PLCB2_RAT
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 03-AUG-2022, entry version 150.
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 iPTMnet; O89040; -.
DR PhosphoSitePlus; O89040; -.
DR PRIDE; O89040; -.
DR Ensembl; ENSRNOT00000078037; ENSRNOP00000070903; ENSRNOG00000058337. [O89040-1]
DR GeneID; 85240; -.
DR KEGG; rno:85240; -.
DR UCSC; RGD:621004; rat. [O89040-1]
DR CTD; 5330; -.
DR RGD; 621004; Plcb2.
DR GeneTree; ENSGT00940000159326; -.
DR InParanoid; O89040; -.
DR OrthoDB; 368239at2759; -.
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:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0031680; C:G-protein beta/gamma-subunit complex; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA: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:0050913; P:sensory perception of bitter taste; ISO:RGD.
DR CDD; cd13361; PH_PLC_beta; 1.
DR Gene3D; 1.20.1230.10; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR Gene3D; 3.20.20.190; -; 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.
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; PTHR10336; 1.
DR PANTHER; PTHR10336:SF10; PTHR10336:SF10; 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; SSF47473; SSF47473; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF51695; SSF51695; 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
