ID   PLCB3_RAT               Reviewed;        1234 AA.
AC   Q99JE6; Q62887; Q9QW29;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 2.
DT   08-NOV-2023, entry version 155.
DE   RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 {ECO:0000305};
DE            EC=3.1.4.11 {ECO:0000269|PubMed:8454637};
DE   AltName: Full=Phosphoinositide phospholipase C-beta-3;
DE   AltName: Full=Phospholipase C-beta-3;
DE            Short=PLC-beta-3;
GN   Name=Plcb3 {ECO:0000312|RGD:61993};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000312|EMBL:AAK14906.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
RX   PubMed=9332346; DOI=10.1016/s0378-1119(97)00213-8;
RA   Kang J.S., Lee H.B., Rhee S.G., Park K., Yoo O.J.;
RT   "The 5'-upstream region of the rat phospholipase C-beta 3 gene contains two
RT   critical Sp1 sites and an HIV Inr-like element.";
RL   Gene 197:19-28(1997).
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 17-1234, FUNCTION, TISSUE SPECIFICITY,
RP   SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RC   STRAIN=Fischer; TISSUE=Thyroid;
RX   PubMed=8454637; DOI=10.1016/s0021-9258(18)53300-7;
RA   Jhon D.-Y., Lee H.-H., Park D., Lee C.-W., Lee K.-H., Yoo O.J., Rhee S.G.;
RT   "Cloning, sequencing, purification, and Gq-dependent activation of
RT   phospholipase C-beta 3.";
RL   J. Biol. Chem. 268:6654-6661(1993).
RN   [3]
RP   INTERACTION WITH SHANK2.
RX   PubMed=15632121; DOI=10.1074/jbc.m410740200;
RA   Hwang J.-I., Kim H.S., Lee J.R., Kim E., Ryu S.H., Suh P.-G.;
RT   "The interaction of phospholipase C-beta3 with Shank2 regulates mGluR-
RT   mediated calcium signal.";
RL   J. Biol. Chem. 280:12467-12473(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535 AND SER-1105, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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:0000250|UniProtKB:P51432, ECO:0000269|PubMed:8454637}.
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:0000269|PubMed:8454637};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC         Evidence={ECO:0000305|PubMed:8454637};
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:0000269|PubMed:8454637};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43485;
CC         Evidence={ECO:0000305|PubMed:8454637};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000269|PubMed:8454637};
CC   -!- SUBUNIT: Interacts with LPAR2 (By similarity). Interacts with SHANK2
CC       (PubMed:15632121). {ECO:0000250|UniProtKB:Q01970,
CC       ECO:0000269|PubMed:15632121}.
CC   -!- INTERACTION:
CC       Q99JE6; Q9QX74: Shank2; NbExp=4; IntAct=EBI-36481538, EBI-397902;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8454637}. Membrane
CC       {ECO:0000269|PubMed:8454637}. Nucleus {ECO:0000250|UniProtKB:P51432}.
CC       Note=And particulate fractions.
CC   -!- TISSUE SPECIFICITY: Expressed in parotid gland, brain, liver, uterus,
CC       lung, heart, adrenal gland, and ovary. Not detected in spleen,
CC       pancreas, intestine, thymus or kidney. {ECO:0000269|PubMed:8454637}.
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DR   EMBL; U41411; AAC53366.1; -; Genomic_DNA.
DR   EMBL; M99567; AAK14906.1; -; mRNA.
DR   PIR; A45493; A45493.
DR   AlphaFoldDB; Q99JE6; -.
DR   SMR; Q99JE6; -.
DR   IntAct; Q99JE6; 1.
DR   MINT; Q99JE6; -.
DR   STRING; 10116.ENSRNOP00000028720; -.
DR   SwissLipids; SLP:000000945; -.
DR   iPTMnet; Q99JE6; -.
DR   PhosphoSitePlus; Q99JE6; -.
DR   jPOST; Q99JE6; -.
DR   PaxDb; 10116-ENSRNOP00000028720; -.
DR   PeptideAtlas; Q99JE6; -.
DR   UCSC; RGD:61993; rat.
DR   AGR; RGD:61993; -.
DR   RGD; 61993; Plcb3.
DR   eggNOG; KOG1265; Eukaryota.
DR   InParanoid; Q99JE6; -.
DR   BRENDA; 3.1.4.11; 5301.
DR   Reactome; R-RNO-112043; PLC beta mediated events.
DR   Reactome; R-RNO-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR   Reactome; R-RNO-399997; Acetylcholine regulates insulin secretion.
DR   Reactome; R-RNO-416476; G alpha (q) signalling events.
DR   Reactome; R-RNO-434316; Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
DR   PRO; PR:Q99JE6; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0099524; C:postsynaptic cytosol; ISO:RGD.
DR   GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR   GO; GO:0042383; C:sarcolemma; IDA:RGD.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005516; F:calmodulin binding; ISO:RGD.
DR   GO; GO:0060090; F:molecular adaptor activity; ISO:RGD.
DR   GO; GO:0140677; F:molecular function activator activity; ISO:RGD.
DR   GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IDA:UniProtKB.
DR   GO; GO:0004629; F:phospholipase C activity; TAS:RGD.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:RGD.
DR   GO; GO:0032957; P:inositol trisphosphate metabolic process; IDA:RGD.
DR   GO; GO:0031161; P:phosphatidylinositol catabolic process; IDA:RGD.
DR   GO; GO:0046488; P:phosphatidylinositol metabolic process; ISO:RGD.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; NAS:UniProtKB.
DR   GO; GO:0006892; P:post-Golgi vesicle-mediated transport; IDA:RGD.
DR   GO; GO:0003073; P:regulation of systemic arterial blood pressure; ISO:RGD.
DR   GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IBA:GO_Central.
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; 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; 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   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   1: Evidence at protein level;
KW   Acetylation; Calcium; Cytoplasm; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Membrane; Nucleus; Phosphoprotein; Reference proteome;
KW   Transducer.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q01970"
FT   CHAIN           2..1234
FT                   /note="1-phosphatidylinositol 4,5-bisphosphate
FT                   phosphodiesterase beta-3"
FT                   /id="PRO_0000088493"
FT   DOMAIN          315..466
FT                   /note="PI-PLC X-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT   DOMAIN          589..705
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT   DOMAIN          706..834
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   REGION          465..586
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          886..936
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1196..1234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1231..1234
FT                   /note="Interaction with SHANK2"
FT                   /evidence="ECO:0000269|PubMed:15632121"
FT   COMPBIAS        482..517
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        886..911
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1214..1234
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        330
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT   ACT_SITE        377
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01970"
FT   MOD_RES         472
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01970"
FT   MOD_RES         488
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01970"
FT   MOD_RES         493
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01970"
FT   MOD_RES         535
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         925
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01970"
FT   MOD_RES         1105
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   CONFLICT        17
FT                   /note="T -> A (in Ref. 2; AAK14906)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1234 AA;  139450 MW;  2EBD7282F052CA6A CRC64;
     MAGARPGVHA LQLEPPTVVE TLRRGSKFIK WDEEASSRNL VTLRLDPNGF FLYWTGPNME
     VDTLDISSIR DTRTGRYARL PKDPKIREVL GFGGPDTRLE EKLMTVVAGP DPVNTTFLNF
     MAVQDDTVKV WSEELFKLAM NILAQNAPEH VLRKAYTKLK LQVNQDGRIP VKNILKMFSA
     DKKRVETALI CGLNFNRSES IRPDEFSLEI FERFLNKLLL RPDIDKILLE IGAKGKPYLT
     LEQLMDFINQ KQRDPRLNEV LYPPLRSSQA RLLIEKYEPN KQFLERDQMS MEGFSRYLGG
     EENGILPLEA LDLSMDMTQP LSAYFINSSH NTYLTAGQLA GTSSVEMYRQ ALLWGCRCVE
     LDVWKGRPPE EEPFITHGFT MTTEVPLRDV LEAIAETAFK TSPYPVILSF ENHVDSAKQQ
     AKMAEYCRSI FGEALLIDPL DKYPLSAGTP LPSPQDLMGR ILVKNKKRHR PSTGVPDSSV
     AKRPLEQSNS ALSESSAATE PSSPQLGSPS SDSCPGLSNG EEVGLEKTSL EPQKSLGEEG
     LNRGPNVLMP DRDREDEEED EEEEETTDPK KPTTDEGTAS SEVNATEEMS TLVNYVEPVK
     FKSFEASRKR NKCFEMSSFV ETKAMEQLTK SPMEFVEYNK QQLSRIYPKG TRVDSSNYMP
     QLFWNVGCQL VALNFQTLDL PMQLNAGVFE YNGRSGYLLK PEFMRRPDKS FDPFTEVIVD
     GIVANALRVK VISGQFLSDR KVGIYVEVDM FGLPVDTRRK YRTRTSQGNS FNPVWDEEPF
     DFPKVVLPTL ASLRIAAFEE GGRFVGHRIL PVSAIRSGYH YVCLRNEANQ PLCLPALLIY
     TEASDYIPDD HQDYAEALIN PIKHVSLMDQ RAKQLAALIG ESEAQASTEM CQETPSQQQG
     SQLSSNPVPN PLDDSPRWPP GPTTSPTSTS LSSPGQRDDL IASILSEVTP TPLEELRSHK
     AMVKLRSRQD RDLRELHKKH QRKAVALTRR LLDGLAQARA EGKCRPSSSA LSRATNVEDV
     KEEEKEAARQ YREFQNRQVQ SLLELREAQA DAETERRLEH LKQAQQRLRE VVLDAHTTQF
     KRLKELNERE KKELQKILDR KRNNSISEAK TREKHKKEVE LTEINRRHIT ESVNSIRRLE
     EAQKQRHERL LAGQQQVLQQ LVEEEPKLVA QLTQECQEQR ERLPQEIRRC LLGETSEGLG
     DGPLVACASN GHAAGSGGHQ SGADSESQEE NTQL
//