PLCB1_RAT
ID PLCB1_RAT Reviewed; 1216 AA.
AC P10687;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 {ECO:0000305};
DE EC=3.1.4.11 {ECO:0000269|PubMed:8454637};
DE AltName: Full=PLC-154;
DE AltName: Full=Phosphoinositide phospholipase C-beta-1;
DE AltName: Full=Phospholipase C-I;
DE Short=PLC-I;
DE AltName: Full=Phospholipase C-beta-1;
DE Short=PLC-beta-1;
GN Name=Plcb1 {ECO:0000312|RGD:3344};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3390863; DOI=10.1016/0092-8674(88)90548-x;
RA Suh P.-G., Ryu S.H., Moon K.H., Suh H.W., Rhee S.G.;
RT "Cloning and sequence of multiple forms of phospholipase C.";
RL Cell 54:161-169(1988).
RN [2]
RP CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582; SER-1197; SER-1199 AND
RP SER-1200, AND 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: Catalyzes the hydrolysis of 1-phosphatidylinositol 4,5-
CC bisphosphate into diacylglycerol (DAG) and inositol 1,4,5-trisphosphate
CC (IP3) and mediates intracellular signaling downstream of G protein-
CC coupled receptors. Regulates the function of the endothelial barrier.
CC {ECO:0000250|UniProtKB:Q9Z1B3}.
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 -!- SUBUNIT: Interacts with DGKQ. {ECO:0000250|UniProtKB:Q9NQ66}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250|UniProtKB:Q9Z1B3}.
CC Cytoplasm {ECO:0000269|PubMed:8454637}. Note=Colocalizes with the
CC adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of
CC cardiac myocytes. {ECO:0000250|UniProtKB:Q9Z1B3}.
CC -!- TISSUE SPECIFICITY: Highest expression in brain. Also expressed in
CC parotid gland, liver, uterus, lung, heart, adrenal gland and ovary. Not
CC detected in spleen, pancreas, intestine, thymus or kidney.
CC {ECO:0000269|PubMed:8454637}.
CC -!- PTM: Palmitoylated. Palmitoylation at Cys-17 by ZDHHC21 regulates the
CC signaling activity of PLCB1 and the function of the endothelial
CC barrier. Palmitoylation by ZDHHC21 is stimulated by inflammation.
CC {ECO:0000250|UniProtKB:Q9Z1B3}.
CC -!- MISCELLANEOUS: The receptor-mediated activation of PLC-beta-1 is
CC mediated by two G-protein alpha subunits, alpha-Q and alpha-11.
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DR EMBL; M20636; AAA41885.1; -; mRNA.
DR PIR; A28821; A28821.
DR RefSeq; NP_001071109.1; NM_001077641.1.
DR RefSeq; XP_017446955.1; XM_017591466.1.
DR AlphaFoldDB; P10687; -.
DR SMR; P10687; -.
DR BioGRID; 246789; 162.
DR IntAct; P10687; 4.
DR MINT; P10687; -.
DR STRING; 10116.ENSRNOP00000006389; -.
DR BindingDB; P10687; -.
DR SwissLipids; SLP:000000946; -.
DR iPTMnet; P10687; -.
DR PhosphoSitePlus; P10687; -.
DR SwissPalm; P10687; -.
DR PaxDb; P10687; -.
DR PRIDE; P10687; -.
DR Ensembl; ENSRNOT00000006389; ENSRNOP00000006389; ENSRNOG00000004810.
DR GeneID; 24654; -.
DR KEGG; rno:24654; -.
DR UCSC; RGD:3344; rat.
DR CTD; 23236; -.
DR RGD; 3344; Plcb1.
DR eggNOG; KOG1265; Eukaryota.
DR GeneTree; ENSGT00940000155428; -.
DR InParanoid; P10687; -.
DR OrthoDB; 368239at2759; -.
DR PhylomeDB; P10687; -.
DR TreeFam; TF313216; -.
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 SABIO-RK; P10687; -.
DR PRO; PR:P10687; -.
DR Proteomes; UP000002494; Chromosome 3.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; ISS:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; IDA:BHF-UCL.
DR GO; GO:0005516; F:calmodulin binding; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0005096; F:GTPase activator activity; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:BHF-UCL.
DR GO; GO:0005521; F:lamin binding; ISO:RGD.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IDA:RGD.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:RGD.
DR GO; GO:0060466; P:activation of meiosis involved in egg activation; ISS:BHF-UCL.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:1902618; P:cellular response to fluoride; IDA:RGD.
DR GO; GO:1905631; P:cellular response to glyceraldehyde; IDA:RGD.
DR GO; GO:1904637; P:cellular response to ionomycin; IDA:RGD.
DR GO; GO:1904117; P:cellular response to vasopressin; IDA:RGD.
DR GO; GO:0021987; P:cerebral cortex development; ISS:BHF-UCL.
DR GO; GO:0045444; P:fat cell differentiation; ISO:RGD.
DR GO; GO:0007213; P:G protein-coupled acetylcholine receptor signaling pathway; ISO:RGD.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISO:RGD.
DR GO; GO:0007215; P:glutamate receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:0032957; P:inositol trisphosphate metabolic process; IDA:RGD.
DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:0070498; P:interleukin-1-mediated signaling pathway; ISO:RGD.
DR GO; GO:0035722; P:interleukin-12-mediated signaling pathway; ISO:RGD.
DR GO; GO:0035723; P:interleukin-15-mediated signaling pathway; ISO:RGD.
DR GO; GO:0007612; P:learning; IEP:RGD.
DR GO; GO:0007613; P:memory; IEP:RGD.
DR GO; GO:2000438; P:negative regulation of monocyte extravasation; ISS:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:BHF-UCL.
DR GO; GO:0031161; P:phosphatidylinositol catabolic process; IDA:RGD.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IEP:RGD.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:2000344; P:positive regulation of acrosome reaction; ISO:RGD.
DR GO; GO:2000560; P:positive regulation of CD24 production; ISS:BHF-UCL.
DR GO; GO:0048639; P:positive regulation of developmental growth; ISS:BHF-UCL.
DR GO; GO:0040019; P:positive regulation of embryonic development; ISO:RGD.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISS:BHF-UCL.
DR GO; GO:0032735; P:positive regulation of interleukin-12 production; ISS:BHF-UCL.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISO:RGD.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; ISS:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:BHF-UCL.
DR GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:1903140; P:regulation of establishment of endothelial barrier; ISO:RGD.
DR GO; GO:0080154; P:regulation of fertilization; ISO:RGD.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:0099178; P:regulation of retrograde trans-synaptic signaling by endocanabinoid; ISO:RGD.
DR GO; GO:0034284; P:response to monosaccharide; IDA:BHF-UCL.
DR GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IDA:BHF-UCL.
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; IPR028400; PLC-beta1.
DR InterPro; IPR014815; PLC-beta_C.
DR InterPro; IPR042531; PLC-beta_C_sf.
DR InterPro; IPR009535; PLC-beta_CS.
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:SF12; PTHR10336:SF12; 1.
DR Pfam; PF06631; DUF1154; 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 1: Evidence at protein level;
KW Calcium; Cytoplasm; Hydrolase; Lipid degradation; Lipid metabolism;
KW Lipoprotein; Membrane; Nucleus; Palmitate; Phosphoprotein;
KW Reference proteome; Transducer.
FT CHAIN 1..1216
FT /note="1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase beta-1"
FT /id="PRO_0000088488"
FT DOMAIN 316..467
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 540..656
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 656..784
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 469..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 967..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1072..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1172..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..521
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..875
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..982
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 331
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 378
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1B3"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1B3"
FT MOD_RES 509
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1B3"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1B3"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 887
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P10894"
FT MOD_RES 978
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1B3"
FT MOD_RES 987
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1B3"
FT MOD_RES 1197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT LIPID 17
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1B3"
SQ SEQUENCE 1216 AA; 138344 MW; 92F23691781F788E CRC64;
MAGAQPGVHA LQLKPVCVSD SLKKGTKFVK WDDDSTIVTP IILRTDPQGF FFYWTDQNKE
TELLDLSLVK DARCGKHAKA PKDPKLRELL DVGNIGHLEQ RMITVVYGPD LVNISHLNLV
AFQEEVAKEW TNEVFSLATN LLAQNMSRDA FLEKAYTKLK LQVTPEGRIP LKNIYRLFSA
DRKRVETALE ACSLPSSRND SIPQEDFTPD VYRVFLNNLC PRPEIDNIFS EFGAKSKPYL
TVDQMMDFIN LKQRDPRLNE ILYPPLKQEQ VQVLIEKYEP NSSLAKKGQM SVDGFMRYLS
GEENGVVSPE KLDLNEDMSQ PLSHYFINSS HNTYLTAGQL AGNSSVEMYR QVLLSGCRCV
ELDCWKGRTA EEEPVITHGF TMTTEISFKE VIEAIAECAF KTSPFPILLS FENHVDSPKQ
QAKMAEYCRL IFGDALLMEP LEKYPLESGV PLPSPMDLMY KILVKNKKKS HKSSEGSGKK
KLSEQASNTY SDSSSVFEPS SPGAGEADTE SDDDDDDDDC KKSSMDEGTA GSEAMATEEM
SNLVNYIQPV KFESFETSKK RNKSFEMSSF VETKGLEQLT KSPVEFVEYN KMQLSRIYPK
GTRVDSSNYM PQLFWNAGCQ MVALNFQTVD LAMQINMGMY EYNGKSGYRL KPEFMRRPDK
HFDPFTEGIV DGIVANTLSV KIISGQFLSD KKVGTYVEVD MFGLPVDTRR KAFKTKTSQG
NAVNPVWEEE PIVFKKVVLP SLACLRIAAY EEGGKFIGHR ILPVQAIRPG YHYICLRNER
NQPLMLPAVF VYIEVKDYVP DTYADVIEAL SNPIRYVNLM EQRAKQLAAL TLEDEEEVKK
EADPGETSSE APSETRTTPA ENGVNHTATL APKPPSQAPH SQPAPGSVKA PAKTEDLIQS
VLTEVEAQTI EELKQQKSFV KLQKKHYKEM KDLVKRHHKK TTELIKEHTT KYNEIQNDYL
RRRAALEKSA KKDSKKKSEP SSPDHGSSAI EQDLAALDAE MTQKLIDLKD KQQQQLLNLR
QEQYYSEKYQ KREHIKLLIQ KLTDVAEECQ NNQLKKLKEI CEKEKKELKK KMDKKRQEKI
TEAKSKDKSQ MEEEKTEMIR SYIQEVVQYI KRLEEAQSKR QEKLVEKHKE IRQQILDEKP
KLQMELEQEY QDKFKRLPLE ILEFVQEAMK GKVSEDSNHG SAPPSLASDP AKVNLKSPSS
EEVQGENAGR EFDTPL
