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
//