ID A0A3Q3RXY4_9TELE Unreviewed; 1259 AA.
AC A0A3Q3RXY4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase {ECO:0000256|PIRNR:PIRNR000956};
DE EC=3.1.4.11 {ECO:0000256|PIRNR:PIRNR000956};
OS Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000012995.1, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000012995.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: The production of the second messenger molecules
CC diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated
CC by activated phosphatidylinositol-specific phospholipase C enzymes.
CC {ECO:0000256|PIRNR:PIRNR000956}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + H2O =
CC 1D-myo-inositol 1-phosphate + a 1,2-diacyl-sn-glycerol + H(+);
CC Xref=Rhea:RHEA:43484, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:57880, ChEBI:CHEBI:58433;
CC Evidence={ECO:0000256|ARBA:ARBA00023726};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43485;
CC Evidence={ECO:0000256|ARBA:ARBA00023726};
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|ARBA:ARBA00023674};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC Evidence={ECO:0000256|ARBA:ARBA00023674};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR000956-2};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR000956-2};
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DR AlphaFoldDB; A0A3Q3RXY4; -.
DR STRING; 205130.ENSMAMP00000012995; -.
DR Ensembl; ENSMAMT00000013347.2; ENSMAMP00000012995.1; ENSMAMG00000008785.2.
DR GeneTree; ENSGT00940000160539; -.
DR InParanoid; A0A3Q3RXY4; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000261640; Unplaced.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:UniProtKB-UniRule.
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; cd13361; PH_PLC_beta; 1.
DR CDD; cd08591; PI-PLCc_beta; 1.
DR Gene3D; 2.30.29.240; -; 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; 1.20.1230.10; Phospholipase C beta, distal C-terminal domain; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR016280; PLC-beta.
DR InterPro; IPR014815; PLC-beta_C.
DR InterPro; IPR042531; PLC-beta_C_sf.
DR InterPro; IPR009535; PLC-beta_CS.
DR InterPro; IPR037862; PLC-beta_PH.
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:SF11; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE BETA-3; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR Pfam; PF06631; DUF1154; 1.
DR Pfam; PF09279; EF-hand_like; 1.
DR Pfam; PF17787; PH_14; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR Pfam; PF08703; PLC-beta_C; 1.
DR PIRSF; PIRSF000956; PLC-beta; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR SMART; SM00239; C2; 1.
DR SMART; SM00148; PLCXc; 1.
DR SMART; SM00149; PLCYc; 1.
DR SUPFAM; SSF69989; C-terminal domain of PLC-beta; 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 Calcium {ECO:0000256|PIRSR:PIRSR000956-2};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR000956, ECO:0000256|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|PIRNR:PIRNR000956,
KW ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|PIRNR:PIRNR000956,
KW ECO:0000256|RuleBase:RU361133};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000956-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000261640};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PIRNR:PIRNR000956}.
FT DOMAIN 567..683
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 686..810
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 466..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1191..1259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 933..960
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1007..1114
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 516..533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..879
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1194..1259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 332
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT ACT_SITE 379
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT BINDING 333
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 362
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 364
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 413
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
SQ SEQUENCE 1259 AA; 143637 MW; 5CA7312EE0FCFFE3 CRC64;
MAGAKPGVHA LQLKPVSVHE ALKSGGKFIK WDEEPSSGNP TQVTLKVDPG GFFLYWNVGS
GQEVEVLDIS TIRDTRIGKY AKQPKDPKVR EIVSGKGDNG EGKLVSIVHG NDLVNISFLN
LYATQEDTAK FFTDELFTLA TNILSQNASR NTFLLKAYTK LKLQVSQDGK IPVKNILKMF
SDKKRVETAL EQCGLVNNRS EGIKPDDFTW EAFQKFLDNL CLRPEIQSIF EESGSKRKPF
ISLDQLTDFI NRKQRDSRLN EVLYPPLKRE QVRLIMEKYE TNTSQLERDQ ISLQAFSRYL
GGEENGIVPP ERLDVLDDMN QPLSHYFINS SHNTYLTVGQ LTGLSSVEMY RQVLLTGCRC
IELDCWKGRP TDEEPYITHG FTMTTEISFK EVIEAIAESA FKTSPYPVIL SFENHVDSAK
QQAKMAEYCR TIFGDALLID PLDKYPLVPG QPLPSPQELM GKILIKNKKK HHHHRPSSGG
SIRRRELGEQ SSPNNECLLA ESEGSQLLSN GEEKLAERMV KDSGPRKSIG GEGESEEEEE
DEPVPELKKP NTDEGTASSE VNATEEMSTL VNYIEPVKFK SFEVATKRKK YFEMSSFVET
KGMDTLKSSP IEFVEYNKNQ LSRIYPKGTR VDSSNYMPQL FWNVGCQMVA LNFQTLDLPM
QLNMGVFEYN GRSGYLLKPE FMRRTDKHFD PFTENIVDGI VANTIKIRVI SGQFLTDKKV
GVYVEVDIFG LPVDTKRKYR TKTSNGNSLD PVWDDEMFVF NKIVLPTLAS LRIAVFEENG
KFIGHRILPV SAIRPGYHYI NLKNELNQPL LLPSLLVYTE AQDYIPNEHQ EYAEALTNPI
KHISQLDKRE TQLAVLIEDN SEHVPIQPKE GDTKKENEVI PGGRLPPTFY NVPPCPMDES
PDIIKLPAPA PSQKEDLIAT VLTDVQVHSV EELRQQKSYL KLLKKQSQEL KELRKKHLKK
VWNLSKEQKN RSSQLQSDSK RRRSQMEKHL KRSIKKNEPQ EPVERELTAL NQELEKQTVQ
LREWQMQELL KLRQELHSLE REKKKAHLLE ALEKLKDTAH ECQTAQLKKL RETCEKEKKE
LQKILDRKRQ NSITEAKTRE KEKAETELNE INRKHIQDSV ASIRRLEEAQ SRRQDKLILR
HREVVQHIDE ELPMLQSQLE KELEEEYQRL PEEICQHLQV ELQNKGLGKD ALFSPFSNHS
SPSPSSGSGP PSNCSTPSNP STPNRSTWNR SMDNSITSLA DSSSSSTTPV LSEPEMSFS
//