ID PLCB1_HUMAN Reviewed; 1216 AA. AC Q9NQ66; D3DW12; D3DW13; O60325; Q17RQ6; Q5TFF7; Q5TGC9; Q8IV93; Q9BQW2; AC Q9H4H2; Q9H8H5; Q9NQ65; Q9NQH9; Q9NTH4; Q9UJP6; Q9UM26; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 220. DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 {ECO:0000305}; DE EC=3.1.4.11 {ECO:0000269|PubMed:9188725}; 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|HGNC:HGNC:15917}; Synonyms=KIAA0581; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B). RC TISSUE=Brain; RX PubMed=11118617; DOI=10.1016/s0167-4781(00)00260-8; RA Caricasole A., Sala C., Roncarati R., Formenti E., Terstappen G.C.; RT "Cloning and characterization of the human phosphoinositide-specific RT phospholipase C-beta 1 (PLCbeta1)."; RL Biochim. Biophys. Acta 1517:63-72(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A). RC TISSUE=Brain; RX PubMed=10760467; DOI=10.1016/s1388-1981(00)00012-3; RA Peruzzi D., Calabrese G., Faenza I., Manzoli L., Matteucci A., RA Gianfrancesco F., Billi A.M., Stuppia L., Palka G., Cocco L.; RT "Identification and chromosomal localisation by fluorescence in situ RT hybridisation of human gene of phosphoinositide-specific phospholipase C RT beta 1."; RL Biochim. Biophys. Acta 1484:175-182(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). RC TISSUE=Brain; RX PubMed=9628581; DOI=10.1093/dnares/5.1.31; RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., RA Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. IX. The RT complete sequences of 100 new cDNA clones from brain which can code for RT large proteins in vitro."; RL DNA Res. 5:31-39(1998). RN [4] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 261-1216 (ISOFORM B). RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 417-1062 (ISOFORMS A AND B). RC TISSUE=Placenta; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [10] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=9188725; DOI=10.1021/bi9702288; RA Tall E., Dorman G., Garcia P., Runnels L., Shah S., Chen J., Profit A., RA Gu Q.M., Chaudhary A., Prestwich G.D., Rebecchi M.J.; RT "Phosphoinositide binding specificity among phospholipase C isozymes as RT determined by photo-cross-linking to novel substrate and product analogs."; RL Biochemistry 36:7239-7248(1997). RN [11] RP INTERACTION WITH DGKQ. RX PubMed=12799190; DOI=10.1016/s0014-4827(03)00115-0; RA Tabellini G., Bortul R., Santi S., Riccio M., Baldini G., Cappellini A., RA Billi A.M., Berezney R., Ruggeri A., Cocco L., Martelli A.M.; RT "Diacylglycerol kinase-theta is localized in the speckle domains of the RT nucleus."; RL Exp. Cell Res. 287:143-154(2003). RN [12] RP INVOLVEMENT IN DEE12. RX PubMed=20833646; DOI=10.1093/brain/awq238; RA Kurian M.A., Meyer E., Vassallo G., Morgan N.V., Prakash N., Pasha S., RA Hai N.A., Shuib S., Rahman F., Wassmer E., Cross J.H., O'Callaghan F.J., RA Osborne J.P., Scheffer I.E., Gissen P., Maher E.R.; RT "Phospholipase C beta 1 deficiency is associated with early-onset epileptic RT encephalopathy."; RL Brain 133:2964-2970(2010). RN [13] RP VARIANT [LARGE SCALE ANALYSIS] PRO-907. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). 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 (PubMed:9188725). Regulates the function of the CC endothelial barrier. {ECO:0000250|UniProtKB:Q9Z1B3, CC ECO:0000269|PubMed:9188725}. 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:9188725}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180; CC Evidence={ECO:0000305|PubMed:9188725}; 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:P10687}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43485; CC Evidence={ECO:0000250|UniProtKB:P10687}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC -!- SUBUNIT: Interacts with DGKQ. {ECO:0000269|PubMed:12799190}. CC -!- INTERACTION: CC Q9NQ66; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-3396023, EBI-742887; CC Q9NQ66; Q13363-2: CTBP1; NbExp=3; IntAct=EBI-3396023, EBI-10171858; CC Q9NQ66; P56545: CTBP2; NbExp=3; IntAct=EBI-3396023, EBI-741533; CC Q9NQ66; P56545-3: CTBP2; NbExp=3; IntAct=EBI-3396023, EBI-10171902; CC Q9NQ66; Q12800: TFCP2; NbExp=3; IntAct=EBI-3396023, EBI-717422; CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250|UniProtKB:Q9Z1B3}. CC Cytoplasm {ECO:0000250|UniProtKB:P10687}. Note=Colocalizes with the CC adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of CC cardiac myocytes. {ECO:0000250|UniProtKB:Q9Z1B3}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=A; CC IsoId=Q9NQ66-1; Sequence=Displayed; CC Name=B; CC IsoId=Q9NQ66-2; Sequence=VSP_004718; 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 -!- DISEASE: Developmental and epileptic encephalopathy 12 (DEE12) CC [MIM:613722]: A form of epilepsy characterized by frequent tonic CC seizures or spasms beginning in infancy with a specific EEG finding of CC suppression-burst patterns, characterized by high-voltage bursts CC alternating with almost flat suppression phases. Patients may progress CC to West syndrome, which is characterized by tonic spasms with CC clustering, arrest of psychomotor development, and hypsarrhythmia on CC EEG. {ECO:0000269|PubMed:20833646}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- MISCELLANEOUS: The receptor-mediated activation of PLC-beta-1 is CC mediated by two G-protein alpha subunits, alpha-Q and alpha-11. CC -!- SEQUENCE CAUTION: CC Sequence=BAA25507.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB14641.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/41742/PLCB1"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ278313; CAB98142.1; -; mRNA. DR EMBL; AJ278314; CAB98143.1; -; mRNA. DR EMBL; AY004175; AAF86613.1; -; mRNA. DR EMBL; AB011153; BAA25507.3; ALT_INIT; mRNA. DR EMBL; AL031683; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL034551; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL049593; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL049632; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL050315; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL050323; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471133; EAX10372.1; -; Genomic_DNA. DR EMBL; CH471133; EAX10373.1; -; Genomic_DNA. DR EMBL; CH471133; EAX10374.1; -; Genomic_DNA. DR EMBL; CH471133; EAX10376.1; -; Genomic_DNA. DR EMBL; BC069420; AAH69420.1; -; mRNA. DR EMBL; BC117231; AAI17232.1; -; mRNA. DR EMBL; AL137267; CAB70666.1; -; mRNA. DR EMBL; AK023689; BAB14641.1; ALT_INIT; mRNA. DR CCDS; CCDS13102.1; -. [Q9NQ66-1] DR CCDS; CCDS13103.1; -. [Q9NQ66-2] DR RefSeq; NP_056007.1; NM_015192.3. [Q9NQ66-1] DR RefSeq; NP_877398.1; NM_182734.2. [Q9NQ66-2] DR AlphaFoldDB; Q9NQ66; -. DR SMR; Q9NQ66; -. DR BioGRID; 116841; 51. DR CORUM; Q9NQ66; -. DR IntAct; Q9NQ66; 18. DR MINT; Q9NQ66; -. DR STRING; 9606.ENSP00000338185; -. DR BindingDB; Q9NQ66; -. DR ChEMBL; CHEMBL4034; -. DR SwissLipids; SLP:000000662; -. DR MoonProt; Q9NQ66; -. DR GlyGen; Q9NQ66; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; Q9NQ66; -. DR PhosphoSitePlus; Q9NQ66; -. DR SwissPalm; Q9NQ66; -. DR BioMuta; PLCB1; -. DR DMDM; 12643814; -. DR EPD; Q9NQ66; -. DR jPOST; Q9NQ66; -. DR MassIVE; Q9NQ66; -. DR MaxQB; Q9NQ66; -. DR PaxDb; 9606-ENSP00000338185; -. DR PeptideAtlas; Q9NQ66; -. DR ProteomicsDB; 82087; -. [Q9NQ66-1] DR ProteomicsDB; 82088; -. [Q9NQ66-2] DR Pumba; Q9NQ66; -. DR Antibodypedia; 3795; 319 antibodies from 36 providers. DR DNASU; 23236; -. DR Ensembl; ENST00000338037.11; ENSP00000338185.6; ENSG00000182621.19. [Q9NQ66-1] DR Ensembl; ENST00000378637.6; ENSP00000367904.2; ENSG00000182621.19. [Q9NQ66-2] DR Ensembl; ENST00000378641.7; ENSP00000367908.3; ENSG00000182621.19. [Q9NQ66-2] DR GeneID; 23236; -. DR KEGG; hsa:23236; -. DR MANE-Select; ENST00000338037.11; ENSP00000338185.6; NM_015192.4; NP_056007.1. DR UCSC; uc002wna.5; human. [Q9NQ66-1] DR AGR; HGNC:15917; -. DR CTD; 23236; -. DR DisGeNET; 23236; -. DR GeneCards; PLCB1; -. DR HGNC; HGNC:15917; PLCB1. DR HPA; ENSG00000182621; Tissue enhanced (brain). DR MalaCards; PLCB1; -. DR MIM; 607120; gene. DR MIM; 613722; phenotype. DR neXtProt; NX_Q9NQ66; -. DR OpenTargets; ENSG00000182621; -. DR Orphanet; 3451; Infantile spasms syndrome. DR Orphanet; 293181; Malignant migrating focal seizures of infancy. DR PharmGKB; PA33384; -. DR VEuPathDB; HostDB:ENSG00000182621; -. DR eggNOG; KOG1265; Eukaryota. DR GeneTree; ENSGT00940000155428; -. DR InParanoid; Q9NQ66; -. DR OMA; GKVNHKP; -. DR OrthoDB; 2900494at2759; -. DR PhylomeDB; Q9NQ66; -. DR TreeFam; TF313216; -. DR BioCyc; MetaCyc:HS11935-MONOMER; -. DR BRENDA; 3.1.4.11; 2681. DR PathwayCommons; Q9NQ66; -. DR Reactome; R-HSA-112043; PLC beta mediated events. DR Reactome; R-HSA-1855204; Synthesis of IP3 and IP4 in the cytosol. DR Reactome; R-HSA-399997; Acetylcholine regulates insulin secretion. DR Reactome; R-HSA-4086398; Ca2+ pathway. DR Reactome; R-HSA-416476; G alpha (q) signalling events. DR Reactome; R-HSA-418217; G beta:gamma signalling through PLC beta. DR Reactome; R-HSA-434316; Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion. DR Reactome; R-HSA-500657; Presynaptic function of Kainate receptors. DR SignaLink; Q9NQ66; -. DR SIGNOR; Q9NQ66; -. DR BioGRID-ORCS; 23236; 12 hits in 1160 CRISPR screens. DR ChiTaRS; PLCB1; human. DR GeneWiki; PLCB1; -. DR GenomeRNAi; 23236; -. DR Pharos; Q9NQ66; Tbio. DR PRO; PR:Q9NQ66; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; Q9NQ66; Protein. DR Bgee; ENSG00000182621; Expressed in endothelial cell and 197 other cell types or tissues. DR ExpressionAtlas; Q9NQ66; baseline and differential. DR GO; GO:0000785; C:chromatin; ISS:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016607; C:nuclear speck; IDA:BHF-UCL. DR GO; GO:0005634; C:nucleus; NAS:UniProtKB. DR GO; GO:0099524; C:postsynaptic cytosol; IEA:Ensembl. DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl. DR GO; GO:0005516; F:calmodulin binding; IDA:BHF-UCL. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0005096; F:GTPase activator activity; IDA:BHF-UCL. DR GO; GO:0042802; F:identical protein binding; ISS:BHF-UCL. DR GO; GO:0005521; F:lamin binding; IEA:Ensembl. DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IDA:UniProtKB. DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:BHF-UCL. DR GO; GO:0004629; F:phospholipase C activity; TAS:Reactome. DR GO; GO:0060466; P:activation of meiosis involved in egg activation; ISS:BHF-UCL. DR GO; GO:1902618; P:cellular response to fluoride; IEA:Ensembl. DR GO; GO:1905631; P:cellular response to glyceraldehyde; IEA:Ensembl. DR GO; GO:1904637; P:cellular response to ionomycin; IEA:Ensembl. DR GO; GO:1904117; P:cellular response to vasopressin; IEA:Ensembl. DR GO; GO:0021987; P:cerebral cortex development; ISS:BHF-UCL. DR GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl. DR GO; GO:0007213; P:G protein-coupled acetylcholine receptor signaling pathway; ISS:BHF-UCL. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:Reactome. DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISS:BHF-UCL. DR GO; GO:0007215; P:glutamate receptor signaling pathway; ISS:BHF-UCL. DR GO; GO:0032957; P:inositol trisphosphate metabolic process; IEA:Ensembl. 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; IDA:BHF-UCL. DR GO; GO:0035722; P:interleukin-12-mediated signaling pathway; IDA:BHF-UCL. DR GO; GO:0035723; P:interleukin-15-mediated signaling pathway; IDA:BHF-UCL. DR GO; GO:0099105; P:ion channel modulating, G protein-coupled receptor signaling pathway; IEA:Ensembl. DR GO; GO:0007612; P:learning; IEA:Ensembl. DR GO; GO:1990806; P:ligand-gated ion channel signaling pathway; IEA:Ensembl. DR GO; GO:0007613; P:memory; ISS:BHF-UCL. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:BHF-UCL. DR GO; GO:2000438; P:negative regulation of monocyte extravasation; ISS:BHF-UCL. DR GO; GO:0031161; P:phosphatidylinositol catabolic process; IEA:Ensembl. DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IDA:UniProtKB. DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central. DR GO; GO:0007207; P:phospholipase C-activating G protein-coupled acetylcholine receptor signaling pathway; IEA:Ensembl. DR GO; GO:2000344; P:positive regulation of acrosome reaction; ISS:BHF-UCL. 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:0045893; P:positive regulation of DNA-templated transcription; ISS:BHF-UCL. DR GO; GO:0040019; P:positive regulation of embryonic development; ISS:BHF-UCL. DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISS:BHF-UCL. DR GO; GO:0032024; P:positive regulation of insulin secretion; IEA:Ensembl. DR GO; GO:0032735; P:positive regulation of interleukin-12 production; ISS:BHF-UCL. DR GO; GO:0046330; P:positive regulation of JNK cascade; IDA:BHF-UCL. DR GO; GO:0045663; P:positive regulation of myoblast differentiation; ISS:BHF-UCL. DR GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; IEA:Ensembl. DR GO; GO:1903140; P:regulation of establishment of endothelial barrier; IEA:Ensembl. DR GO; GO:0080154; P:regulation of fertilization; ISS:BHF-UCL. 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; IEA:Ensembl. DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IBA:GO_Central. DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB. DR CDD; cd00275; C2_PLC_like; 1. DR CDD; cd16208; EFh_PI-PLCbeta1; 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; IPR028400; PLC-beta1_EF. 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:SF12; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE BETA-1; 1. DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 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; 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. DR Genevisible; Q9NQ66; HS. PE 1: Evidence at protein level; KW Alternative splicing; Calcium; Cytoplasm; Epilepsy; Hydrolase; KW Lipid degradation; Lipid metabolism; Lipoprotein; Membrane; Nucleus; KW Palmitate; Phosphoprotein; Reference proteome; Transducer. FT CHAIN 1..1216 FT /note="1-phosphatidylinositol 4,5-bisphosphate FT phosphodiesterase beta-1" FT /id="PRO_0000088486" 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..786 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 963..994 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1071..1095 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1173..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 851..883 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 963..982 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1178..1194 FT /note="Polar 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:0000250|UniProtKB:Q9Z1B3" 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 1199 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Z1B3" FT MOD_RES 1200 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Z1B3" FT LIPID 17 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250|UniProtKB:Q9Z1B3" FT VAR_SEQ 1142..1216 FT /note="LQVELEQEYQDKFKRLPLEILEFVQEAMKGKISEDSNHGSAPLSLSSDPGKV FT NHKTPSSEELGGDIPGKEFDTPL -> GEGSSSFLSETCHEDPSVSPNFTPPNPQALKW FT (in isoform B)" FT /evidence="ECO:0000303|PubMed:11118617, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:17974005" FT /id="VSP_004718" FT VARIANT 854 FT /note="E -> K (in dbSNP:rs1227346164)" FT /id="VAR_050541" FT VARIANT 907 FT /note="A -> P (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036547" FT CONFLICT 1..34 FT /note="MAGAQPGVHALQLKPVCVSDSLKKGTKFVKWDDD -> MGSLQGIATKILIR FT ILSDALIRKETDLKS (in Ref. 2; AAF86613)" FT /evidence="ECO:0000305" FT CONFLICT 189 FT /note="L -> M (in Ref. 2; AAF86613)" FT /evidence="ECO:0000305" FT CONFLICT 203 FT /note="P -> L (in Ref. 2; AAF86613)" FT /evidence="ECO:0000305" FT CONFLICT 216 FT /note="L -> F (in Ref. 2; AAF86613)" FT /evidence="ECO:0000305" FT CONFLICT 221 FT /note="P -> L (in Ref. 2; AAF86613)" FT /evidence="ECO:0000305" FT CONFLICT 266 FT /note="L -> P (in Ref. 2; AAF86613)" FT /evidence="ECO:0000305" FT CONFLICT 309 FT /note="P -> T (in Ref. 2; AAF86613)" FT /evidence="ECO:0000305" FT CONFLICT 320 FT /note="Q -> R (in Ref. 2; AAF86613)" FT /evidence="ECO:0000305" FT CONFLICT 352 FT /note="V -> A (in Ref. 2; AAF86613)" FT /evidence="ECO:0000305" FT CONFLICT 366 FT /note="K -> R (in Ref. 2; AAF86613)" FT /evidence="ECO:0000305" FT CONFLICT 393 FT /note="E -> K (in Ref. 2; AAF86613)" FT /evidence="ECO:0000305" FT CONFLICT 983 FT /note="P -> S (in Ref. 1; CAB98143)" FT /evidence="ECO:0000305" SQ SEQUENCE 1216 AA; 138567 MW; 6F4263D1A50C6FD1 CRC64; MAGAQPGVHA LQLKPVCVSD SLKKGTKFVK WDDDSTIVTP IILRTDPQGF FFYWTDQNKE TELLDLSLVK DARCGRHAKA PKDPKLRELL DVGNIGRLEQ RMITVVYGPD LVNISHLNLV AFQEEVAKEW TNEVFSLATN LLAQNMSRDA FLEKAYTKLK LQVTPEGRIP LKNIYRLFSA DRKRVETALE ACSLPSSRND SIPQEDFTPE VYRVFLNNLC PRPEIDNIFS EFGAKSKPYL TVDQMMDFIN LKQRDPRLNE ILYPPLKQEQ VQVLIEKYEP NNSLARKGQI SVDGFMRYLS GEENGVVSPE KLDLNEDMSQ PLSHYFINSS HNTYLTAGQL AGNSSVEMYR QVLLSGCRCV ELDCWKGRTA EEEPVITHGF TMTTEISFKE VIEAIAECAF KTSPFPILLS FENHVDSPKQ QAKMAEYCRL IFGDALLMEP LEKYPLESGV PLPSPMDLMY KILVKNKKKS HKSSEGSGKK KLSEQASNTY SDSSSMFEPS SPGAGEADTE SDDDDDDDDC KKSSMDEGTA GSEAMATEEM SNLVNYIQPV KFESFEISKK RNKSFEMSSF VETKGLEQLT KSPVEFVEYN KMQLSRIYPK GTRVDSSNYM PQLFWNAGCQ MVALNFQTMD LAMQINMGMY EYNGKSGYRL KPEFMRRPDK HFDPFTEGIV DGIVANTLSV KIISGQFLSD KKVGTYVEVD MFGLPVDTRR KAFKTKTSQG NAVNPVWEEE PIVFKKVVLP TLACLRIAVY EEGGKFIGHR ILPVQAIRPG YHYICLRNER NQPLTLPAVF VYIEVKDYVP DTYADVIEAL SNPIRYVNLM EQRAKQLAAL TLEDEEEVKK EADPGETPSE APSEARTTPA ENGVNHTTTL TPKPPSQALH SQPAPGSVKA PAKTEDLIQS VLTEVEAQTI EELKQQKSFV KLQKKHYKEM KDLVKRHHKK TTDLIKEHTT KYNEIQNDYL RRRAALEKSA KKDSKKKSEP SSPDHGSSTI EQDLAALDAE MTQKLIDLKD KQQQQLLNLR QEQYYSEKYQ KREHIKLLIQ KLTDVAEECQ NNQLKKLKEI CEKEKKELKK KMDKKRQEKI TEAKSKDKSQ MEEEKTEMIR SYIQEVVQYI KRLEEAQSKR QEKLVEKHKE IRQQILDEKP KLQVELEQEY QDKFKRLPLE ILEFVQEAMK GKISEDSNHG SAPLSLSSDP GKVNHKTPSS EELGGDIPGK EFDTPL //