ID  Q9Z1B3;
PN  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1;
GN  Plcb1;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000269|PubMed:18802028}. Cytoplasm {ECO:0000250|UniProtKB:P10687}. Note=Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes. {ECO:0000269|PubMed:18802028}.
DR  UNIPROT: Q9Z1B3;
DR  UNIPROT: Q62075;
DR  UNIPROT: Q6PDH1;
DR  UNIPROT: Q8K5A5;
DR  UNIPROT: Q8K5A6;
DR  UNIPROT: Q9Z0E5;
DR  UNIPROT: Q9Z2T5;
DR  Pfam: PF06631;
DR  Pfam: PF09279;
DR  Pfam: PF17787;
DR  Pfam: PF00388;
DR  Pfam: PF00387;
DR  Pfam: PF08703;
DR  PROSITE: PS50004;
DR  PROSITE: PS50007;
DR  PROSITE: PS50008;
DE  Function: Catalyzes the hydrolysis of 1-phosphatidylinositol 4,5- bisphosphate into diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) and mediates intracellular signaling downstream of G protein- coupled receptors (PubMed:27653213). Regulates the function of the endothelial barrier (PubMed:27653213). {ECO:0000269|PubMed:27653213, ECO:0000303|PubMed:27653213}.
DE  Reference Proteome: Yes;
DE  Interaction: P35438; IntAct: EBI-398049; Score: 0.35
DE  Interaction: P63101; IntAct: EBI-2255635; Score: 0.35
DE  Interaction: Q4ACU6; IntAct: EBI-16726570; Score: 0.53
DE  Interaction: Q6NZM9; IntAct: EBI-26472137; Score: 0.35
DE  Interaction: P16056; IntAct: EBI-27118288; Score: 0.35
GO  GO:0000785;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0098982;
GO  GO:0098978;
GO  GO:0016020;
GO  GO:0043209;
GO  GO:0031965;
GO  GO:0016607;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0098794;
GO  GO:0032991;
GO  GO:0005509;
GO  GO:0005516;
GO  GO:0019899;
GO  GO:0005096;
GO  GO:0042802;
GO  GO:0005521;
GO  GO:0004435;
GO  GO:0005546;
GO  GO:0060466;
GO  GO:0007420;
GO  GO:0007155;
GO  GO:1902618;
GO  GO:1905631;
GO  GO:1904637;
GO  GO:1904117;
GO  GO:0021987;
GO  GO:0030218;
GO  GO:0045444;
GO  GO:0007213;
GO  GO:0000086;
GO  GO:0007215;
GO  GO:0032957;
GO  GO:0008286;
GO  GO:0048009;
GO  GO:0070498;
GO  GO:0035722;
GO  GO:0035723;
GO  GO:0007612;
GO  GO:0030225;
GO  GO:0007613;
GO  GO:0006397;
GO  GO:0045892;
GO  GO:2000438;
GO  GO:0001556;
GO  GO:0031161;
GO  GO:0046488;
GO  GO:0048015;
GO  GO:2000344;
GO  GO:2000560;
GO  GO:0048639;
GO  GO:0045893;
GO  GO:0040019;
GO  GO:1900087;
GO  GO:0032735;
GO  GO:0046330;
GO  GO:0045663;
GO  GO:0032417;
GO  GO:0099170;
GO  GO:1903140;
GO  GO:0080154;
GO  GO:0008277;
GO  GO:0099178;
GO  GO:0034284;
GO  GO:0043434;
GO  GO:0007165;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:27653213};
SQ  MAGAQPGVHALQLKPVCVSDSLKKGTKFVKWDDDSTIVTPIILRTDPQGFFFYWTDQNKETELLDLSLVKDARCGKHAKA
SQ  PKDPKLRELLDVGNIGHLEQRMITVVYGPDLVNISHLNLVAFQEEVAKEWTNEVFSLATNLLAQNMSRDAFLEKAYTKLK
SQ  LQVTPEGRIPLKNIYRLFSADRKRVETALEACSLPSSRNDSIPQEDFTPDVYRVFLNNLCPRPEIDNIFSEFGAKSKPYL
SQ  TVDQMMDFINLKQRDPRLNEILYPPLKQEQVQVLIEKYEPNSSLAKKGQMSVDGFMRYLSGEENGVVSPEKLDLNEDMSQ
SQ  PLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEAIAECAF
SQ  KTSPFPILLSFENHVDSPKQQAKMAEYCRLIFGDALLMEPLEKYPLESGVPLPSPMDLMYKILVKNKKKSHKSSEGSGKK
SQ  KLSEQASNTYSDSSSVFEPSSPGAGEADTESDDDDDDDDCKKSSMDEGTAGSEAMATEEMSNLVNYIQPVKFESFEISKK
SQ  RNKSFEMSSFVETKGLEQLTKSPVEFVEYNKMQLSRIYPKGTRVDSSNYMPQLFWNAGCQMVALNFQTVDLAMQINMGMY
SQ  EYNGKSGYRLKPEFMRRPDKHFDPFTEGIVDGIVANTLSVKIISGQFLSDKKVGTYVEVDMFGLPVDTRRKAFKTKTSQG
SQ  NAVNPVWEEEPIVFKKVVLPSLACLRIAAYEEGGKFIGHRILPVQAIRPGYHYICLRNERNQPLTLPAVFVYIEVKDYVP
SQ  DTYADVIEALSNPIRYVNLMEQRAKQLAALTLEDEEEVKKEADPGETSSEAPSETRTTPAENGVNHTASLAPKPPSQAPH
SQ  SQPAPGSVKAPAKTEDLIQSVLTEVEAQTIEELKQQKSFVKLQKKHYKEMKDLVKRHHKKTTELIKEHTTKYNEIQNDYL
SQ  RRRAALEKSAKKDSKKKSEPSSPDHGSSAIEQDLAALDAEMTQKLIDLKDKQQQQLLNLRQEQYYSEKYQKREHIKLLIQ
SQ  KLTDVAEECQNNQLKKLKEICEKEKKELKKKMDKKRQEKITEAKSKDKSQMEEEKTEMIRSYIQEVVQYIKRLEEAQSKR
SQ  QEKLVEKHNEIRQQILDEKPKLQTELEQEYQDKFKRLPLEILEFVQEAMKGKISEDSNHGSAPPSLASDAAKVNLKSPSS
SQ  EEIERENPGREFDTPL
//