ID A0A3B3BMZ5_ORYME Unreviewed; 1226 AA.
AC A0A3B3BMZ5;
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 Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000006946.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000006946.1}
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; A0A3B3BMZ5; -.
DR Ensembl; ENSOMET00000004966.1; ENSOMEP00000006946.1; ENSOMEG00000008118.1.
DR GeneTree; ENSGT00940000160539; -.
DR OMA; ETAMEQC; -.
DR Proteomes; UP000261560; 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|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|ARBA:ARBA00023224, ECO:0000256|PIRNR:PIRNR000956}.
FT DOMAIN 569..685
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 688..812
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 472..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1174..1226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 276..303
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 920..947
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 987..1078
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1119..1146
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 519..536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 339
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT ACT_SITE 384
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT BINDING 340
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 369
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 371
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 418
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
SQ SEQUENCE 1226 AA; 140363 MW; BAE3DE8D9A2BAEF7 CRC64;
MAGAKPGVHA LQLKPISVHE ELKRGGKFIK WDEPTLDPKL KDPNSGSPTL VTLKVDPEGF
FLFWTAGSNL EVEILDISTI RDTRTGKYAR QPKEAKMRDM LSVGKDNFQG KSVTIVYGSD
LVNISYLNFQ AMSEEGAKLW TEELFSLATN ILSQNATRNS YLLKAYSKLK LQLNQEGKIP
IKNLLKMFSD KRRVETALEQ CGLVKNKSEG IKPDDFTWEA FQRFLDHLCL RPEIQTIFEE
SSKKKPSISL DQFMDFLNRR QRDPRLNEVL YPPLKRDQVR QIMEKYETNI SQLERDLISL
KAFGRYLGGE ENGIVPPERL DVIDDMNQPL SHYFINSSHN TYLTVGQLTG LSSVEMYRQV
LLTGCRCIEL DCWQRQDEEP HITHGFTMTT EIPFKDVIEA IAESAFKTSP YPVILSFENH
VDSPKHQNKM AEYCRNIFGD ALLIDPLEKY PLVPGQLLPS PQDMMGKILI KNKKKHHHHR
PSENSVRRKE LEEPSSVPND CPLSDGDGNQ MLSNGEEKLA ESLMKEAEPR KSIADGESEE
EEEDEPATET KKNSDEGTAG SEVNATEEMS NLVNYVEPVK FKSFEVAAKR RKFFEMSSFV
ETKGMEALKN SPVEFVEYNK NQLSRIYPKG TRVDSSNYMP QLFWNVGCQM VALNFQTLDL
PMQLNMGVFE YNGRSGYLLK PEFMRRIDKH FDPFTESIVD GIVANTVKIK VVSGQFLTEK
KVGVYVEVDM FGLPADTKRK FKTKTSNGNS LDPVWDDEPF VFHKVVLPTL ASLRLAVCEE
NGKFIGHRIL PISAIRPGYH YINLKNELNQ PLLLPSLLIY TEVQDYVPNE HQEYADALTD
PIKYINQLAK RERQLAGLMD GEVQDSTQPK DDVRRASEIT AGDQLPASIQ QLPSSPADDC
PDVIIKPVPP DMEVLSIEEL KQQKNYVKLL KKQEKDLKEL RKKHLKKVCS LYKKQKSLSS
QLESDTQKKR TQMEKNLKRS IKKNEPQEVV KNELTKLEQE AEELTVKLWE GQMEKLVKLR
QELHLLERQM QEKQLVEAFD KLKETCQESL GAQTRKLKDS CEKEKKELQK ILERKRLNSI
SEAKNKGEQD KINTKHITES VSLFRKLETE QEKRQDKLAQ KYTEMLQHIQ EELPTLQTQL
AQKLKEEFQR LPEEICQHLN LELQNKGLRR FSKDISPGSN CGTPSLPSTP DQSLLNRSMD
RSTSSLADSC SPSTTPVHSE AEISFT
//
