ID PLCB1_MOUSE Reviewed; 1216 AA. AC Q9Z1B3; Q62075; Q6PDH1; Q8K5A5; Q8K5A6; Q9Z0E5; Q9Z2T5; DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 27-MAR-2024, entry version 201. DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 {ECO:0000305}; DE EC=3.1.4.11 {ECO:0000250|UniProtKB:Q9NQ66}; DE AltName: Full=PLC-154; DE AltName: Full=Phosphoinositide phospholipase C-beta-1; DE AltName: Full=Phospholipase C-beta-1; DE Short=PLC-beta-1; GN Name=Plcb1 {ECO:0000312|MGI:MGI:97613}; Synonyms=Plcb; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B). RC STRAIN=SWR/J; RA Bai J., Wu K., Marks D.L., Machamer C., Pagano R.E.; RT "Cloning of PI-specific phospholipase C's from 3T3 cells. Expression and RT membrane targeting of a novel phospholipase C-beta-1 isoform."; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C). RC STRAIN=ILS, and ISS; RX PubMed=11471062; DOI=10.1007/s00335-001-1001-x; RA Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., RA Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.; RT "High-throughput sequence identification of gene coding variants within RT alcohol-related QTLs."; RL Mamm. Genome 12:657-663(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). RC STRAIN=C57BL/6J; 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 29-145. RC STRAIN=C57BL/6J; RX PubMed=9753089; DOI=10.1046/j.1460-9568.1998.00213.x; RA Watanabe M., Nakamura M., Sato K., Kano M., Simon M.I., Inoue Y.; RT "Patterns of expression for the mRNA corresponding to the four isoforms of RT phospholipase Cbeta in mouse brain."; RL Eur. J. Neurosci. 10:2016-2025(1998). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 428-615. RC TISSUE=Oocyte; RX PubMed=8687404; DOI=10.1042/bj3160583; RA Dupont G., McGuinness O.M., Johnson M.H., Berridge M.J., Borgese F.; RT "Phospholipase C in mouse oocytes: characterization of beta and gamma RT isoforms and their possible involvement in sperm-induced Ca2+ spiking."; RL Biochem. J. 316:583-591(1996). RN [7] RP SUBCELLULAR LOCATION. RX PubMed=18802028; DOI=10.1161/circresaha.108.176024; RA Wright C.D., Chen Q., Baye N.L., Huang Y., Healy C.L., Kasinathan S., RA O'Connell T.D.; RT "Nuclear alpha1-adrenergic receptors signal activated ERK localization to RT caveolae in adult cardiac myocytes."; RL Circ. Res. 103:992-1000(2008). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236; SER-417; THR-509; RP SER-511; SER-582; SER-978; SER-987; SER-1197; SER-1199 AND SER-1200, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, and Pancreas; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [9] RP FUNCTION, AND PALMITOYLATION AT CYS-17 BY ZDHHC21. RX PubMed=27653213; DOI=10.1038/ncomms12823; RA Beard R.S. Jr., Yang X., Meegan J.E., Overstreet J.W., Yang C.G., RA Elliott J.A., Reynolds J.J., Cha B.J., Pivetti C.D., Mitchell D.A., RA Wu M.H., Deschenes R.J., Yuan S.Y.; RT "Palmitoyl acyltransferase DHHC21 mediates endothelial dysfunction in RT systemic inflammatory response syndrome."; RL Nat. Commun. 7:12823-12823(2016). 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:27653213). Regulates the function of the CC endothelial barrier (PubMed:27653213). {ECO:0000269|PubMed:27653213, CC ECO:0000303|PubMed:27653213}. 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:Q9NQ66}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180; CC Evidence={ECO:0000250|UniProtKB:Q9NQ66}; 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; Evidence={ECO:0000250}; CC -!- SUBUNIT: Interacts with DGKQ. {ECO:0000250|UniProtKB:Q9NQ66}. CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:18802028}. 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:0000269|PubMed:18802028}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=A; Synonyms=C-beta-1a; CC IsoId=Q9Z1B3-1; Sequence=Displayed; CC Name=B; Synonyms=C-beta-1b; CC IsoId=Q9Z1B3-2; Sequence=VSP_008917; CC Name=C; CC IsoId=Q9Z1B3-3; Sequence=VSP_008918; CC -!- PTM: Palmitoylated (PubMed:27653213). Palmitoylation at Cys-17 by CC ZDHHC21 regulates the signaling activity of PLCB1 and the function of CC the endothelial barrier (Probable). Palmitoylation by ZDHHC21 is CC stimulated by inflammation (PubMed:27653213). CC {ECO:0000269|PubMed:27653213, ECO:0000305|PubMed:27653213}. 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 --------------------------------------------------------------------------- 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; U85712; AAD00571.1; -; mRNA. DR EMBL; U85713; AAD00572.1; -; mRNA. DR EMBL; U85714; AAD00573.1; -; mRNA. DR EMBL; AF498249; AAM22966.1; -; mRNA. DR EMBL; AF498250; AAM22967.1; -; mRNA. DR EMBL; AL840635; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL928635; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL928956; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL935278; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC058710; AAH58710.1; -; mRNA. DR EMBL; AF022801; AAD01749.1; -; mRNA. DR EMBL; X95344; CAA64637.1; -; mRNA. DR CCDS; CCDS16787.1; -. [Q9Z1B3-2] DR CCDS; CCDS50729.1; -. [Q9Z1B3-1] DR PIR; S68256; S68256. DR RefSeq; NP_001139302.1; NM_001145830.1. [Q9Z1B3-1] DR RefSeq; NP_062651.2; NM_019677.2. [Q9Z1B3-2] DR AlphaFoldDB; Q9Z1B3; -. DR SMR; Q9Z1B3; -. DR BioGRID; 202232; 11. DR IntAct; Q9Z1B3; 5. DR MINT; Q9Z1B3; -. DR STRING; 10090.ENSMUSP00000105743; -. DR GlyGen; Q9Z1B3; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9Z1B3; -. DR PhosphoSitePlus; Q9Z1B3; -. DR SwissPalm; Q9Z1B3; -. DR MaxQB; Q9Z1B3; -. DR PaxDb; 10090-ENSMUSP00000105743; -. DR PeptideAtlas; Q9Z1B3; -. DR ProteomicsDB; 289918; -. [Q9Z1B3-1] DR ProteomicsDB; 289919; -. [Q9Z1B3-2] DR ProteomicsDB; 289920; -. [Q9Z1B3-3] DR Pumba; Q9Z1B3; -. DR Antibodypedia; 3795; 319 antibodies from 36 providers. DR DNASU; 18795; -. DR Ensembl; ENSMUST00000070724.12; ENSMUSP00000064844.6; ENSMUSG00000051177.17. [Q9Z1B3-2] DR Ensembl; ENSMUST00000110116.8; ENSMUSP00000105743.2; ENSMUSG00000051177.17. [Q9Z1B3-1] DR Ensembl; ENSMUST00000131552.5; ENSMUSP00000118756.3; ENSMUSG00000051177.17. [Q9Z1B3-2] DR GeneID; 18795; -. DR KEGG; mmu:18795; -. DR UCSC; uc008mnx.2; mouse. [Q9Z1B3-2] DR UCSC; uc008mny.2; mouse. [Q9Z1B3-1] DR AGR; MGI:97613; -. DR CTD; 23236; -. DR MGI; MGI:97613; Plcb1. DR VEuPathDB; HostDB:ENSMUSG00000051177; -. DR eggNOG; KOG1265; Eukaryota. DR GeneTree; ENSGT00940000155428; -. DR InParanoid; Q9Z1B3; -. DR OMA; GKVNHKP; -. DR OrthoDB; 2900494at2759; -. DR PhylomeDB; Q9Z1B3; -. DR TreeFam; TF313216; -. DR BRENDA; 3.1.4.11; 3474. DR Reactome; R-MMU-112043; PLC beta mediated events. DR Reactome; R-MMU-1855204; Synthesis of IP3 and IP4 in the cytosol. DR Reactome; R-MMU-399997; Acetylcholine regulates insulin secretion. DR Reactome; R-MMU-4086398; Ca2+ pathway. DR Reactome; R-MMU-416476; G alpha (q) signalling events. DR Reactome; R-MMU-418217; G beta:gamma signalling through PLC beta. DR Reactome; R-MMU-434316; Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion. DR Reactome; R-MMU-500657; Presynaptic function of Kainate receptors. DR BioGRID-ORCS; 18795; 3 hits in 79 CRISPR screens. DR ChiTaRS; Plcb1; mouse. DR PRO; PR:Q9Z1B3; -. DR Proteomes; UP000000589; Chromosome 2. DR RNAct; Q9Z1B3; Protein. DR Bgee; ENSMUSG00000051177; Expressed in caudate-putamen and 241 other cell types or tissues. DR ExpressionAtlas; Q9Z1B3; baseline and differential. DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL. DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO. DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO. DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB. 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; IDA:BHF-UCL. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0099524; C:postsynaptic cytosol; IDA:SynGO. DR GO; GO:0032991; C:protein-containing complex; IDA:MGI. DR GO; GO:0005509; F:calcium ion binding; ISO:MGI. DR GO; GO:0005516; F:calmodulin binding; ISS:BHF-UCL. DR GO; GO:0019899; F:enzyme binding; ISS:BHF-UCL. DR GO; GO:0005096; F:GTPase activator activity; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; ISS:BHF-UCL. DR GO; GO:0005521; F:lamin binding; IPI:BHF-UCL. DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IDA:BHF-UCL. DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:BHF-UCL. DR GO; GO:0060466; P:activation of meiosis involved in egg activation; IDA:BHF-UCL. DR GO; GO:0007420; P:brain development; NAS:BHF-UCL. DR GO; GO:0007155; P:cell adhesion; IC:BHF-UCL. DR GO; GO:1902618; P:cellular response to fluoride; ISO:MGI. DR GO; GO:1905631; P:cellular response to glyceraldehyde; ISO:MGI. DR GO; GO:1904637; P:cellular response to ionomycin; ISO:MGI. DR GO; GO:1904117; P:cellular response to vasopressin; ISO:MGI. DR GO; GO:0021987; P:cerebral cortex development; IMP:BHF-UCL. DR GO; GO:0030218; P:erythrocyte differentiation; TAS:BHF-UCL. DR GO; GO:0045444; P:fat cell differentiation; IDA:BHF-UCL. DR GO; GO:0007213; P:G protein-coupled acetylcholine receptor signaling pathway; IMP:BHF-UCL. DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IDA:BHF-UCL. DR GO; GO:0007215; P:glutamate receptor signaling pathway; IMP:BHF-UCL. DR GO; GO:0032957; P:inositol trisphosphate metabolic process; ISO:MGI. DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:BHF-UCL. DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IDA:BHF-UCL. DR GO; GO:0070498; P:interleukin-1-mediated signaling pathway; ISO:MGI. DR GO; GO:0035722; P:interleukin-12-mediated signaling pathway; ISS:BHF-UCL. DR GO; GO:0035723; P:interleukin-15-mediated signaling pathway; ISS:BHF-UCL. DR GO; GO:0099105; P:ion channel modulating, G protein-coupled receptor signaling pathway; IMP:MGI. DR GO; GO:0007612; P:learning; IEA:Ensembl. DR GO; GO:1990806; P:ligand-gated ion channel signaling pathway; IMP:MGI. DR GO; GO:0030225; P:macrophage differentiation; NAS:BHF-UCL. DR GO; GO:0007613; P:memory; IMP:BHF-UCL. DR GO; GO:0006397; P:mRNA processing; TAS:BHF-UCL. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:BHF-UCL. DR GO; GO:2000438; P:negative regulation of monocyte extravasation; IDA:BHF-UCL. DR GO; GO:0001556; P:oocyte maturation; NAS:BHF-UCL. DR GO; GO:0031161; P:phosphatidylinositol catabolic process; ISO:MGI. DR GO; GO:0046488; P:phosphatidylinositol metabolic process; ISS: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; IMP:MGI. DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IMP:MGI. DR GO; GO:2000344; P:positive regulation of acrosome reaction; IMP:BHF-UCL. DR GO; GO:2000560; P:positive regulation of CD24 production; IDA:BHF-UCL. DR GO; GO:0048639; P:positive regulation of developmental growth; IMP:BHF-UCL. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:BHF-UCL. DR GO; GO:0040019; P:positive regulation of embryonic development; IMP:BHF-UCL. DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IDA:BHF-UCL. DR GO; GO:0032024; P:positive regulation of insulin secretion; IMP:MGI. DR GO; GO:0032735; P:positive regulation of interleukin-12 production; IMP:BHF-UCL. DR GO; GO:0046330; P:positive regulation of JNK cascade; ISS:BHF-UCL. DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IDA:BHF-UCL. DR GO; GO:0032417; P:positive regulation of sodium:proton antiporter activity; NAS:BHF-UCL. DR GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; IDA:SynGO. DR GO; GO:1903140; P:regulation of establishment of endothelial barrier; IMP:UniProtKB. DR GO; GO:0080154; P:regulation of fertilization; IMP:BHF-UCL. DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IMP:BHF-UCL. DR GO; GO:0099178; P:regulation of retrograde trans-synaptic signaling by endocanabinoid; IDA:SynGO. DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IBA:GO_Central. DR GO; GO:0034284; P:response to monosaccharide; ISO:MGI. DR GO; GO:0043434; P:response to peptide hormone; ISO:MGI. DR GO; GO:0007165; P:signal transduction; TAS:BHF-UCL. 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; Q9Z1B3; MM. PE 1: Evidence at protein level; KW Alternative splicing; Calcium; Cytoplasm; Hydrolase; Lipid degradation; KW Lipid metabolism; Lipoprotein; Membrane; Nucleus; Palmitate; KW Phosphoprotein; Reference proteome; Transducer. FT CHAIN 1..1216 FT /note="1-phosphatidylinositol 4,5-bisphosphate FT phosphodiesterase beta-1" FT /id="PRO_0000088487" 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 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 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 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 COMPBIAS 1198..1216 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:0007744|PubMed:21183079" FT MOD_RES 417 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 509 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 511 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 582 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" 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:0007744|PubMed:21183079" FT MOD_RES 987 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1197 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1199 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1200 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT LIPID 17 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000269|PubMed:27653213" FT VAR_SEQ 1142..1216 FT /note="LQTELEQEYQDKFKRLPLEILEFVQEAMKGKISEDSNHGSAPPSLASDAAKV FT NLKSPSSEEIERENPGREFDTPL -> GEGPSSVLSEGCHEDPSVPPNFTPPNPQALKW FT (in isoform B)" FT /evidence="ECO:0000303|Ref.1" FT /id="VSP_008917" FT VAR_SEQ 1199..1216 FT /note="Missing (in isoform C)" FT /evidence="ECO:0000303|PubMed:11471062" FT /id="VSP_008918" FT CONFLICT 28 FT /note="F -> L (in Ref. 1; AAD00571/AAD00572/AAD00573)" FT /evidence="ECO:0000305" FT CONFLICT 41 FT /note="I -> T (in Ref. 1; AAD00571/AAD00572/AAD00573)" FT /evidence="ECO:0000305" FT CONFLICT 67 FT /note="S -> T (in Ref. 5; AAD01749)" FT /evidence="ECO:0000305" FT CONFLICT 79 FT /note="K -> E (in Ref. 1; AAD00571/AAD00572/AAD00573)" FT /evidence="ECO:0000305" FT CONFLICT 112 FT /note="V -> A (in Ref. 1; AAD00571/AAD00572/AAD00573)" FT /evidence="ECO:0000305" FT CONFLICT 561 FT /note="R -> I (in Ref. 6; CAA64637)" FT /evidence="ECO:0000305" FT CONFLICT 613 FT /note="L -> I (in Ref. 6; CAA64637)" FT /evidence="ECO:0000305" FT CONFLICT 622 FT /note="V -> M (in Ref. 1; AAD00571/AAD00572/AAD00573)" FT /evidence="ECO:0000305" FT CONFLICT 714 FT /note="K -> T (in Ref. 1; AAD00571/AAD00572/AAD00573)" FT /evidence="ECO:0000305" FT CONFLICT 795 FT /note="V -> D (in Ref. 1; AAD00571/AAD00572/AAD00573)" FT /evidence="ECO:0000305" FT CONFLICT 923 FT /note="Q -> H (in Ref. 1; AAD00571/AAD00572/AAD00573)" FT /evidence="ECO:0000305" FT CONFLICT 957 FT /note="N -> I (in Ref. 1; AAD00571/AAD00572/AAD00573)" FT /evidence="ECO:0000305" FT CONFLICT 1084 FT /note="K -> T (in Ref. 1; AAD00571/AAD00572/AAD00573)" FT /evidence="ECO:0000305" SQ SEQUENCE 1216 AA; 138396 MW; CC751D49895A47D0 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 KFESFEISKK RNKSFEMSSF VETKGLEQLT KSPVEFVEYN KMQLSRIYPK GTRVDSSNYM PQLFWNAGCQ MVALNFQTVD LAMQINMGMY EYNGKSGYRL KPEFMRRPDK HFDPFTEGIV DGIVANTLSV KIISGQFLSD KKVGTYVEVD MFGLPVDTRR KAFKTKTSQG NAVNPVWEEE PIVFKKVVLP SLACLRIAAY EEGGKFIGHR ILPVQAIRPG YHYICLRNER NQPLTLPAVF VYIEVKDYVP DTYADVIEAL SNPIRYVNLM EQRAKQLAAL TLEDEEEVKK EADPGETSSE APSETRTTPA ENGVNHTASL 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 QEKLVEKHNE IRQQILDEKP KLQTELEQEY QDKFKRLPLE ILEFVQEAMK GKISEDSNHG SAPPSLASDA AKVNLKSPSS EEIERENPGR EFDTPL //