ID Q571K9_MOUSE Unreviewed; 1048 AA. AC Q571K9; DT 10-MAY-2005, integrated into UniProtKB/TrEMBL. DT 10-MAY-2005, sequence version 1. DT 28-JUN-2023, entry version 117. DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|ARBA:ARBA00012368, ECO:0000256|RuleBase:RU361133}; DE EC=3.1.4.11 {ECO:0000256|ARBA:ARBA00012368, ECO:0000256|RuleBase:RU361133}; DE Flags: Fragment; GN Name=Plcb3 {ECO:0000313|MGI:MGI:104778}; GN Synonyms=mKIAA4098 {ECO:0000313|EMBL:BAD90365.1}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|EMBL:BAD90365.1}; RN [1] {ECO:0000313|EMBL:BAD90365.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Embryonic tail {ECO:0000313|EMBL:BAD90365.1}; RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Nagase T., Ohara O., Koga H.; RT "Prediction of the Coding Sequences of Mouse Homologues of KIAA Gene. The RT Complete Nucleotide Sequences of Mouse KIAA-homologous cDNAs Identified by RT Screening of Terminal sequences of cDNA Clones Randomly Sampled from Size- RT Fractionated Libraries.."; RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK220180; BAD90365.1; -; mRNA. DR AlphaFoldDB; Q571K9; -. DR PeptideAtlas; Q571K9; -. DR AGR; MGI:104778; -. DR MGI; MGI:104778; Plcb3. DR ChiTaRS; Plcb3; mouse. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. 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; cd16210; EFh_PI-PLCbeta3; 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; IPR042531; PLC-beta_C_sf. 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; PF00168; C2; 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 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 2: Evidence at transcript level; KW Calcium {ECO:0000256|PIRSR:PIRSR000956-2}; KW Hydrolase {ECO:0000256|RuleBase:RU361133}; KW Lipid degradation {ECO:0000256|RuleBase:RU361133}; KW Lipid metabolism {ECO:0000256|RuleBase:RU361133}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000956-2}; KW Transducer {ECO:0000256|ARBA:ARBA00023224}. FT DOMAIN 626..742 FT /note="PI-PLC Y-box" FT /evidence="ECO:0000259|PROSITE:PS50008" FT DOMAIN 743..871 FT /note="C2" FT /evidence="ECO:0000259|PROSITE:PS50004" FT REGION 1..30 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 501..623 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 923..973 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 519..554 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 923..938 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 939..955 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 956..973 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 367 FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1" FT ACT_SITE 414 FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1" FT BINDING 368 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2" FT BINDING 397 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2" FT BINDING 399 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2" FT BINDING 448 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:BAD90365.1" SQ SEQUENCE 1048 AA; 117162 MW; E7B8433C7C3AA3FE CRC64; RRGARAGRAG ACGESSGTVG SRRGSVGPRA APGLAMAGAR PGVHALQLEP PTVVETLRRG SKFIKWDEEA SSRNLVTLRV DPNGFFLYWT GPNMEVDTLD ISSIRDTRTG RYARLPKDPK IREVLGFGGP DTRLEEKLMT VVAGPDPVNT TFLNFMAVQD DTVKVWSEEL FKLAMNILAQ NASRNTFLRK AYTKLKLQVN QDGRIPVKNI LKMFSADKKR VETALESCGL NFNRSESIRP DEFPLEIFER FLNKLCLRPD IDKILLEIGA KGKPYLTLEQ LMDFINQKQR DPRLNEVLYP PLRSSQARLL IEKYETNKQF LERDQMSMEG FSRYLGGEEN GILPLEALDL SMDMTQPLSA YFINSSHNTY LTAGQLAGPS SVEMYRQALL WGCRCVELDV WKGRPPEEEP FITHGFTMTT EVPLRDVLEA IAEAAFKTSP YPVILSFENH VDSAKQQAKM AEYCRSIFGD ALLIDPLDKY PLSAGIPLPS PQDLMGRILV KNKKRHRPST GVPDSSVRKR PLEQSNSALS ESSAATEPSS PQLGSPSSDS CPGLSNGEEV GLEKTSLEPQ KSLGEESLSR EPNVPMPDRD REDEEEDEEE EETTDPKKPT TDEGTASSEV NATEEMSTLV NYVEPVKFKS FEAARKRNKC FEMSSFVETK AMEQLTKSPM EFVEYNKQQL SRIYPKGTRV DSSNYMPQLF WNVGCQLVAL NFQTLDLPMQ LNAGVFEYNG RSGYLLKPEF MRRPDKSFDP FTEVIVDGIV ANALRVKVIS GQFLSDKKVG IYVEVDMFGL PVDTRRKYRT RTSQGNSFNP VWDEEPFDFP KVVLPTLASL RIAAFEEGGK FVGHRILPVS AIRSGYHYVC LRNEANQPLC LPALLIYTEA SDYIPDDHQD YAEALINPIK HVSLMDQRAK QLAALIGESE AQASTETYQE TPCQQPGSQL PSNPTPNPLD ASPRWPPGPT TSSTSSSLSS PGQRDDLIAS ILSEVTPTPL EELRSHKAMV KLRSRQDRDL RELHKKHQRK AVALTRRLLD GLAQARAEGK CRPSPSAL //