ID   PLCB2_RAT               Reviewed;        1183 AA.
AC   O89040;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   24-JAN-2024, entry version 156.
DE   RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2 {ECO:0000305};
DE            EC=3.1.4.11 {ECO:0000250|UniProtKB:Q00722};
DE   AltName: Full=Phosphoinositide phospholipase C-beta-2;
DE   AltName: Full=Phospholipase C-beta-2;
DE            Short=PLC-beta-2;
GN   Name=Plcb2 {ECO:0000312|RGD:621004};
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:CAA09465.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=Sprague-Dawley; TISSUE=Circumvallate papilla;
RX   PubMed=9860142; DOI=10.1016/s0171-9335(98)80114-3;
RA   Roessler P., Kroner C., Freitag J., Noe J., Breer H.;
RT   "Identification of a phospholipase C beta subtype in rat taste cells.";
RL   Eur. J. Cell Biol. 77:253-261(1998).
RN   [2] {ECO:0000305}
RP   TISSUE SPECIFICITY.
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).
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       This protein may be involved in the transduction of bitter taste
CC       stimuli. {ECO:0000250|UniProtKB:Q00722, ECO:0000303|PubMed:9860142}.
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:0000250|UniProtKB:Q00722};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC         Evidence={ECO:0000250|UniProtKB:Q00722};
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:0000250|UniProtKB:Q00722};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43485;
CC         Evidence={ECO:0000250|UniProtKB:Q00722};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:Q00722};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:Q00722};
CC   -!- SUBUNIT: Interacts with RAC1 (By similarity). Forms a complex composed
CC       of at least WDR26, a G-beta:gamma unit, and PLCB2 (By similarity).
CC       {ECO:0000250|UniProtKB:Q00722}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms may be produced.
CC         {ECO:0000303|PubMed:9860142};
CC       Name=1;
CC         IsoId=O89040-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Expressed in the gustatory cells of the
CC       circumvallate papillae. Not detected in non-sensory lingual epithelium,
CC       brain, parotid gland, liver, uterus, lung, heart, adrenal gland, ovary,
CC       spleen, pancreas, intestine, thymus, kidney or muscle.
CC       {ECO:0000269|PubMed:8454637, ECO:0000269|PubMed:9860142}.
CC   -!- MISCELLANEOUS: The receptor-mediated activation of PLC-beta-2 is most
CC       effectively mediated by one G-protein alpha subunit, alpha-16.
CC       {ECO:0000250|UniProtKB:Q00722}.
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DR   EMBL; AJ011035; CAA09465.1; -; mRNA.
DR   RefSeq; NP_445930.1; NM_053478.1. [O89040-1]
DR   AlphaFoldDB; O89040; -.
DR   SMR; O89040; -.
DR   BioGRID; 250044; 1.
DR   STRING; 10116.ENSRNOP00000070903; -.
DR   iPTMnet; O89040; -.
DR   PhosphoSitePlus; O89040; -.
DR   Ensembl; ENSRNOT00000078037.2; ENSRNOP00000070903.2; ENSRNOG00000058337.2. [O89040-1]
DR   Ensembl; ENSRNOT00055004053; ENSRNOP00055003057; ENSRNOG00055002548. [O89040-1]
DR   Ensembl; ENSRNOT00060040306; ENSRNOP00060033278; ENSRNOG00060023267. [O89040-1]
DR   Ensembl; ENSRNOT00065039121; ENSRNOP00065031775; ENSRNOG00065022861. [O89040-1]
DR   GeneID; 85240; -.
DR   KEGG; rno:85240; -.
DR   UCSC; RGD:621004; rat. [O89040-1]
DR   AGR; RGD:621004; -.
DR   CTD; 5330; -.
DR   RGD; 621004; Plcb2.
DR   GeneTree; ENSGT00940000159326; -.
DR   InParanoid; O89040; -.
DR   OMA; RLAKCQD; -.
DR   OrthoDB; 2900494at2759; -.
DR   PhylomeDB; O89040; -.
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:O89040; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0031680; C:G-protein beta/gamma-subunit complex; IDA:RGD.
DR   GO; GO:0098992; C:neuronal dense core vesicle; ISO:RGD.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IDA:RGD.
DR   GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IMP:UniProtKB.
DR   GO; GO:0004629; F:phospholipase C activity; IMP:RGD.
DR   GO; GO:0005543; F:phospholipid binding; IDA:RGD.
DR   GO; GO:0001580; P:detection of chemical stimulus involved in sensory perception of bitter taste; IDA:UniProtKB.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0046488; P:phosphatidylinositol metabolic process; ISS:UniProtKB.
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; IDA:UniProtKB.
DR   GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IBA:GO_Central.
DR   GO; GO:0050913; P:sensory perception of bitter taste; ISO:RGD.
DR   CDD; cd00275; C2_PLC_like; 1.
DR   CDD; cd16209; EFh_PI-PLCbeta2; 1.
DR   CDD; cd13361; PH_PLC_beta; 1.
DR   CDD; cd08624; PI-PLCc_beta2; 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; IPR028403; PLC-beta2_cat.
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; IPR046969; PLCbeta2_EF.
DR   InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR   InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR   PANTHER; PTHR10336:SF10; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE BETA-2; 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   2: Evidence at transcript level;
KW   Alternative splicing; Calcium; Coiled coil; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Metal-binding; Phosphoprotein; Reference proteome;
KW   Transducer.
FT   CHAIN           1..1183
FT                   /note="1-phosphatidylinositol 4,5-bisphosphate
FT                   phosphodiesterase beta-2"
FT                   /id="PRO_0000088490"
FT   DOMAIN          312..463
FT                   /note="PI-PLC X-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT   DOMAIN          550..666
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT   DOMAIN          666..794
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   REGION          462..537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          857..888
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1150..1183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1077..1146
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        503..525
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        857..871
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1150..1164
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        327
FT                   /evidence="ECO:0000250|UniProtKB:P10688,
FT                   ECO:0000255|PROSITE-ProRule:PRU00270"
FT   ACT_SITE        374
FT                   /evidence="ECO:0000250|UniProtKB:P10688,
FT                   ECO:0000255|PROSITE-ProRule:PRU00270"
FT   BINDING         328
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q00722"
FT   BINDING         357
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q00722"
FT   BINDING         359
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q00722"
FT   BINDING         408
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q00722"
FT   MOD_RES         952
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00722"
SQ   SEQUENCE   1183 AA;  134883 MW;  BA3AD63FE074A18C CRC64;
     MSLLNPVLLP PKVKAYLSQG ERFIKWDDET SIASPVILRV DPKGYYLYWT HQSKEMEFLD
     VTSIRDTRFG KFAKIPKSQK LREVFNMDFP DNHFLLKTFT VVSGPDMVGL TFHNFVSYKE
     NVGKDWAEDV LALAKHPMTA NASRSTFLDK ILVKLKMQLS PEGKIPVKNF FQMFPADRKR
     VEAALSACHL AKGKNDAINP EDFPESVYKS FLMSLCPRPE IDEIFTSYHA KAKPYMTKEH
     LTKFINQKQR DPRLNSLLFP PARPEQVQAL IDKYEPSGIN VQRGQLSPEG MVWFLCGPEN
     SVLAHDTLRI HQDMTQPLNH YFINSSHNTY LTAGQFSGPS SAEMYRQVLL SGCRCVELDC
     WKGKPPDEEP IITHGFTMTT DILFKEAVEA IAESAFKTSP YPVILSFENH VDSPRQQAKM
     AEYCRTMFGE TLLTEPLENF PLKPGMPLPS PEDLRGKILI KNKKNQFSGP ASPNKKPDGV
     SEGGFPSSVP VEEDTGWTAE DRTEVEEGEE EEEVEEEEEE ESGNLDEEEI KKMQSDEGTA
     GLEVTAYEEM SSLVNYIQPT KFISFEFSAQ KNRSYLVSSF TELKAYELLS KASMQFVDYN
     KRQMSRVYPK GTRMDSSNYM PQMFWNAGCQ MVALNFQTMD LPMQQNMALF EFNGQSGYLL
     KHEFMRRQDK QFNPFSVDRI DVVVATTLSI TVISGQFLSE RSVRTYVEVE LFGLPGDPKR
     RYRTKLSPTA NSINPVWKEE PFIFEKILVP ELASLRIAVM EEGGKFIGHR IIPINALHSG
     YHHLCLRSES NMPLTMPALF VFLEMKDYVP DTWADLTVAL ANPIKYFSAH DKKSVKLKEV
     TGSLPEKLFS GIPVASQSNG APVSAGNGST APGTKAKEEA TKEVAEPQTT SLEELRELKG
     VVKLQRRHEK ELRELERRGA RRWEELLQRG AAQLAELQDP AASCKLRPGK GSRKKRIVPC
     EETIVVPREV LEGPDPRVQD LKDRLEQELQ QQGEEQYRSV LKRKEQHVTE QIAKMMELAR
     EKQAAELKSF KETSETDTKE MKKKLEAKRL ERIQAMTKVT TDKVAQERLK REINNSHIQE
     VVQAVKQMTE TLERHQEKLE EKQTACLEQI QAMEKQFQEK ALAEYEAKMK GLEAEVKESM
     RACFKACFPT EAEEKPERPC EASEESCPQE PLVNKTDTQE SRL
//