ID   Q571K9_MOUSE            Unreviewed;      1048 AA.
AC   Q571K9;
DT   10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2005, sequence version 1.
DT   27-NOV-2024, entry version 123.
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};
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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   FunFam; 1.10.238.10:FF:000048; 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase; 1.
DR   FunFam; 2.30.29.240:FF:000005; 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase; 1.
DR   FunFam; 2.60.40.150:FF:000008; 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase; 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; IPR037862; PLC-beta_PH.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   InterPro; IPR053945; PLCB1-4-like_EFh.
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; 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   Pfam; PF22631; PLCB1-4-like_EFh; 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|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR000956-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU361133};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW   ECO:0000256|RuleBase:RU361133};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   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
//