ID  Q9NQ66;
PN  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1;
GN  PLCB1;
OS  9606;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Nucleus membrane {ECO:0000250|UniProtKB:Q9Z1B3}. Cytoplasm {ECO:0000250|UniProtKB:P10687}. Note=Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes. {ECO:0000250|UniProtKB:Q9Z1B3}.
DR  UNIPROT: Q9NQ66;
DR  UNIPROT: D3DW12;
DR  UNIPROT: D3DW13;
DR  UNIPROT: O60325;
DR  UNIPROT: Q17RQ6;
DR  UNIPROT: Q5TFF7;
DR  UNIPROT: Q5TGC9;
DR  UNIPROT: Q8IV93;
DR  UNIPROT: Q9BQW2;
DR  UNIPROT: Q9H4H2;
DR  UNIPROT: Q9H8H5;
DR  UNIPROT: Q9NQ65;
DR  UNIPROT: Q9NQH9;
DR  UNIPROT: Q9NTH4;
DR  UNIPROT: Q9UJP6;
DR  UNIPROT: Q9UM26;
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;
DR  OMIM: 607120;
DR  OMIM: 613722;
DR  DisGeNET: 23236;
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:9188725). Regulates the function of the endothelial barrier. {ECO:0000250|UniProtKB:Q9Z1B3, ECO:0000269|PubMed:9188725}.
DE  Disease: Developmental and epileptic encephalopathy 12 (DEE12) [MIM:613722]: A form of epilepsy characterized by frequent tonic seizures or spasms beginning in infancy with a specific EEG finding of suppression-burst patterns, characterized by high-voltage bursts alternating with almost flat suppression phases. Patients may progress to West syndrome, which is characterized by tonic spasms with clustering, arrest of psychomotor development, and hypsarrhythmia on EEG. {ECO:0000269|PubMed:20833646}. Note=The disease is caused by variants affecting the gene represented in this entry.
DE  Reference Proteome: Yes;
DE  Interaction: P01112; IntAct: EBI-27045317; Score: 0.27
DE  Interaction: Q01082; IntAct: EBI-3447119; Score: 0.00
DE  Interaction: P56545; IntAct: EBI-10311798; Score: 0.56
DE  Interaction: Q12800; IntAct: EBI-10311808; Score: 0.56
DE  Interaction: Q13363; IntAct: EBI-10311818; Score: 0.56
DE  Interaction: Q8TAP6; IntAct: EBI-10311838; Score: 0.56
DE  Interaction: Q7KYR7; IntAct: EBI-21541130; Score: 0.35
DE  Interaction: P43115; IntAct: EBI-21607127; Score: 0.35
DE  Interaction: Q6ZN54; IntAct: EBI-21689078; Score: 0.35
DE  Interaction: P11279; IntAct: EBI-16794808; Score: 0.27
DE  Interaction: P05067; IntAct: EBI-20821761; Score: 0.35
DE  Interaction: Q99623; IntAct: EBI-20901888; Score: 0.40
DE  Interaction: Q02539; IntAct: EBI-20928184; Score: 0.40
DE  Interaction: P04156; IntAct: EBI-21014654; Score: 0.35
DE  Interaction: Q969F8; IntAct: EBI-21282024; Score: 0.40
DE  Interaction: P01116; IntAct: EBI-27041844; Score: 0.27
DE  Interaction: P01111; IntAct: EBI-27042293; Score: 0.27
GO  GO:0000785;
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0070062;
GO  GO:0098982;
GO  GO:0098978;
GO  GO:0031965;
GO  GO:0016607;
GO  GO:0005634;
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:0004629;
GO  GO:0060466;
GO  GO:1902618;
GO  GO:1905631;
GO  GO:1904637;
GO  GO:1904117;
GO  GO:0021987;
GO  GO:0045444;
GO  GO:0007213;
GO  GO:0007186;
GO  GO:0000086;
GO  GO:0007215;
GO  GO:0032957;
GO  GO:0048009;
GO  GO:0070498;
GO  GO:0035722;
GO  GO:0035723;
GO  GO:0007612;
GO  GO:0007613;
GO  GO:0045892;
GO  GO:2000438;
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:0099170;
GO  GO:1903140;
GO  GO:0080154;
GO  GO:0008277;
GO  GO:0099178;
GO  GO:0007165;
TP  Membrane Topology: Lipid-Anchored; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q9Z1B3};
SQ  MAGAQPGVHALQLKPVCVSDSLKKGTKFVKWDDDSTIVTPIILRTDPQGFFFYWTDQNKETELLDLSLVKDARCGRHAKA
SQ  PKDPKLRELLDVGNIGRLEQRMITVVYGPDLVNISHLNLVAFQEEVAKEWTNEVFSLATNLLAQNMSRDAFLEKAYTKLK
SQ  LQVTPEGRIPLKNIYRLFSADRKRVETALEACSLPSSRNDSIPQEDFTPEVYRVFLNNLCPRPEIDNIFSEFGAKSKPYL
SQ  TVDQMMDFINLKQRDPRLNEILYPPLKQEQVQVLIEKYEPNNSLARKGQISVDGFMRYLSGEENGVVSPEKLDLNEDMSQ
SQ  PLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEAIAECAF
SQ  KTSPFPILLSFENHVDSPKQQAKMAEYCRLIFGDALLMEPLEKYPLESGVPLPSPMDLMYKILVKNKKKSHKSSEGSGKK
SQ  KLSEQASNTYSDSSSMFEPSSPGAGEADTESDDDDDDDDCKKSSMDEGTAGSEAMATEEMSNLVNYIQPVKFESFEISKK
SQ  RNKSFEMSSFVETKGLEQLTKSPVEFVEYNKMQLSRIYPKGTRVDSSNYMPQLFWNAGCQMVALNFQTMDLAMQINMGMY
SQ  EYNGKSGYRLKPEFMRRPDKHFDPFTEGIVDGIVANTLSVKIISGQFLSDKKVGTYVEVDMFGLPVDTRRKAFKTKTSQG
SQ  NAVNPVWEEEPIVFKKVVLPTLACLRIAVYEEGGKFIGHRILPVQAIRPGYHYICLRNERNQPLTLPAVFVYIEVKDYVP
SQ  DTYADVIEALSNPIRYVNLMEQRAKQLAALTLEDEEEVKKEADPGETPSEAPSEARTTPAENGVNHTTTLTPKPPSQALH
SQ  SQPAPGSVKAPAKTEDLIQSVLTEVEAQTIEELKQQKSFVKLQKKHYKEMKDLVKRHHKKTTDLIKEHTTKYNEIQNDYL
SQ  RRRAALEKSAKKDSKKKSEPSSPDHGSSTIEQDLAALDAEMTQKLIDLKDKQQQQLLNLRQEQYYSEKYQKREHIKLLIQ
SQ  KLTDVAEECQNNQLKKLKEICEKEKKELKKKMDKKRQEKITEAKSKDKSQMEEEKTEMIRSYIQEVVQYIKRLEEAQSKR
SQ  QEKLVEKHKEIRQQILDEKPKLQVELEQEYQDKFKRLPLEILEFVQEAMKGKISEDSNHGSAPLSLSSDPGKVNHKTPSS
SQ  EELGGDIPGKEFDTPL
//