ID A0A0P7TLG5_SCLFO Unreviewed; 930 AA.
AC A0A0P7TLG5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
DE Flags: Fragment;
GN ORFNames=Z043_120100 {ECO:0000313|EMBL:KPP61766.1};
OS Scleropages formosus (Asian bonytongue) (Osteoglossum formosum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Osteoglossidae; Scleropages.
OX NCBI_TaxID=113540 {ECO:0000313|EMBL:KPP61766.1, ECO:0000313|Proteomes:UP000034805};
RN [1] {ECO:0000313|EMBL:KPP61766.1, ECO:0000313|Proteomes:UP000034805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Aro1 {ECO:0000313|EMBL:KPP61766.1};
RA Tan M.H., Gan H.M., Croft L.J., Austin C.M.;
RT "The genome of the Asian arowana (Scleropages formosus).";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPP61766.1}.
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DR EMBL; JARO02009325; KPP61766.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7TLG5; -.
DR STRING; 113540.ENSSFOP00015017336; -.
DR Proteomes; UP000034805; Unassembled WGS sequence.
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 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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000034805};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 631..727
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 730..854
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..553
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KPP61766.1"
FT NON_TER 930
FT /evidence="ECO:0000313|EMBL:KPP61766.1"
SQ SEQUENCE 930 AA; 102883 MW; C97A49AFF251A070 CRC64;
RQGCGGERSR AGAQELHPGG MSQTEPSSNQ QDSEALQQER MKAVPRRSSI IKDHTVQKAG
SGRKKTVSFS SMSSEKKVSS VADCLAFMQG GCELKKVRPN SRIYCRFYTL DPDSTCLCWE
PSKKNSERAR LQISKIHEVR TGKTTDTFRH HGPAEQLPEE AAFSIIHGDG YQSLDLVALS
PDVANIWVTG LCYLVTQPEH AHGGGPEDSL GSKIRYDWLA AEFGKSDEDG NGIVSEDTAV
ATICRLCPGT KEAKVRLKFK EMQRSKEKLT SHVTLEEFQE AYCELCTRPE VYFLLVQLSQ
DRECLHAQDL QLFLETEQGV AHTTAEGCLA IVKQFEPSAL GREQGILSLD GLARYLQSPE
CHLFDPEHQH VCQNMSLPLP HYYISASYHY LSEDHLHRGD SLEGLMKALQ VGCRCLELSV
RDGPENEPVL WLGHGSGLQN SDKTPTPPTT ACSALEFVNK YAFLTSPYPL LILLSHQCSS
AQQQVLAEHL QRVFGTRLYI PAVPSAIGKV GFAAVLPSPE ELKGRVLLVG KKLPEEEEGS
EGEVSEEEED ILGGAPPDDR QMSFPEEEEM GVALRNLSLQ RPRHFHLRKE LSDLVALRHS
GIAYFCNHRA KQKRSTTPSS VLVSPNATTP QNTTYWTLCS LGKVQANRMA SEIPKDLVAF
TQTALIRVPP SLPHEDSSNL SLQEFWMLGC QLVALNRQSP GAMLDLDRAR FTQNGGCGFV
LCPTILREDV SNFTANSQGF VPGMPAQTLR VKVISAQNLP KPQGSDTKNN VINPYVVLEM
HGVPADYAEQ HTHTAGQDSP LFDETFEFQV NMPELAILRF VVLDDSCTSD DFIGQYSVVF
ECIQPGYRTV PLLGREGDVL PCTSLFIHVT ITNRRGGGKA HAKSLSVLRG SHQDREYVTL
RNVGIKLLDD SFCAAKESLT EAIELRVNVQ
//
