ID A0A3B4C1D7_PYGNA Unreviewed; 1167 AA.
AC A0A3B4C1D7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase {ECO:0000256|PIRNR:PIRNR000956};
DE EC=3.1.4.11 {ECO:0000256|PIRNR:PIRNR000956};
OS Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000004606.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000004606.1}
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-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|PIRNR:PIRNR000956,
CC ECO:0000256|RuleBase:RU361133};
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; A0A3B4C1D7; -.
DR STRING; 42514.ENSPNAP00000004606; -.
DR Ensembl; ENSPNAT00000006728.1; ENSPNAP00000004606.1; ENSPNAG00000001520.1.
DR GeneTree; ENSGT00940000160539; -.
DR OMA; ETAMEQC; -.
DR Proteomes; UP000261440; 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; 2.
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; 2.
DR PRINTS; PR00390; PHPHLIPASEC.
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; 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|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000956};
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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transducer {ECO:0000256|PIRNR:PIRNR000956}.
FT DOMAIN 571..691
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT REGION 468..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1113..1167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1004..1066
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 518..536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1116..1167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 333
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT ACT_SITE 380
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT BINDING 334
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 363
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 365
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 414
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
SQ SEQUENCE 1167 AA; 133454 MW; 9465F83EA0D4CF97 CRC64;
MAGAKPGVHT LQLKPVVVHE ILKRGSKFIK WDEPNSGQPT LVNLKVDPYG FFLYWSVGSS
MEVDIVDISH IRDTRTGKFA KIPKDPRVRE VLGIGKGDGN ADGKLVTVVH GNDLVNISFL
NFQAMQEDIA KVWTEELFKL ATNILSHNAS RNNFLLKAYT KLTLQVTQDG KIPVKNILRM
FSDKRRVEAA LEQCGLVANR ADGVKSEEFT WDKFHSFLNS LCLRPEIDRL FLELGSKGKP
FLSLDQMMDF INNKQRDSRL NEVLYPPLKR EQVRQLMEKY ESNLNQLERD QISLMTFSKY
LGGDENAVVP SERFDIMDDM NQPLSHYFIN SSHNTYLTVG QLTGLSSVEM YRQVLLTGCR
CIELDCWKGR PPDEEPIITH GFTMTTEIPF KEVIEAIAES AFKISSYPVI LSFENHVDST
RQQAKMAEYC RSIFGDALLI DPLEKYPLVP GQPLPSPQEL MGKILIKNKK KHHHRASNGG
SVRRRAGEGA DEQASPLNDC PLNEGEAGQV MSNGGEKLAE RMSKDSDIRK SMDRGDGESD
EEEEEEPVTD PKKHNSDEGT ASSEVNATEE MSTLVNYIEP VKFKSFEVAN KRNKYFEMSS
FVETKGMDTM KNSPIEFLEM PVLYNKKQLS RIYPKGTRVD SSNYVPQLFW NVGCQMVALN
FQSLDLPMQL NLSVFEYNGR SGYLLKPEFM RRTDKHFDPF TMNIVDGIVA NTVKIKIVSG
QFLTDKKVGV YAEVDMFGLP TDTRRKFRTK TSNNNSMDPL WEEEPFVFNK VTTLPKLLVM
HTYIHPVWMC FPGYHYINLK NELNQPLLLA SLLVYTEVQD YIPNEHQSYA DALTNPIKHV
LDQRESQLAV FMEDSNDVTK VCVRVTKSDD LIEPQSIEQL KQNKSYLKLL TKHCKELKEL
RKKHLKKVWA LSKEQKTRSN QLNSDIQRRK SQVEKKLRLS VKKKYERKQG GFTTNNFFGP
ICVLIYYVYV WSPEFKVVVV VHMRTKHSYQ KLKEVAQECQ AAQIKKLKEI CDKEKKELQK
ILERKRQNSI IEARKGDKEK LDESQNKRQE KLEVQQKEIL RKIEEEQPVH RLRLEEDCDS
ELQRLPEEIC RYLQGELESK GLRSDALCSQ LPNHDGLGSG PPSNCSTPPF SSPNHSWSPS
LDNSRASLGD SSSSSTPVTS EAELTAV
//
