKKLDSNC TASEGEVTDE DEGAEMSQRM SIESTEQQTN APKKIPLLKD LSDLVTLCKS
     VEFKDFPTSF QKQKPWELCS FNEVFATRCA CDFPGDFVNY NKKFLARVYP SPMRIDSSNM
     NPQDFWKCGC QIVAMNYQTP GLMMDLNIGW FRQNGNSGYV LRPAIMREQV SYFSANTKDS
     VPGVSPQLLH IKIISGQNFP KPKGSGAKGD VVDPYVYVEI HGIPADCAEQ RTKTVHQNGD
     NPLFDESFEF QINLPELAMV RFVVLDDDYI GDEFIGQYTI PFECLQPGFR HVPLQSLTGE
     LLPHTLLFVH VAITNRRGGG KPHKRGLSVR KGKKSREYAS MRVLQIKAVD EVFKTALLPL
     REATDLRENM QNAIVSFKEL CGLSAVANLK QCILALSPRL TGPDNSPLLL FNLSDPYPNL
     ELQGLLPEVL KKVVTSYDMM IQTSKILLES SDCVYERILQ TQKAAMEFHE NLHDLAVKEG
     LKGRKLHKAV ESFTWNITIL KGQADLLKHA RSEVQENLKQ IHYSALTCNL SKGGTAGGSS
     GSTDSKSRRS LEAIPEKATG EEELTDEEN
//
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